Complement c8. Medical search

A glycoprotein that is central in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C3 can be cleaved into COMPLEMENT C3A and COMPLEMENT C3B, spontaneously at low level or by C3 CONVERTASE at high level. The smaller fragment C3a is an ANAPHYLATOXIN and mediator of local inflammatory process. The larger fragment C3b binds with C3 convertase to form C5 convertase.

A glycoprotein that is important in the activation of CLASSICAL COMPLEMENT PATHWAY. C4 is cleaved by the activated COMPLEMENT C1S into COMPLEMENT C4A and COMPLEMENT C4B.

The smaller fragment formed when complement C4 is cleaved by COMPLEMENT C1S. It is an anaphylatoxin that causes symptoms of immediate hypersensitivity (HYPERSENSITIVITY, IMMEDIATE) but its activity is weaker than that of COMPLEMENT C3A or COMPLEMENT C5A.

The smaller fragment generated from the cleavage of complement C3 by C3 CONVERTASE. C3a, a 77-amino acid peptide, is a mediator of local inflammatory process. It induces smooth MUSCLE CONTRACTION, and HISTAMINE RELEASE from MAST CELLS and LEUKOCYTES. C3a is considered an anaphylatoxin along with COMPLEMENT C4A; COMPLEMENT C5A; and COMPLEMENT C5A, DES-ARGININE.

A subcomponent of complement C1, composed of six copies of three polypeptide chains (A, B, and C), each encoded by a separate gene (C1QA; C1QB; C1QC). This complex is arranged in nine subunits (six disulfide-linked dimers of A and B, and three disulfide-linked homodimers of C). C1q has binding sites for antibodies (the heavy chain of IMMUNOGLOBULIN G or IMMUNOGLOBULIN M). The interaction of C1q and immunoglobulin activates the two proenzymes COMPLEMENT C1R and COMPLEMENT C1S, thus initiating the cascade of COMPLEMENT ACTIVATION via the CLASSICAL COMPLEMENT PATHWAY.

The minor fragment formed when C5 convertase cleaves C5 into C5a and COMPLEMENT C5B. C5a is a 74-amino-acid glycopeptide with a carboxy-terminal ARGININE that is crucial for its spasmogenic activity. Of all the complement-derived anaphylatoxins, C5a is the most potent in mediating immediate hypersensitivity (HYPERSENSITIVITY, IMMEDIATE), smooth MUSCLE CONTRACTION; HISTAMINE RELEASE; and migration of LEUKOCYTES to site of INFLAMMATION.

The sequential activation of serum COMPLEMENT PROTEINS to create the COMPLEMENT MEMBRANE ATTACK COMPLEX. Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES.

The large fragment formed when COMPLEMENT C4 is cleaved by COMPLEMENT C1S. The membrane-bound C4b binds COMPLEMENT C2A, a SERINE PROTEASE, to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE).

C5 plays a central role in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C5 is cleaved by C5 CONVERTASE into COMPLEMENT C5A and COMPLEMENT C5B. The smaller fragment C5a is an ANAPHYLATOXIN and mediator of inflammatory process. The major fragment C5b binds to the membrane initiating the spontaneous assembly of the late complement components, C5-C9, into the MEMBRANE ATTACK COMPLEX.

The larger fragment generated from the cleavage of COMPLEMENT C3 by C3 CONVERTASE. It is a constituent of the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb), and COMPLEMENT C5 CONVERTASES in both the classical (C4b2a3b) and the alternative (C3bBb3b) pathway. C3b participates in IMMUNE ADHERENCE REACTION and enhances PHAGOCYTOSIS. It can be inactivated (iC3b) or cleaved by various proteases to yield fragments such as COMPLEMENT C3C; COMPLEMENT C3D; C3e; C3f; and C3g.

Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY).

A 105-kDa serum glycoprotein with significant homology to the other late complement components, C7-C9. It is a polypeptide chain cross-linked by 32 disulfide bonds. C6 is the next complement component to bind to the membrane-bound COMPLEMENT C5B in the assembly of MEMBRANE ATTACK COMPLEX. It is encoded by gene C6.

A 206-amino-acid fragment in the alpha chain (672-1663) of C3b. It is generated when C3b is inactivated (iC3b) and its alpha chain is cleaved by COMPLEMENT FACTOR I into C3c (749-954), and C3dg (955-1303) in the presence COMPLEMENT FACTOR H.

A 302-amino-acid fragment in the alpha chain (672-1663) of C3b. It is generated when C3b is inactivated (iC3b) and its alpha chain is cleaved by COMPLEMENT FACTOR I into C3c, and C3dg (955-1303) in the presence COMPLEMENT FACTOR H. Serum proteases further degrade C3dg into C3d (1002-1303) and C3g (955-1001).

A component of the CLASSICAL COMPLEMENT PATHWAY. C2 is cleaved by activated COMPLEMENT C1S into COMPLEMENT C2B and COMPLEMENT C2A. C2a, the COOH-terminal fragment containing a SERINE PROTEASE, combines with COMPLEMENT C4B to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE).

A 63-kDa serum glycoprotein encoded by gene C9. Monomeric C9 (mC9) binds the C5b-8 complex to form C5b-9 which catalyzes the polymerization of C9 forming C5b-p9 (MEMBRANE ATTACK COMPLEX) and transmembrane channels leading to lysis of the target cell. Patients with C9 deficiency suffer from recurrent bacterial infections.

Molecules on the surface of some B-lymphocytes and macrophages, that recognize and combine with the C3b, C3d, C1q, and C4b components of complement.

A 77-kDa subcomponent of complement C1, encoded by gene C1S, is a SERINE PROTEASE existing as a proenzyme (homodimer) in the intact complement C1 complex. Upon the binding of COMPLEMENT C1Q to antibodies, the activated COMPLEMENT C1R cleaves C1s into two chains, A (heavy) and B (light, the serine protease), linked by disulfide bonds yielding the active C1s. The activated C1s, in turn, cleaves COMPLEMENT C2 and COMPLEMENT C4 to form C4b2a (CLASSICAL C3 CONVERTASE).

A product of COMPLEMENT ACTIVATION cascade, regardless of the pathways, that forms transmembrane channels causing disruption of the target CELL MEMBRANE and cell lysis. It is formed by the sequential assembly of terminal complement components (COMPLEMENT C5B; COMPLEMENT C6; COMPLEMENT C7; COMPLEMENT C8; and COMPLEMENT C9) into the target membrane. The resultant C5b-8-poly-C9 is the "membrane attack complex" or MAC.

A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.

Serum proteins that negatively regulate the cascade process of COMPLEMENT ACTIVATION. Uncontrolled complement activation and resulting cell lysis is potentially dangerous for the host. The complement system is tightly regulated by inactivators that accelerate the decay of intermediates and certain cell surface receptors.

A 93-kDa serum glycoprotein encoded by C7 gene. It is a polypeptide chain with 28 disulfide bridges. In the formation of MEMBRANE ATTACK COMPLEX; C7 is the next component to bind the C5b-6 complex forming a trimolecular complex C5b-7 which is lipophilic, resembles an integral membrane protein, and serves as an anchor for the late complement components, C8 and C9.

Serine proteases that cleave COMPLEMENT C3 into COMPLEMENT C3A and COMPLEMENT C3B, or cleave COMPLEMENT C5 into COMPLEMENT C5A and COMPLEMENT C5B. These include the different forms of C3/C5 convertases in the classical and the alternative pathways of COMPLEMENT ACTIVATION. Both cleavages take place at the C-terminal of an ARGININE residue.

A glycine-rich, heat-labile serum glycoprotein that contains a component of the C3 CONVERTASE ALTERNATE PATHWAY (C3bBb). Bb, a serine protease, is generated when factor B is cleaved by COMPLEMENT FACTOR D into Ba and Bb.

Complement activation initiated by the interaction of microbial ANTIGENS with COMPLEMENT C3B. When COMPLEMENT FACTOR B binds to the membrane-bound C3b, COMPLEMENT FACTOR D cleaves it to form alternative C3 CONVERTASE (C3BBB) which, stabilized by COMPLEMENT FACTOR P, is able to cleave multiple COMPLEMENT C3 to form alternative C5 CONVERTASE (C3BBB3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.

Complement activation initiated by the binding of COMPLEMENT C1 to ANTIGEN-ANTIBODY COMPLEXES at the COMPLEMENT C1Q subunit. This leads to the sequential activation of COMPLEMENT C1R and COMPLEMENT C1S subunits. Activated C1s cleaves COMPLEMENT C4 and COMPLEMENT C2 forming the membrane-bound classical C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.

A 150-kDa serum glycoprotein composed of three subunits with each encoded by a different gene (C8A; C8B; and C8G). This heterotrimer contains a disulfide-linked C8alpha-C8gamma heterodimer and a noncovalently associated C8beta chain. C8 is the next component to bind the C5-7 complex forming C5b-8 that binds COMPLEMENT C9 and acts as a catalyst in the polymerization of C9.

The first complement component to act in the activation of CLASSICAL COMPLEMENT PATHWAY. It is a calcium-dependent trimolecular complex made up of three subcomponents: COMPLEMENT C1Q; COMPLEMENT C1R; and COMPLEMENT C1S at 1:2:2 ratios. When the intact C1 binds to at least two antibodies (involving C1q), C1r and C1s are sequentially activated, leading to subsequent steps in the cascade of COMPLEMENT ACTIVATION.

Molecular sites on or in some B-lymphocytes and macrophages that recognize and combine with COMPLEMENT C3B. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids.

An important soluble regulator of the alternative pathway of complement activation (COMPLEMENT ACTIVATION PATHWAY, ALTERNATIVE). It is a 139-kDa glycoprotein expressed by the liver and secreted into the blood. It binds to COMPLEMENT C3B and makes iC3b (inactivated complement 3b) susceptible to cleavage by COMPLEMENT FACTOR I. Complement factor H also inhibits the association of C3b with COMPLEMENT FACTOR B to form the C3bB proenzyme, and promotes the dissociation of Bb from the C3bBb complex (COMPLEMENT C3 CONVERTASE, ALTERNATIVE PATHWAY).

The larger fragment generated from the cleavage of C5 by C5 CONVERTASE that yields COMPLEMENT C5A and C5b (beta chain + alpha' chain, the residual alpha chain, bound by disulfide bond). C5b remains bound to the membrane and initiates the spontaneous assembly of the late complement components to form C5b-8-poly-C9, the MEMBRANE ATTACK COMPLEX.

The COOH-terminal fragment of COMPLEMENT 2, released by the action of activated COMPLEMENT C1S. It is a SERINE PROTEASE. C2a combines with COMPLEMENT C4B to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE).

A G-protein-coupled receptor that signals an increase in intracellular calcium in response to the potent ANAPHYLATOXIN peptide COMPLEMENT C5A.

Enzymes that activate one or more COMPLEMENT PROTEINS in the complement system leading to the formation of the COMPLEMENT MEMBRANE ATTACK COMPLEX, an important response in host defense. They are enzymes in the various COMPLEMENT ACTIVATION pathways.

Compounds that negatively regulate the cascade process of COMPLEMENT ACTIVATION. Uncontrolled complement activation and resulting cell lysis is potentially dangerous for the host.

A screening assay for circulating COMPLEMENT PROTEINS. Diluted SERUM samples are added to antibody-coated ERYTHROCYTES and the percentage of cell lysis is measured. The values are expressed by the so called CH50, in HEMOLYTIC COMPLEMENT units per milliliter, which is the dilution of serum required to lyse 50 percent of the erythrocytes in the assay.

Serum proteins that inhibit, antagonize, or inactivate COMPLEMENT C1 or its subunits.

Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognize and combine with COMPLEMENT C3D. Human complement receptor 2 (CR2) serves as a receptor for both C3dg and the gp350/220 glycoprotein of HERPESVIRUS 4, HUMAN, and binds the monoclonal antibody OKB7, which blocks binding of both ligands to the receptor.

Serum peptides derived from certain cleaved COMPLEMENT PROTEINS during COMPLEMENT ACTIVATION. They induce smooth MUSCLE CONTRACTION; mast cell HISTAMINE RELEASE; PLATELET AGGREGATION; and act as mediators of the local inflammatory process. The order of anaphylatoxin activity from the strongest to the weakest is C5a, C3a, C4a, and C5a des-arginine.

Serologic tests based on inactivation of complement by the antigen-antibody complex (stage 1). Binding of free complement can be visualized by addition of a second antigen-antibody system such as red cells and appropriate red cell antibody (hemolysin) requiring complement for its completion (stage 2). Failure of the red cells to lyse indicates that a specific antigen-antibody reaction has taken place in stage 1. If red cells lyse, free complement is present indicating no antigen-antibody reaction occurred in stage 1.

A serum protein which is important in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY. This enzyme cleaves the COMPLEMENT C3B-bound COMPLEMENT FACTOR B to form C3bBb which is ALTERNATIVE PATHWAY C3 CONVERTASE.

A plasma serine proteinase that cleaves the alpha-chains of C3b and C4b in the presence of the cofactors COMPLEMENT FACTOR H and C4-binding protein, respectively. It is a 66-kDa glycoprotein that converts C3b to inactivated C3b (iC3b) followed by the release of two fragments, C3c (150-kDa) and C3dg (41-kDa). It was formerly called KAF, C3bINF, or enzyme 3b inactivator.

A serum protein that regulates the CLASSICAL COMPLEMENT ACTIVATION PATHWAY. It binds as a cofactor to COMPLEMENT FACTOR I which then hydrolyzes the COMPLEMENT C4B in the CLASSICAL PATHWAY C3 CONVERTASE (C4bC2a).

Endogenous proteins that inhibit or inactivate COMPLEMENT C3B. They include COMPLEMENT FACTOR H and COMPLEMENT FACTOR I (C3b/C4b inactivator). They cleave or promote the cleavage of C3b into inactive fragments, and thus are important in the down-regulation of COMPLEMENT ACTIVATION and its cytolytic sequence.

GPI-linked membrane proteins broadly distributed among hematopoietic and non-hematopoietic cells. CD55 prevents the assembly of C3 CONVERTASE or accelerates the disassembly of preformed convertase, thus blocking the formation of the membrane attack complex.

Important enzymes in the CLASSICAL COMPLEMENT ACTIVATION PATHWAY. They cleave COMPLEMENT C3 and COMPLEMENT C5.

The N-terminal fragment of COMPLEMENT 2, released by the action of activated COMPLEMENT C1S.

Small glycoproteins found on both hematopoietic and non-hematopoietic cells. CD59 restricts the cytolytic activity of homologous complement by binding to C8 and C9 and blocking the assembly of the membrane attack complex. (From Barclay et al., The Leukocyte Antigen FactsBook, 1993, p234)

Venoms from snakes of the genus Naja (family Elapidae). They contain many specific proteins that have cytotoxic, hemolytic, neurotoxic, and other properties. Like other elapid venoms, they are rich in enzymes. They include cobramines and cobralysins.

The complex formed by the binding of antigen and antibody molecules. The deposition of large antigen-antibody complexes leading to tissue damage causes IMMUNE COMPLEX DISEASES.

An adrenal microsomal cytochrome P450 enzyme that catalyzes the 21-hydroxylation of steroids in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP21 gene, converts progesterones to precursors of adrenal steroid hormones (CORTICOSTERONE; HYDROCORTISONE). Defects in CYP21 cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL).

Important enzymes in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY. They cleave COMPLEMENT C3 and COMPLEMENT C5.

An endogenous 105-kDa plasma glycoprotein produced primarily by the LIVER and MONOCYTES. It inhibits a broad spectrum of proteases, including the COMPLEMENT C1R and the COMPLEMENT C1S proteases of the CLASSICAL COMPLEMENT PATHWAY, and the MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASES. C1-INH-deficient individuals suffer from HEREDITARY ANGIOEDEMA TYPES I AND II.

The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.

The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.

A serine protease that is the complex of COMPLEMENT C3B and COMPLEMENT FACTOR BB. It cleaves multiple COMPLEMENT C3 into COMPLEMENT C3A (anaphylatoxin) and COMPLEMENT C3B in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY.

A serine protease that cleaves multiple COMPLEMENT 5 into COMPLEMENT 5A (anaphylatoxin) and COMPLEMENT 5B in the CLASSICAL COMPLEMENT ACTIVATION PATHWAY. It is a complex of CLASSICAL PATHWAY C3 CONVERTASE (C4b2a) with an additional COMPLEMENT C3B, or C4b2a3b.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

A serine protease that cleaves multiple COMPLEMENT 3 into COMPLEMENT 3A (anaphylatoxin) and COMPLEMENT 3B in the CLASSICAL COMPLEMENT ACTIVATION PATHWAY. It is a complex of COMPLEMENT 4B and COMPLEMENT 2A (C4b2a).

A ubiquitously expressed complement receptor that binds COMPLEMENT C3B and COMPLEMENT C4B and serves as a cofactor for their inactivation. CD46 also interacts with a wide variety of pathogens and mediates immune response.

Proteins that bind to particles and cells to increase susceptibility to PHAGOCYTOSIS, especially ANTIBODIES bound to EPITOPES that attach to FC RECEPTORS. COMPLEMENT C3B may also participate.

Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.

A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.

A serine protease that cleaves multiple COMPLEMENT C5 into COMPLEMENT C5A (anaphylatoxin) and COMPLEMENT C5B in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY. It is the complex of ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb) with an additional COMPLEMENT C3B, or C3bBb3b.

The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES).

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Complement activation triggered by the interaction of microbial POLYSACCHARIDES with serum MANNOSE-BINDING LECTIN resulting in the activation of MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASES. As in the classical pathway, MASPs cleave COMPLEMENT C4 and COMPLEMENT C2 to form C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.

A 53-kDa protein that is a positive regulator of the alternate pathway of complement activation (COMPLEMENT ACTIVATION PATHWAY, ALTERNATIVE). It stabilizes the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb) and protects it from rapid inactivation, thus facilitating the cascade of COMPLEMENT ACTIVATION and the formation of MEMBRANE ATTACK COMPLEX. Individuals with mutation in the PFC gene exhibit properdin deficiency and have a high susceptibility to infections.

A derivative of complement C5a, generated when the carboxy-terminal ARGININE is removed by CARBOXYPEPTIDASE B present in normal human serum. C5a des-Arg shows complete loss of spasmogenic activity though it retains some chemotactic ability (CHEMOATTRACTANTS).

C57BL mice are a commonly used strain of laboratory mice that are inbred to produce consistent and predictable results in scientific research.

An adhesion-promoting leukocyte surface membrane heterodimer. The alpha subunit consists of the CD11b ANTIGEN and the beta subunit the CD18 ANTIGEN. The antigen, which is an integrin, functions both as a receptor for complement 3 and in cell-cell and cell-substrate adhesive interactions.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A cluster of convoluted capillaries beginning at each nephric tubule in the kidney and held together by connective tissue.

The clear portion of BLOOD that is left after BLOOD COAGULATION to remove BLOOD CELLS and clotting proteins.

Chronic glomerulonephritis characterized histologically by proliferation of MESANGIAL CELLS, increase in the MESANGIAL EXTRACELLULAR MATRIX, and a thickening of the glomerular capillary walls. This may appear as a primary disorder or secondary to other diseases including infections and autoimmune disease SYSTEMIC LUPUS ERYTHEMATOSUS. Various subtypes are classified by their abnormal ultrastructures and immune deposits. Hypocomplementemia is a characteristic feature of all types of MPGN.

A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally being called a macroglobulin.

A genus of trematode flukes belonging to the family Schistosomatidae. There are over a dozen species. These parasites are found in man and other mammals. Snails are the intermediate hosts.

A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.

An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.

Inflammation of the renal glomeruli (KIDNEY GLOMERULUS) that can be classified by the type of glomerular injuries including antibody deposition, complement activation, cellular proliferation, and glomerulosclerosis. These structural and functional abnormalities usually lead to HEMATURIA; PROTEINURIA; HYPERTENSION; and RENAL INSUFFICIENCY.

Thickening of the walls of small ARTERIES or ARTERIOLES due to cell proliferation or HYALINE deposition.

Antibodies produced by a single clone of cells.

The genetic region which contains the loci of genes which determine the structure of the serologically defined (SD) and lymphocyte-defined (LD) TRANSPLANTATION ANTIGENS, genes which control the structure of the IMMUNE RESPONSE-ASSOCIATED ANTIGENS, HUMAN; the IMMUNE RESPONSE GENES which control the ability of an animal to respond immunologically to antigenic stimuli, and genes which determine the structure and/or level of the first four components of complement.

Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.

Antibodies that react with self-antigens (AUTOANTIGENS) of the organism that produced them.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)

Established cell cultures that have the potential to propagate indefinitely.

The capacity of a normal organism to remain unaffected by microorganisms and their toxins. It results from the presence of naturally occurring ANTI-INFECTIVE AGENTS, constitutional factors such as BODY TEMPERATURE and immediate acting immune cells such as NATURAL KILLER CELLS.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

BALB/C is a commonly used strain of inbred mice in medical research, known for their genetic uniformity and susceptibility to various diseases.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The natural bactericidal property of BLOOD due to normally occurring antibacterial substances such as beta lysin, leukin, etc. This activity needs to be distinguished from the bactericidal activity contained in a patient's serum as a result of antimicrobial therapy, which is measured by a SERUM BACTERICIDAL TEST.

Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.

Variant forms of the same gene, occupying the same locus on homologous CHROMOSOMES, and governing the variants in production of the same gene product.

Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).

Proteins prepared by recombinant DNA technology.

An IgG autoantibody against the ALTERNATIVE PATHWAY C3 CONVERTASE, found in serum of patients with MESANGIOCAPILLARY GLOMERULONEPHRITIS. The binding of this autoantibody to C3bBb stabilizes the enzyme thus reduces the actions of C3b inactivators (COMPLEMENT FACTOR H; COMPLEMENT FACTOR I). This abnormally stabilized enzyme induces a continuous COMPLEMENT ACTIVATION and generation of C3b thereby promoting the assembly of MEMBRANE ATTACK COMPLEX and cytolysis.

Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.

Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses.

Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.

Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).

Glomerulonephritis associated with autoimmune disease SYSTEMIC LUPUS ERYTHEMATOSUS. Lupus nephritis is histologically classified into 6 classes: class I - normal glomeruli, class II - pure mesangial alterations, class III - focal segmental glomerulonephritis, class IV - diffuse glomerulonephritis, class V - diffuse membranous glomerulonephritis, and class VI - advanced sclerosing glomerulonephritis (The World Health Organization classification 1982).

Autoantibodies directed against various nuclear antigens including DNA, RNA, histones, acidic nuclear proteins, or complexes of these molecular elements. Antinuclear antibodies are found in systemic autoimmune diseases including systemic lupus erythematosus, Sjogren's syndrome, scleroderma, polymyositis, and mixed connective tissue disease.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Plasmids containing at least one cos (cohesive-end site) of PHAGE LAMBDA. They are used as cloning vehicles.

In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.

Proteins found in any species of bacterium.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.

A pathological process characterized by injury or destruction of tissues caused by a variety of cytologic and chemical reactions. It is usually manifested by typical signs of pain, heat, redness, swelling, and loss of function.

Transport proteins that carry specific substances in the blood or across cell membranes.

Serum serine proteases which participate in COMPLEMENT ACTIVATION. They are activated when complexed with the MANNOSE-BINDING LECTIN, therefore also known as Mannose-binding protein-Associated Serine Proteases (MASPs). They cleave COMPLEMENT C4 and COMPLEMENT C2 to form C4b2a, the CLASSICAL PATHWAY C3 CONVERTASE.

A group of inherited disorders of the ADRENAL GLANDS, caused by enzyme defects in the synthesis of cortisol (HYDROCORTISONE) and/or ALDOSTERONE leading to accumulation of precursors for ANDROGENS. Depending on the hormone imbalance, congenital adrenal hyperplasia can be classified as salt-wasting, hypertensive, virilizing, or feminizing. Defects in STEROID 21-HYDROXYLASE; STEROID 11-BETA-HYDROXYLASE; STEROID 17-ALPHA-HYDROXYLASE; 3-beta-hydroxysteroid dehydrogenase (3-HYDROXYSTEROID DEHYDROGENASES); TESTOSTERONE 5-ALPHA-REDUCTASE; or steroidogenic acute regulatory protein; among others, underlie these disorders.

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

An individual in which both alleles at a given locus are identical.

Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.

The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.

Biologically active substances whose activities affect or play a role in the functioning of the immune system.

Zymosan is a polysaccharide derived from yeast cell walls that is used in medical research to induce an inflammatory response in animals.

Elements of limited time intervals, contributing to particular results or situations.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Histochemical localization of immunoreactive substances using labeled antibodies as reagents.

The number of copies of a given gene present in the cell of an organism. An increase in gene dosage (by GENE DUPLICATION for example) can result in higher levels of gene product formation. GENE DOSAGE COMPENSATION mechanisms result in adjustments to the level GENE EXPRESSION when there are changes or differences in gene dosage.

The genetic constitution of individuals with respect to one member of a pair of allelic genes, or sets of genes that are closely linked and tend to be inherited together such as those of the MAJOR HISTOCOMPATIBILITY COMPLEX.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Antigens determined by leukocyte loci found on chromosome 6, the major histocompatibility loci in humans. They are polypeptides or glycoproteins found on most nucleated cells and platelets, determine tissue types for transplantation, and are associated with certain diseases.

Glycoproteins found on the membrane or surface of cells.

The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.

The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.

Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles.

The sum of the weight of all the atoms in a molecule.

The rate dynamics in chemical or physical systems.

Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.

The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.

Lymphoid cells concerned with humoral immunity. They are short-lived cells resembling bursa-derived lymphocytes of birds in their production of immunoglobulin upon appropriate stimulation.

The presence of proteins in the urine, an indicator of KIDNEY DISEASES.

Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.

The production of ANTIBODIES by proliferating and differentiated B-LYMPHOCYTES under stimulation by ANTIGENS.

Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.

A gram-positive organism found in the upper respiratory tract, inflammatory exudates, and various body fluids of normal and/or diseased humans and, rarely, domestic animals.

A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region.

Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A plasma protein that circulates in increased amounts during inflammation and after tissue damage.

The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.

A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.

Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed)

Protein precursors are the building blocks of proteins that are synthesized in the body from amino acids.

Cytochrome P-450 monooxygenases (MIXED FUNCTION OXYGENASES) that are important in steroid biosynthesis and metabolism.

Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.

Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

A method (first developed by E.M. Southern) for detection of DNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.

Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.

Degenerative changes in the RETINA usually of older adults which results in a loss of vision in the center of the visual field (the MACULA LUTEA) because of damage to the retina. It occurs in dry and wet forms.

A constitution or condition of the body which makes the tissues react in special ways to certain extrinsic stimuli and thus tends to make the individual more than usually susceptible to certain diseases.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.

A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

The record of descent or ancestry, particularly of a particular condition or trait, indicating individual family members, their relationships, and their status with respect to the trait or condition.

Studies which start with the identification of persons with a disease of interest and a control (comparison, referent) group without the disease. The relationship of an attribute to the disease is examined by comparing diseased and non-diseased persons with regard to the frequency or levels of the attribute in each group.

Variation occurring within a species in the presence or length of DNA fragment generated by a specific endonuclease at a specific site in the genome. Such variations are generated by mutations that create or abolish recognition sites for these enzymes or change the length of the fragment.

The proportion of one particular in the total of all ALLELES for one genetic locus in a breeding POPULATION.

A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research.

A method for the detection of very small quantities of antibody in which the antigen-antibody-complement complex adheres to indicator cells, usually primate erythrocytes or nonprimate blood platelets. The reaction is dependent on the number of bound C3 molecules on the C3b receptor sites of the indicator cell.

DBA mice are a strain of inbred mice commonly used in medical research due to their susceptibility to a variety of diseases and genetic disorders.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

A technique that combines protein electrophoresis and double immunodiffusion. In this procedure proteins are first separated by gel electrophoresis (usually agarose), then made visible by immunodiffusion of specific antibodies. A distinct elliptical precipitin arc results for each protein detectable by the antisera.

Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.

A chronic systemic disease, primarily of the joints, marked by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. Etiology is unknown, but autoimmune mechanisms have been implicated.

Immunoglobulins produced in a response to BACTERIAL ANTIGENS.

The systematic study of the complete complement of proteins (PROTEOME) of organisms.

Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.

A cytokine that stimulates the growth and differentiation of B-LYMPHOCYTES and is also a growth factor for HYBRIDOMAS and plasmacytomas. It is produced by many different cells including T-LYMPHOCYTES; MONOCYTES; and FIBROBLASTS.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

A latent susceptibility to disease at the genetic level, which may be activated under certain conditions.

A condition characterized by the recurrence of HEMOGLOBINURIA caused by intravascular HEMOLYSIS. In cases occurring upon cold exposure (paroxysmal cold hemoglobinuria), usually after infections, there is a circulating antibody which is also a cold hemolysin. In cases occurring during or after sleep (paroxysmal nocturnal hemoglobinuria), the clonal hematopoietic stem cells exhibit a global deficiency of cell membrane proteins.

A single nucleotide variation in a genetic sequence that occurs at appreciable frequency in the population.

Group of diseases mediated by the deposition of large soluble complexes of antigen and antibody with resultant damage to tissue. Besides SERUM SICKNESS and the ARTHUS REACTION, evidence supports a pathogenic role for immune complexes in many other IMMUNE SYSTEM DISEASES including GLOMERULONEPHRITIS, systemic lupus erythematosus (LUPUS ERYTHEMATOSUS, SYSTEMIC) and POLYARTERITIS NODOSA.

Complement component C8gamma is expressed in human fetal and adult kidney independent of C8alpha. (1/110)

Human complement component C8gamma is an unusual complement factor since it shows no homology to other complement proteins but is a member of the lipocalin superfamily. So far, it has been found exclusively in plasma, covalently linked to C8alpha by disulfide bridging. We have used dot blot and Northern blot analyses of a large number of different human tissues to survey systematically the expression pattern of C8gamma. Our experiments clearly showed that besides in liver, this gene is also expressed in fetal and adult kidney. Renal expression of C8gamma is not dependent on C8alpha expression, since we could not detect C8alpha expression in kidney. Thus its physiological function is not restricted to a specific action in association with complement components. As a prerequisite for further characterization of the structure and binding activities of the uncomplexed C8gamma, we have expressed the encoding cDNA in Escherichia coli. To increase the probability for proper folding of the characteristic intramolecular disulfide bridge the recombinant protein was produced by secretion to the periplasm. (+info)

Increased ion permeability of planar lipid bilayer membranes after treatment with the C5b-9 cytolytic attack mechanism of complement. (2/110)

The ion permeability of planar lipid bilayers, as measured electrically, was found to increase modestly upon treatment with purified complement complex C5b,6 and complement components C7 and C8. The subsequent addition C9 greatly amplified this change. No permeability changes occurred when components were added individually to the membrane, or when they were used in paired combinations, or when C5b, C7, C8, and C9 were admixed prior to addition. Thus, there is a significant parallel between the permeability changes induced in the model membrane and damage produced in biological membranes by the C5b-9 complement attack sequence. The efficiency of membrane action by C5b-9 was critically dependent on the order in whcih components were added to the membrane. There were also differences in the electrical properties of membranes treated with C5b-8 and C5b-9, though in both cases the enhanced bilayer permeability is best attributed to the formation of trans-membrane channels. Collectively, the data are consistent with the hypothesis that the mechanism of membrane action by complement involves the production of a stable channel across the lipid bilayer, resulting in cell death by colloid-osmotic lysis. (+info)

The role of Fcgamma receptor polymorphisms and C3 in the immune defence against Neisseria meningitidis in complement-deficient individuals. (3/110)

Individuals with either a late (C5-9) complement component deficiency (LCCD) or properdin deficiency are at increased risk to develop meningococcal disease, often due to serogroups W135 and Y. Anti-meningococcal defence in both LCCD persons and properdin-deficient individuals without bactericidal antibodies depends mainly on phagocytosis. Three types of opsonin receptors are involved in phagocytosis by polymorphonuclear cells (PMN). These represent the polymorphic FcgammaRIIa (CD32) and FcgammaRIIIb (CD16b) receptors, and the C3 receptor CR3 (CD11b/CD18). When the distribution of FcgammaRIIa and FcgammaRIIIb allotypes was assessed in 15 LCCD and in 15 properdin-deficient patients with/without previous meningococcal disease, we found the combination of FcgammaRIIa-R/R131 with FcgammaRIIIb-NA2/NA2 allotypes to be associated with previous meningococcal disease (odds ratio 13.9, Fisher's test P = 0.036). No such relation was observed in the properdin-deficient patients. The importance of FcgammaRIIa allotypes was also demonstrated using in vitro phagocytosis assays. PMN from FcgammaRIIa-R/R131 homozygous donors internalized IgG2 opsonized meningococci W135 significantly (P < 0.05) less than PMN from FcgammaRIIa-H/H131 donors. When properdin-deficient serum was tested, it was observed that reconstitution with properdin resulted in enhanced PMN phagocytosis of the W135 meningococci (P = 0.001). This enhanced phagocytosis was parallelled by an increase in C3 deposition onto the opsonized meningococci W135 (r = 0.6568, P = 0. 01). We conclude that the occurrence of meningococcal disease in LCCD patients is associated with certain FcgammaR allotypes. Properdin-deficient individuals are susceptible to meningococcal disease because of an insufficient C3 deposition on the surface of meningococci, resulting in insufficient phagocytosis. (+info)

Free radicals upregulate complement expression in rabbit isolated heart. (4/110)

Both free radicals and complement activation can injure tissue. Our study determined whether free radicals alter complement production by the myocardium. Isolated hearts from New Zealand White rabbits were perfused on a Langendorff apparatus and exposed to xanthine (X; 100 microM) plus xanthine oxidase (XO; 8 mU/ml) (X/XO). The free radical-generating system significantly (P < 0.05) increased C1q and also increased C1r, C3, C8, and C9 transcription compared with controls. Immunohistological examination revealed augmented membrane attack complex deposition on X/XO-treated tissue. X/XO-treated hearts also exhibited significant (P < 0.05) increases in coronary perfusion pressure and left ventricular end-diastolic pressure and a decrease in left-ventricular developed pressure. N-(2-mercaptopropionyl)-glycine (3 mM), in conjunction with the superoxide dismutase mimetic SC-52608 (100 microM), significantly (P < 0.05) reduced the upregulation of C1q, C1r, C3, C8, and C9 mRNA expression elicited by X/XO. The antioxidants also ameliorated the deterioration in function caused by X/XO. Local complement activation may represent a mechanism by which free radicals mediate tissue injury. (+info)

CD59 protects rat kidney from complement mediated injury in collaboration with crry. (5/110)

BACKGROUND: As previously reported, the membrane-bound complement regulator at the C3 level (Crry/p65) is important in maintaining normal integrity of the kidney in rats. However, the role of a complement regulator at the C8/9 level (CD59) is not clear, especially when activation of complement occurs at the C3 level. The aim of this work was to elucidate the in vivo role of CD59 under C3 activating conditions. METHODS: Two monoclonal antibodies, 5I2 and 6D1, were used to suppress the function of Crry and CD59, respectively. In order to activate alternative the pathway of complement, the left kidney was perfused with 5I2 and/or 6D1 and was recirculated. RESULTS: In the kidneys perfused with 5I2 alone, deposition of C3 and membrane attack complex (MAC) was observed in the peritubular capillaries, vasa recta, and tubular basement membranes. Cast formation, tubular dilation and degeneration, and cellular infiltration were observed at days 1 and 4, and they recovered by day 7. Further suppression of CD59 by 6D1 significantly enhanced the deposition of MAC and worsened the already exacerbated tubulointerstitial injury. These effects of 6D1 were dose dependent. Perfusion with 6D1 alone did not induce histologic damage or MAC deposition in the tubulointerstitium. CONCLUSIONS: In rats, CD59 maintains normal integrity of the kidney in collaboration with Crry in rats against complement-mediated damage in vivo. (+info)

Hypochlorite-induced alterations to canine serum complement. (6/110)

Changes in the concentration of the components of complement produced by NaOC1 both in vitro and in vivo are recorded. C1, C4 and C7 are particularly sensitive to this oxidizing agent, although all components decrease at high concentrations of NaOC1. Following oxidation, complement componenets return rapidly to normal. Data are presented to indicate that part of this repair mechanism is due to the action of reducing agents such as ascorbic acid and part is due to the synthesis of the individual components. The unique sensitivity of complement components to oxidation make this treatment of potential value in suppressing the inflammatory response. (+info)

Novel mechanism of antibody-independent complement neutralization of herpes simplex virus type 1. (7/110)

The envelope surface glycoprotein C (gC) of HSV-1 interferes with the complement cascade by binding C3 and activation products C3b, iC3b, and C3c, and by blocking the interaction of C5 and properdin with C3b. Wild-type HSV-1 is resistant to Ab-independent complement neutralization; however, HSV-1 mutant virus lacking gC is highly susceptible to complement resulting in > or =100-fold reduction in virus titer. We evaluated the mechanisms by which complement inhibits HSV-1 gC null virus to better understand how gC protects against complement-mediated neutralization. C8-depleted serum prepared from an HSV-1 and -2 Ab-negative donor neutralized gC null virus comparable to complement-intact serum, indicating that C8 and terminal lytic activity are not required. In contrast, C5-depleted serum from the same donor failed to neutralize gC null virus, supporting a requirement for C5. EDTA-treated serum did not neutralize gC null virus, indicating that complement activation is required. Factor D-depleted and C6-depleted sera neutralized virus, suggesting that the alternative complement pathway and complement components beyond C5 are not required. Complement did not aggregate virus or block attachment to cells. However, complement inhibited infection before early viral gene expression, indicating that complement affects one or more of the following steps in virus replication: virus entry, uncoating, DNA transport to the nucleus, or immediate early gene expression. Therefore, in the absence of gC, HSV-1 is readily inhibited by complement by a C5-dependent mechanism that does not require viral lysis, aggregation, or blocking virus attachment. (+info)

Human complement protein C8 gamma. (8/110)

Human C8 gamma is a 22 kDa subunit of complement component C8, which is one of five components (C5b, C6, C7, C8, C9) that interact to form the cytolytic membrane attack complex (MAC) of complement. C8 contains three nonidentical subunits (alpha, beta, gamma) that are products of different genes. These subunits are arranged asymmetrically to form a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta. C8 alpha and C8 beta are homologous to C6, C7 and C9 and together these proteins comprise what is referred to as the 'MAC protein family'. By comparison, C8 gamma is distinct in that it belongs to the lipocalin family of small, secreted proteins which have the common ability to bind small hydrophobic ligands. While specific roles have been identified for C8 alpha and C8 beta in the formation and function of the MAC, a function for C8 gamma and the identity of its ligand are unknown. This review summarizes the current status of C8 gamma structure and function and the progress made from efforts to determine its role in the complement system. (+info)

Complement C3 is a protein that plays a crucial role in the immune system's defense against infections. It is one of the proteins that make up the complement system, a series of proteins that work together to help the immune system identify and destroy invading pathogens. C3 is synthesized in the liver and circulates in the bloodstream. When it encounters a pathogen, it becomes activated and splits into two fragments: C3a and C3b. C3a is a small protein that acts as a signaling molecule, attracting immune cells to the site of infection and promoting inflammation. C3b, on the other hand, binds to the surface of the pathogen and helps to recruit other immune cells to destroy it. In medical testing, the level of complement C3 in the blood can be measured to help diagnose and monitor certain medical conditions. For example, low levels of C3 can be a sign of complement deficiency, which can increase the risk of infections. High levels of C3 can be a sign of certain autoimmune disorders, such as lupus or rheumatoid arthritis.

Complement C4 is a protein that is part of the complement system, which is a group of proteins that work together to help the immune system fight off infections. The complement system is activated when the body recognizes a foreign substance, such as a virus or bacteria, and begins to attack it. Complement C4 is one of several proteins that are produced in response to this activation, and it plays a role in the destruction of the foreign substance by helping to recruit other immune cells to the site of the infection.

Complement C4a is a protein that is produced as part of the complement system, which is a group of proteins that plays a role in the immune response. C4a is produced when the complement system is activated, and it functions as an inflammatory mediator, helping to recruit immune cells to the site of infection or injury. C4a can also help to activate other components of the complement system, amplifying the immune response. In the medical field, levels of C4a can be measured in blood tests as a way to assess the activity of the complement system and to diagnose or monitor certain conditions, such as autoimmune diseases or infections.

Complement C3a is a protein that is produced as a result of the activation of the complement system, which is a part of the immune system. The complement system is a series of proteins that work together to help the body fight off infections and other foreign substances. C3a is one of several complement proteins that are produced when the complement system is activated. It is a small protein that is released from the larger complement protein C3 when it is cleaved by enzymes. C3a has several functions in the immune system, including attracting immune cells to the site of an infection, promoting the release of other immune system molecules, and helping to regulate the immune response. In the medical field, C3a is often measured as a way to assess the activity of the complement system. Abnormal levels of C3a can be associated with a variety of medical conditions, including autoimmune disorders, infections, and certain types of cancer.

Complement C1q is a protein that plays a central role in the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. C1q is a component of the C1 complex, which is the first step in the activation of the complement system. When C1q binds to a pathogen or damaged cell, it triggers a cascade of events that leads to the destruction of the pathogen or cell by the immune system. C1q is also involved in the regulation of the complement system, helping to prevent overactivation and damage to healthy cells.

Complement C5a is a protein that is produced as a result of the activation of the complement system, which is a part of the immune system. The complement system is a series of proteins that work together to help the body fight off infections and other foreign substances. Complement C5a is a potent inflammatory mediator that is involved in the recruitment of immune cells to the site of infection or injury. It does this by binding to receptors on the surface of immune cells, such as neutrophils and macrophages, and triggering a signaling cascade that leads to the release of these cells from the blood vessels and their migration to the site of inflammation. Complement C5a also has other functions, such as promoting the activation of the complement system and enhancing the ability of immune cells to phagocytose (engulf and destroy) pathogens. In the medical field, complement C5a is often measured as a marker of inflammation and immune system activation. It is also being studied as a potential therapeutic target for a variety of conditions, including autoimmune diseases, infections, and cancer.

Complement activation is a complex process that occurs in the immune system in response to the presence of foreign substances, such as bacteria, viruses, or other pathogens. The complement system is a group of proteins that circulate in the blood and are activated when they encounter a pathogen. There are three main pathways of complement activation: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of steps that ultimately lead to the formation of a membrane attack complex (MAC), which can directly destroy the pathogen or cause it to be engulfed and destroyed by immune cells. Complement activation is an important part of the immune response and helps to protect the body against infection. However, in some cases, the complement system can be overactive and cause damage to healthy cells and tissues. This can occur in conditions such as autoimmune diseases, where the immune system mistakenly attacks the body's own cells, or in certain types of infections, where the complement system is activated inappropriately.

Complement C4b is a protein that is part of the complement system, a complex series of proteins that plays a role in the body's immune response. The complement system helps to identify and destroy foreign substances, such as bacteria and viruses, that enter the body. C4b is one of several proteins that are produced when the complement system is activated. It is produced when C4, another protein in the complement system, is cleaved by an enzyme called C1s. C4b is then attached to the surface of a pathogen, marking it for destruction by other components of the complement system. C4b is also involved in the formation of the membrane attack complex (MAC), which is a group of proteins that form a pore in the membrane of a pathogen, causing it to burst and be destroyed. The MAC is one of the most powerful weapons in the complement system, and it is able to destroy even highly resistant pathogens. In addition to its role in the immune response, C4b has been implicated in a number of other biological processes, including inflammation, cell signaling, and the regulation of the complement system itself.

Complement C5 is a protein that plays a crucial role in the immune system's response to infections and inflammation. It is one of the proteins in the complement system, a group of proteins that work together to help the immune system identify and destroy invading pathogens. Complement C5 is produced by immune cells and is activated when it comes into contact with the surface of a pathogen. Once activated, it cleaves into two fragments, C5a and C5b, which then trigger a series of reactions that lead to the destruction of the pathogen. C5a is a potent inflammatory mediator that attracts immune cells to the site of infection and stimulates the release of other inflammatory molecules. C5b, on the other hand, is a key component of the membrane attack complex (MAC), which forms a pore in the membrane of the pathogen, leading to its destruction. Complement C5 is also involved in other immune processes, such as the clearance of immune complexes from the bloodstream and the regulation of inflammation. Deficiencies in complement C5 can lead to increased susceptibility to infections and autoimmune diseases.

Complement C3b is a protein fragment that is generated when the complement system, a part of the immune system, is activated. The complement system is a complex network of proteins that work together to help the body fight off infections and remove damaged or abnormal cells. C3b is produced when the complement protein C3 is cleaved by enzymes in the complement system. C3b plays an important role in the complement system by binding to the surface of pathogens or damaged cells and marking them for destruction by immune cells. It also helps to recruit immune cells to the site of infection or injury and can activate other components of the complement system to enhance the immune response. In the medical field, C3b is often measured as a marker of complement system activation. Abnormal levels of C3b can be associated with a variety of medical conditions, including autoimmune disorders, infections, and certain types of cancer.

The complement system is a complex network of proteins that plays a crucial role in the immune system's defense against infections. Complement system proteins are a group of proteins that are produced by the liver and other cells in the body and circulate in the blood. These proteins work together to identify and destroy invading pathogens, such as bacteria and viruses, by forming a membrane attack complex (MAC) that punctures the pathogen's cell membrane, causing it to burst and die. There are several different types of complement system proteins, including: 1. Complement proteins: These are the primary components of the complement system and include C1, C2, C3, C4, C5, C6, C7, C8, and C9. 2. Complement regulatory proteins: These proteins help to control the activation of the complement system and prevent it from attacking healthy cells. Examples include C1 inhibitor, C4 binding protein, and decay-accelerating factor. 3. Complement receptors: These proteins are found on the surface of immune cells and help to bind to and activate complement proteins. Examples include CR1, CR2, and CR3. Complement system proteins play a critical role in the immune response and are involved in a wide range of diseases, including autoimmune disorders, infections, and cancer.

Complement C6 is a protein that is part of the complement system, which is a complex network of proteins in the blood that helps to defend the body against infections. The complement system is activated when pathogens, such as bacteria or viruses, enter the body, and it works to destroy them by forming a membrane attack complex (MAC) that punctures the pathogen's cell membrane, causing it to burst and die. Complement C6 is one of several proteins that are involved in the formation of the MAC. It is produced by the liver and other cells in the body, and it plays a critical role in the complement system by helping to stabilize the MAC and promote its insertion into the pathogen's cell membrane. Abnormalities in the complement system, including defects in complement C6, can lead to a variety of medical conditions, including complement-mediated diseases such as atypical hemolytic uremic syndrome (aHUS) and membranoproliferative glomerulonephritis (MPGN). These conditions can cause a range of symptoms, including kidney damage, blood clots, and an increased risk of infections.

Complement C3c is a protein that is a part of the complement system, which is a complex series of proteins that plays a role in the body's immune response. The complement system helps to identify and destroy foreign substances, such as bacteria and viruses, that enter the body. Complement C3c is a cleavage product of the larger complement protein C3, which is produced by the liver and other cells in the body. When the complement system is activated, C3 is cleaved into several smaller fragments, including C3c. C3c is an important component of the complement system because it can bind to the surface of pathogens and help to recruit immune cells to the site of infection. It can also help to activate other components of the complement system, which can lead to the destruction of the pathogen. Abnormal levels of complement C3c can be associated with a variety of medical conditions, including autoimmune disorders, infections, and certain types of cancer. In some cases, measuring complement C3c levels may be useful for diagnosing or monitoring these conditions.

Complement C3d is a protein fragment that is generated when the complement system, a part of the immune system, is activated. The complement system is a complex network of proteins that work together to help the body fight off infections and remove damaged or abnormal cells. C3d is produced when the complement protein C3 is cleaved by an enzyme called C3 convertase. This cleavage event releases C3d from the larger C3 protein molecule. C3d is an important component of the complement system because it helps to bind complement proteins to the surface of pathogens or damaged cells, marking them for destruction by other components of the complement system. In the medical field, C3d is often measured as a marker of complement activation. Abnormal levels of C3d in the blood can be an indication of certain medical conditions, such as autoimmune disorders, infections, or kidney disease.

Complement C2 is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. Complement C2 is a component of the classical pathway of the complement system, which is activated by the binding of antibodies to the surface of pathogens or damaged cells. Complement C2 is synthesized in the liver and circulates in the blood as a soluble protein. When the classical pathway is activated, Complement C2 is cleaved into two fragments, C2a and C2b. C2b then binds to C4b, which is another component of the complement system, to form a complex that can bind to the surface of pathogens or damaged cells. Once bound to the surface of a pathogen or damaged cell, the complement system is activated, leading to the formation of a membrane attack complex (MAC) that can destroy the pathogen or cell. Complement C2 is also involved in other immune responses, such as the recruitment of immune cells to sites of infection or injury. In summary, Complement C2 is a protein that plays a critical role in the complement system, which helps to defend the body against infections and other harmful substances.

Complement C9 is a protein that is part of the complement system, which is a group of proteins that plays a role in the immune system's defense against infections. The complement system is activated when pathogens, such as bacteria or viruses, enter the body, and it helps to destroy the pathogens by forming a membrane attack complex (MAC) that punctures the pathogen's cell membrane, causing it to burst and die. Complement C9 is the final component of the MAC, and it is responsible for forming the central pore in the complex that allows the other components to pass through and puncture the pathogen's cell membrane. Complement C9 is produced by the liver and other cells in the body, and it is stored in inactive form until it is activated by the complement system. Deficiencies in complement C9 can lead to increased susceptibility to infections, while excessive activation of the complement system can cause damage to healthy cells and tissues.

Receptors, Complement refers to a group of proteins that are part of the complement system, a complex network of proteins in the blood that helps to defend the body against infections. These receptors are located on the surface of immune cells, such as macrophages and neutrophils, and bind to specific molecules on the surface of pathogens, such as bacteria and viruses. This binding triggers a series of reactions that ultimately lead to the destruction of the pathogen. The complement receptors play a crucial role in the immune response and are important for the clearance of pathogens from the body.

In the medical field, "Complement C1s" refers to a specific protein component of the complement system, which is a group of proteins that play a crucial role in the immune system's defense against infections and other harmful substances. The complement system is activated when pathogens or damaged cells are present in the body, and it works by forming a membrane attack complex (MAC) that can directly destroy the pathogen or infected cell. Complement C1s is one of the first proteins to be activated in the complement cascade, and it helps to initiate the formation of the MAC. Complement C1s is typically measured in blood tests as a way to assess the overall function of the complement system and to diagnose or monitor certain medical conditions, such as autoimmune disorders, infections, and certain types of cancer. Abnormal levels of complement C1s can indicate problems with the complement system, which may require further investigation and treatment.

The Complement Membrane Attack Complex (MAC) is a group of proteins that are part of the complement system, a complex series of proteins in the blood that help the immune system fight off infections. The MAC is formed when certain complement proteins, called terminal complement proteins, come together to form a pore in the membrane of a pathogen, such as a virus or bacteria. This pore allows ions, water, and other molecules to flow out of the pathogen, ultimately leading to its destruction. The MAC is an important part of the body's defense against infections and is also involved in the regulation of the immune response.

Complement C1r is a protein that plays a role in the complement system, which is a part of the immune system that helps to defend the body against infections. The complement system is made up of a series of proteins that work together to identify and destroy foreign substances, such as bacteria and viruses. C1r is one of several proteins that make up the first step in the complement system, known as the classical pathway. When C1r is activated, it cleaves another protein called C1s, which then cleaves a third protein called C4. This cleavage event triggers a cascade of reactions that ultimately leads to the destruction of the foreign substance. Complement C1r is encoded by the "C1R" gene, which is located on chromosome 19 in humans. Mutations in the "C1R" gene can lead to a deficiency in C1r, which can result in a weakened immune system and an increased susceptibility to infections.

Complement inactivator proteins are a group of proteins that regulate the complement system, a part of the immune system that helps to defend the body against infections. These proteins act as inhibitors, preventing the complement system from attacking healthy cells and tissues. They are important for maintaining immune homeostasis and preventing autoimmune diseases. Examples of complement inactivator proteins include C1 inhibitor, C4 binding protein, and decay accelerating factor.

Complement C7 is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. The complement system is made up of a series of proteins that work together to identify and destroy foreign invaders, such as bacteria and viruses. Complement C7 is one of the proteins in the terminal complement pathway, which is the final stage of the complement system's attack on invaders. In this pathway, Complement C7 is activated by the binding of other complement proteins to the surface of a pathogen, and it then helps to form a membrane attack complex (MAC) that punctures the pathogen's cell membrane, leading to its destruction. Complement C7 deficiency can result in a weakened immune system and an increased susceptibility to infections. It is a rare genetic disorder that is inherited in an autosomal recessive pattern, meaning that an individual must inherit two copies of the defective gene (one from each parent) in order to develop the condition.

In the medical field, Complement C3-C5 Convertases are enzymes that play a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. The complement system consists of a series of proteins that work together to identify and eliminate pathogens, such as bacteria and viruses. Complement C3-C5 Convertases are enzymes that cleave and activate certain complement proteins, including C3 and C5, which are essential components of the complement system. There are two types of Complement C3-C5 Convertases: the classical pathway convertase and the alternative pathway convertase. The classical pathway convertase is formed when antibodies bind to antigens on the surface of a pathogen, while the alternative pathway convertase is activated spontaneously. Once activated, Complement C3-C5 Convertases cleave C3 and C5 into smaller fragments, which then interact with other complement proteins to form a membrane attack complex (MAC) that can directly destroy the pathogen. The complement system also plays a role in inflammation and the recruitment of immune cells to the site of infection. Complement C3-C5 Convertases are important for the proper functioning of the complement system, and defects in these enzymes can lead to a variety of immune disorders, such as complement deficiency diseases and autoimmune diseases.

Complement Factor B (CFB) is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and remove damaged cells. CFB is a soluble protein that is produced by the liver and circulates in the bloodstream. In the complement system, CFB is involved in the activation of the alternative pathway, which is one of three pathways that can activate the complement system. The alternative pathway is activated when antibodies bind to foreign substances on the surface of cells, and CFB helps to amplify the immune response by promoting the formation of a complex that leads to the activation of other complement proteins. Deficiencies in CFB can lead to a condition called complement factor B deficiency, which can result in recurrent infections and other immune system disorders.

The complement pathway, alternative, is a series of proteins that are part of the body's immune system. It is an alternative to the classical complement pathway and is activated by the binding of mannose-binding lectin (MBL) or ficolins to specific carbohydrate patterns on the surface of pathogens. The alternative pathway plays a role in the clearance of pathogens and the recruitment of immune cells to the site of infection. It is also involved in the formation of the membrane attack complex (MAC), which can directly kill certain types of pathogens.

The complement pathway, classical, is a series of proteins that are part of the body's immune system. It is one of three pathways that work together to help the body fight off infections and remove damaged cells. The classical pathway begins when antibodies bind to specific proteins on the surface of a pathogen, such as a virus or bacteria. This binding triggers a series of reactions that ultimately lead to the destruction of the pathogen. The complement pathway is an important part of the body's defense against infection and is also involved in the inflammatory response.

Complement C8 is a protein that is part of the complement system, which is a group of proteins that work together to help the immune system fight off infections. The complement system is made up of several proteins, including C8, that are present in the blood and other body fluids. When the immune system detects the presence of a pathogen, such as a virus or bacteria, it triggers the complement system to activate and help destroy the pathogen. C8 plays a role in this process by helping to form a membrane attack complex, which is a structure that punctures the cell membrane of the pathogen, causing it to burst and be destroyed.

Complement C1 is a protein complex that plays a central role in the complement system, which is a part of the immune system that helps to defend the body against infections. C1 is composed of three proteins: C1q, C1r, and C1s. When a pathogen enters the body, the complement system is activated, and C1 binds to the pathogen's surface. This binding triggers a series of chemical reactions that ultimately lead to the destruction of the pathogen. C1 is also involved in the regulation of the complement system, helping to prevent excessive activation and damage to healthy cells. Deficiencies in C1 can lead to increased susceptibility to infections and other immune-related disorders.

Receptors, Complement 3b (CR3b) are a type of immune cell receptor found on the surface of certain white blood cells, such as neutrophils and macrophages. These receptors bind to complement protein C3b, which is a component of the complement system, a part of the immune system that helps to identify and destroy pathogens. CR3b receptors play an important role in the immune response by recognizing and binding to C3b-coated pathogens, such as bacteria and viruses. This binding triggers a series of events that lead to the destruction of the pathogen, including the release of chemicals that attract other immune cells to the site of infection and the formation of a membrane attack complex that can directly damage the pathogen. CR3b receptors are also involved in the process of phagocytosis, in which immune cells engulf and destroy pathogens. By binding to C3b-coated pathogens, CR3b receptors help to facilitate the engulfment of the pathogen by the immune cell. In addition to their role in the immune response, CR3b receptors have been implicated in a number of other physiological processes, including the regulation of blood clotting and the clearance of apoptotic cells (cells that are undergoing programmed cell death).

Complement Factor H (CFH) is a protein that plays a critical role in the complement system, which is a part of the immune system that helps to defend the body against infections. CFH is a soluble protein that is present in the blood and helps to regulate the activity of the complement system by inhibiting the formation of the membrane attack complex (MAC), which is a group of proteins that can cause damage to cells and tissues. CFH is also involved in the regulation of inflammation and the immune response, and it has been implicated in a number of diseases, including age-related macular degeneration (AMD), a common eye disorder that can lead to vision loss, and atypical hemolytic uremic syndrome (aHUS), a rare and life-threatening disorder that can cause kidney failure and other complications. In addition to its role in the complement system, CFH has also been shown to have anti-inflammatory and anti-apoptotic effects, and it may play a role in the development of other diseases, such as cancer and neurodegenerative disorders.

Complement C5b is a protein that plays a central role in the complement system, which is a part of the immune system that helps to defend the body against infections. C5b is produced when the complement system is activated, and it is involved in the formation of a membrane attack complex (MAC) that can cause lysis (rupture) of cells. The MAC is formed by the assembly of multiple complement proteins, including C5b, on the surface of a pathogen or infected cell. The MAC can then create pores in the cell membrane, leading to the influx of water and ions and ultimately causing the cell to burst. C5b is also involved in the recruitment of immune cells to the site of infection and in the clearance of immune complexes from the body.

Complement C2a is a fragment of the complement protein C2, which is a part of the complement system in the human body. The complement system is a group of proteins that work together to help the immune system fight off infections and remove damaged cells and other foreign substances from the body. C2 is a large protein that is produced by the liver and other cells in the body. When the complement system is activated, C2 is cleaved into two fragments: C2a and C2b. C2a is a smaller fragment that is involved in the early stages of the complement system's response to an infection or injury. C2a plays a role in the formation of the membrane attack complex (MAC), which is a group of proteins that can puncture the membranes of bacteria and other pathogens, killing them. C2a is also involved in the recruitment of immune cells to the site of an infection or injury, and in the activation of other components of the complement system. In the medical field, C2a is sometimes measured as a marker of complement system activation. Abnormal levels of C2a may be associated with certain medical conditions, such as autoimmune diseases, infections, and certain types of cancer.

The receptor for Anaphylatoxin C5a, also known as C5aR, is a protein found on the surface of various cells in the immune system. It is a G protein-coupled receptor that binds to the inflammatory mediator Anaphylatoxin C5a, which is produced during the complement cascade, a series of chemical reactions that occurs in response to an infection or injury. When C5a binds to its receptor, it triggers a cascade of intracellular signaling events that activate various immune cells, such as neutrophils and macrophages, and promote inflammation. This can lead to the recruitment of immune cells to the site of infection or injury, the release of inflammatory mediators, and the destruction of pathogens. C5aR is also expressed on non-immune cells, such as endothelial cells and epithelial cells, and can play a role in regulating various physiological processes, such as blood pressure and inflammation. In some cases, excessive activation of C5aR can lead to the development of various inflammatory diseases, such as atherosclerosis and asthma.

Complement activating enzymes are a group of proteins that are part of the complement system, a complex series of proteins that plays a crucial role in the immune response. These enzymes are responsible for activating the complement system, which helps to destroy pathogens and remove damaged cells from the body. There are several different complement activating enzymes, including: 1. Complement C1: This enzyme is composed of three subunits, C1q, C1r, and C1s. When it binds to a pathogen or damaged cell, it triggers a cascade of reactions that ultimately leads to the destruction of the target. 2. Mannose-binding lectin (MBL): This enzyme is part of the lectin pathway of the complement system, which is activated by the presence of specific carbohydrates on the surface of pathogens. MBL binds to these carbohydrates and triggers a series of reactions that lead to the destruction of the pathogen. 3. Complement C3 convertase: This enzyme is responsible for converting the complement protein C3 into C3a and C3b, which are key components of the complement system. C3a is an anaphylatoxin that helps to recruit immune cells to the site of infection, while C3b helps to bind the pathogen to immune cells and facilitate its destruction. Complement activating enzymes play a critical role in the immune response and are involved in a wide range of diseases, including autoimmune disorders, infections, and cancer.

Complement inactivating agents are substances that interfere with the complement system, a part of the immune system that helps to destroy pathogens and remove damaged cells. The complement system consists of a series of proteins that are activated in response to an infection or injury. Complement inactivating agents can either prevent the activation of the complement system or inhibit the activity of the complement proteins once they have been activated. There are several types of complement inactivating agents, including: 1. Complement inhibitors: These are proteins that bind to and inhibit the activity of complement proteins. Examples include C1 esterase inhibitors, which prevent the activation of the complement component C1, and factor H, which inhibits the activity of C3 convertase, an enzyme that cleaves the complement protein C3. 2. Complement receptor blockers: These are molecules that bind to complement receptors on the surface of immune cells and prevent them from activating the complement system. Examples include soluble complement receptor 1 (sCR1), which binds to C3b, a complement protein that is involved in the opsonization of pathogens, and complement receptor 2 (CR2), which binds to C3d, a complement protein that is involved in the activation of B cells. 3. Complement depleting agents: These are substances that remove complement proteins from the blood or tissue. Examples include eculizumab, a monoclonal antibody that targets complement protein C5 and is used to treat paroxysmal nocturnal hemoglobinuria (PNH), a rare blood disorder, and rituximab, a monoclonal antibody that targets CD20, a protein on the surface of B cells, and is used to treat certain types of cancer. Complement inactivating agents are used to treat a variety of conditions, including autoimmune diseases, inflammatory disorders, and certain types of cancer. They can help to reduce inflammation and prevent the destruction of healthy cells by the immune system. However, they can also increase the risk of infections, as the complement system plays an important role in the body's defense against pathogens.

The Complement Hemolytic Activity Assay (CH50) is a laboratory test used to measure the ability of the complement system to lyse (break down) red blood cells. The complement system is a group of proteins that work together to help the body fight infections and remove damaged cells. The CH50 test is often used to diagnose and monitor certain types of autoimmune diseases, such as lupus, and to evaluate the effectiveness of certain medications that affect the complement system. The test involves mixing a sample of a person's blood with a solution that contains complement proteins and measuring the amount of hemolysis (breakdown of red blood cells) that occurs over time. The results of the test can help healthcare providers determine the underlying cause of a person's symptoms and guide treatment decisions.

Complement C1 Inactivator Proteins (C1INH) are a group of proteins that play a crucial role in regulating the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. The complement system consists of a series of proteins that work together to identify and eliminate pathogens, such as bacteria and viruses. C1INH is a plasma protein that is produced by the liver and circulates in the bloodstream. It functions as an inhibitor of the complement system by binding to and neutralizing the activity of complement protein C1, which is the first protein activated in the complement cascade. By inhibiting the activity of C1, C1INH helps to prevent the overactivation of the complement system, which can lead to tissue damage and inflammation. Deficiencies or mutations in C1INH can lead to a condition called hereditary angioedema (HAE), which is characterized by recurrent episodes of swelling in the face, extremities, and other parts of the body. HAE can be life-threatening if left untreated, as it can cause difficulty breathing and other serious complications. Treatment for HAE typically involves the administration of C1INH replacement therapy, which can help to prevent or reduce the severity of attacks.

Receptors, Complement 3d, also known as C3d receptors, are proteins found on the surface of certain immune cells, such as B cells and macrophages. These receptors bind to the complement protein C3d, which is generated during the complement cascade, a series of chemical reactions that occurs in response to an infection or injury. The binding of C3d to its receptor on immune cells triggers a signaling cascade that activates the immune response. This can include the activation of B cells, which leads to the production of antibodies, and the recruitment of immune cells to the site of infection or injury. C3d receptors are important for the proper functioning of the immune system, as they help to amplify and direct the immune response. Mutations in the genes encoding C3d receptors have been associated with various immune disorders, including autoimmune diseases and infections.

Anaphylatoxins are a group of small proteins that are released by mast cells and basophils in response to an allergen or other inflammatory stimulus. They are also known as complement system activation products because they are produced as part of the complement system, a complex series of proteins that plays a role in the immune response. There are five main anaphylatoxins: histamine, heparin, platelet-activating factor (PAF), leukotrienes, and prostaglandins. These molecules act on various cells in the body, including blood vessels, smooth muscle cells, and immune cells, to cause a range of symptoms, including itching, redness, swelling, and constriction of blood vessels. Anaphylatoxins are involved in many allergic reactions, including hay fever, food allergies, and asthma. They can also play a role in other inflammatory conditions, such as sepsis and shock. Treatment for anaphylatoxin reactions typically involves antihistamines, corticosteroids, and other medications to reduce inflammation and counteract the effects of the anaphylatoxins.

Complement fixation tests are a type of serological test used in the medical field to detect the presence of specific antibodies in a patient's blood. These tests are based on the principle that antibodies can bind to specific antigens, causing a change in the complement system, a group of proteins that play a role in the immune response. In a complement fixation test, a known amount of antigen is mixed with a patient's serum, and the mixture is then incubated to allow the antibodies in the serum to bind to the antigen. The bound antibodies then activate the complement system, which leads to the formation of a visible precipitate or clot. The amount of precipitate or clot formed is proportional to the amount of antibodies present in the serum. Complement fixation tests are used to diagnose a variety of infectious diseases, including syphilis, rheumatic fever, and Lyme disease. They are also used to detect the presence of certain types of cancer, such as Hodgkin's lymphoma and multiple myeloma. These tests are generally considered to be highly specific, meaning that they are less likely to produce false-positive results than other types of serological tests. However, they may be less sensitive, meaning that they may produce false-negative results in some cases.

Complement Factor D (CFD) is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and remove damaged cells. CFD is also known as complement factor Bb or membrane attack complex (MAC) convertase. CFD is synthesized in the liver and circulates in the blood as an inactive form. When it encounters a pathogen or damaged cell, it is activated by proteolytic cleavage, which generates two active fragments: C3 convertase and C5 convertase. These convertases cleave other complement proteins, leading to the formation of the membrane attack complex (MAC), which can directly lyse the pathogen or damaged cell. In addition to its role in the complement system, CFD has also been implicated in the development of various diseases, including age-related macular degeneration, atherosclerosis, and systemic lupus erythematosus. Therefore, CFD is an important target for the development of new therapies for these diseases.

Complement Factor I (C1) is a protein complex that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections and remove damaged cells. C1 is composed of three subunits: C1q, C1r, and C1s. When a pathogen enters the body, it triggers the activation of the complement system, which leads to the formation of a cascade of proteins that ultimately results in the destruction of the pathogen. C1 is the first protein in this cascade to be activated, and it plays a critical role in identifying and binding to the pathogen. Once C1 binds to the pathogen, it triggers the activation of C1r and C1s, which then cleave and activate other complement proteins, leading to the formation of a membrane attack complex (MAC) that can directly destroy the pathogen. C1 also plays a role in regulating the complement system by inhibiting its activation in the absence of a pathogen. In summary, Complement Factor I (C1) is a protein complex that plays a critical role in the complement system, which helps to defend the body against infections and remove damaged cells. It is the first protein in the complement cascade to be activated and plays a critical role in identifying and binding to pathogens.

Complement C4b-Binding Protein (C4BP) is a plasma protein that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections. C4BP is a soluble protein that binds to the complement protein C4b, which is a key component of the complement cascade. The complement system is a complex network of proteins that work together to identify and eliminate pathogens, such as bacteria and viruses, from the body. When a pathogen enters the body, the complement system is activated, leading to the production of various proteins that help to destroy the pathogen. C4BP plays a critical role in regulating the complement system by inhibiting the activity of the complement protein C3 convertase, which is responsible for cleaving the complement protein C3 into C3a and C3b. C3b is an important component of the complement cascade that helps to opsonize pathogens and promote their clearance by phagocytic cells. In addition to its role in regulating the complement system, C4BP has been implicated in a number of other biological processes, including inflammation, coagulation, and the regulation of immune cell function. Dysregulation of C4BP has been associated with a number of diseases, including autoimmune disorders, thrombotic disorders, and infections.

Complement C3b Inactivator Proteins (C3bI) are a group of proteins that play a role in regulating the complement system, which is a part of the immune system that helps to defend the body against infections. The complement system is activated when pathogens enter the body, and it works by tagging pathogens with molecules that mark them for destruction by immune cells. C3bI proteins help to inactivate a specific complement protein called C3b, which is involved in this tagging process. By inactivating C3b, C3bI proteins help to prevent the overactivation of the complement system, which can cause damage to healthy cells and tissues. C3bI proteins are important for maintaining the balance of the immune system and preventing it from attacking the body's own cells.

CD55 is a protein that is expressed on the surface of many different types of cells in the body, including immune cells, blood cells, and cells in the nervous system. It is also known as decay-accelerating factor (DAF) because it has the ability to accelerate the decay of complement proteins, which are part of the body's immune system. Antigens, CD55 refers to molecules that bind to the CD55 protein on the surface of cells. These antigens can be recognized by the immune system as foreign and can trigger an immune response. In some cases, the immune system may attack cells that express CD55 as a result of an autoimmune disorder, which is a condition in which the immune system mistakenly attacks healthy cells in the body.

Complement C3-C5 convertases, classical pathway refers to a group of enzymes that play a crucial role in the complement system, a part of the immune system that helps to defend the body against infections. The classical pathway is one of three pathways that activate the complement system, and it involves the activation of the complement protein C3. The complement C3-C5 convertases are responsible for cleaving and activating the complement proteins C3 and C5, which are key components of the complement system. These enzymes are formed when the complement proteins C1, C4, and C2 are activated by antibodies or immune complexes on the surface of pathogens or damaged cells. Once activated, the complement C3-C5 convertases cleave C3 into C3a and C3b, which can then bind to pathogens or damaged cells and mark them for destruction by immune cells. C3b can also bind to C4b2a, forming the C3 convertase, which cleaves C3 into C3a and C3b and can further cleave C5 into C5a and C5b, forming the C5 convertase. The C5 convertase cleaves C5 into C5a and C5b, which can then form the membrane attack complex (MAC), a pore that inserts into the membrane of pathogens or damaged cells, leading to their destruction. Overall, the complement C3-C5 convertases, classical pathway play a critical role in the immune response by activating the complement system and marking pathogens or damaged cells for destruction.

Complement C2b is a protein fragment that is generated when the complement protein C2 is cleaved by the enzyme C1s or C1r. The complement system is a part of the immune system that helps to clear pathogens and damaged cells from the body. C2b is an intermediate fragment in the activation of the complement cascade, which is a series of chemical reactions that leads to the formation of a membrane attack complex (MAC) and the destruction of the target cell. C2b is involved in the recruitment of immune cells to the site of infection or injury and plays a role in the inflammatory response. It is also involved in the regulation of the complement system and can be measured in the blood as a marker of complement activation.

CD59 is a protein that is expressed on the surface of many types of cells in the body, including red blood cells, white blood cells, and platelets. It is a member of the complement regulatory protein family, which helps to control the activation of the complement system, a part of the immune system that helps to fight off infections. Antigens, CD59 refers to molecules that bind to the CD59 protein on the surface of cells. These antigens can be recognized by the immune system as foreign and can trigger an immune response, leading to the production of antibodies that can bind to and neutralize the antigens. In some cases, the immune system may mistakenly recognize CD59 itself as an antigen and attack cells that express it, leading to a condition known as autoimmune hemolytic anemia, in which the immune system destroys red blood cells.

Cobra venoms are toxic substances produced by cobras, a group of venomous snakes found in various parts of the world. These venoms contain a complex mixture of proteins, enzymes, and other molecules that can cause a range of physiological effects in humans and other animals. The effects of cobra venom can vary depending on the species of cobra, the dose of venom injected, and the individual's health status. Some common effects of cobra venom include pain, swelling, and muscle spasms at the site of the bite, as well as more systemic effects such as nausea, vomiting, dizziness, and difficulty breathing. In the medical field, cobra venom is studied for its potential therapeutic uses, such as in the development of new drugs for pain management, anti-inflammatory treatments, and cancer therapies. However, cobra venom is also a significant health hazard, and bites from venomous cobras can be life-threatening if not treated promptly and appropriately. Treatment typically involves antivenom therapy, which is designed to neutralize the venom and prevent its harmful effects on the body.

An antigen-antibody complex is a type of immune complex that forms when an antigen (a foreign substance that triggers an immune response) binds to an antibody (a protein produced by the immune system to recognize and neutralize antigens). When an antigen enters the body, it is recognized by specific antibodies that bind to it, forming an antigen-antibody complex. This complex can then be targeted by other immune cells, such as phagocytes, which engulf and destroy the complex. Antigen-antibody complexes can also deposit in tissues, leading to inflammation and damage. This can occur in conditions such as immune complex-mediated diseases, where the immune system mistakenly attacks healthy tissues that have been coated with antigens and antibodies. Overall, the formation of antigen-antibody complexes is a normal part of the immune response, but when it becomes dysregulated, it can lead to a variety of medical conditions.

Steroid 21-Hydroxylase is an enzyme that plays a crucial role in the biosynthesis of steroid hormones in the human body. It is located in the mitochondria of various cells, including adrenal gland cells, and is responsible for converting cholesterol into various steroid hormones, such as cortisol, aldosterone, and androgens. The enzyme catalyzes the hydroxylation of the 21st carbon atom of the steroid molecule, which is a critical step in the biosynthesis of these hormones. Without sufficient activity of the enzyme, the production of these hormones is impaired, leading to a variety of medical conditions. In particular, a deficiency in steroid 21-hydroxylase can result in a group of genetic disorders known as congenital adrenal hyperplasia (CAH). CAH is a common inherited disorder that affects the adrenal glands and can cause a range of symptoms, including ambiguous genitalia in newborns, salt-wasting crises, and hormonal imbalances. Treatment for CAH typically involves hormone replacement therapy to correct the imbalances caused by the enzyme deficiency.

Complement C3-C5 convertases, alternative pathway refers to a group of enzymes that play a crucial role in the complement system, a part of the immune system that helps to defend the body against infections. These enzymes are involved in the activation of the alternative pathway of the complement system, which is one of three pathways that work together to destroy pathogens and remove damaged cells from the body. The alternative pathway is activated when the complement protein C3 binds to the surface of a pathogen or damaged cell. This binding triggers a series of reactions that ultimately lead to the formation of the C3-C5 convertases, which cleave and activate the complement proteins C3 and C5. The activated C5 protein then forms a complex with other complement proteins that can directly destroy the pathogen or mark it for destruction by other immune cells. The complement C3-C5 convertases, alternative pathway are important for the proper functioning of the immune system and are involved in a variety of physiological processes, including inflammation, tissue repair, and the clearance of immune complexes. Defects in the complement system can lead to a variety of disorders, including complement deficiency, atypical hemolytic uremic syndrome, and age-related macular degeneration.

Complement C1 Inhibitor Protein (C1INH) is a plasma protein that plays a crucial role in regulating the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. C1INH acts as an inhibitor of the complement component C1, which is the first enzyme activated in the complement cascade. When C1 is activated, it triggers a series of reactions that can lead to inflammation and tissue damage. C1INH binds to C1 and prevents it from activating, thus inhibiting the complement cascade and reducing inflammation. C1INH deficiency or dysfunction can lead to a condition called hereditary angioedema (HAE), which is characterized by recurrent episodes of swelling in the face, extremities, and other parts of the body. HAE can be life-threatening if left untreated.

Immunoglobulin G (IgG) is a type of protein that is produced by the immune system in response to the presence of foreign substances, such as bacteria, viruses, and toxins. It is the most abundant type of immunoglobulin in the blood and is responsible for the majority of the body's defense against infections. IgG is produced by B cells, which are a type of white blood cell that plays a key role in the immune response. When a B cell encounters a foreign substance, it produces IgG antibodies that can recognize and bind to the substance, marking it for destruction by other immune cells. IgG antibodies can also be transferred from mother to child through the placenta during pregnancy, providing the baby with some protection against infections during the first few months of life. In addition, some vaccines contain IgG antibodies to help stimulate the immune system and provide protection against specific diseases. Overall, IgG is an important component of the immune system and plays a critical role in protecting the body against infections and diseases.

Hemolysis is the breakdown of red blood cells (RBCs) in the bloodstream. This process can occur due to various factors, including mechanical stress, exposure to certain medications or toxins, infections, or inherited genetic disorders. When RBCs are damaged or destroyed, their contents, including hemoglobin, are released into the bloodstream. Hemoglobin is a protein that carries oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. When hemoglobin is released into the bloodstream, it can cause the blood to appear dark brown or black, a condition known as hemoglobinuria. Hemolysis can lead to a variety of symptoms, including jaundice (yellowing of the skin and eyes), fatigue, shortness of breath, abdominal pain, and dark urine. In severe cases, hemolysis can cause life-threatening complications, such as kidney failure or shock. Treatment for hemolysis depends on the underlying cause. In some cases, treatment may involve medications to slow down the breakdown of RBCs or to remove excess hemoglobin from the bloodstream. In other cases, treatment may involve blood transfusions or other supportive therapies to manage symptoms and prevent complications.

Complement C3 convertase, alternative pathway is an enzyme that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections. The complement system is made up of a series of proteins that work together to identify and destroy foreign substances, such as bacteria and viruses. The alternative pathway is one of three pathways that can activate the complement system. It is activated when the complement protein C3 is cleaved into two fragments, C3a and C3b, by the enzyme complement C3 convertase, alternative pathway. This cleavage event triggers a cascade of reactions that ultimately leads to the formation of the membrane attack complex (MAC), which can destroy the cell membrane of invading pathogens. Complement C3 convertase, alternative pathway is composed of two proteins, C3b and factor B, which are activated by the binding of the complement protein C3 to the surface of a pathogen. Once activated, the enzyme cleaves C3 into C3a and C3b, which then triggers the rest of the complement cascade. In summary, complement C3 convertase, alternative pathway is an enzyme that plays a critical role in activating the complement system and helping to defend the body against infections.

Complement C5 convertase, classical pathway is an enzyme that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections. The classical pathway is one of three pathways that activate the complement system, and it is triggered by the binding of antibodies to the surface of pathogens or damaged cells. The complement C5 convertase enzyme is responsible for cleaving the complement protein C5 into two fragments, C5a and C5b. C5a is a potent inflammatory mediator that attracts immune cells to the site of infection or injury, while C5b is a key component of the membrane attack complex (MAC), which forms a pore in the membrane of pathogens or damaged cells, leading to their destruction. In summary, the complement C5 convertase, classical pathway is a critical enzyme in the complement system that helps to activate the immune response against pathogens and damaged cells.

Complement C3 convertase, classical pathway is an enzyme that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections. The classical pathway is one of three pathways that activate the complement system, and it involves the activation of the complement protein C3. The complement C3 convertase enzyme is responsible for cleaving the complement protein C3 into two fragments: C3a and C3b. C3a is a small peptide that acts as a signaling molecule, activating immune cells and promoting inflammation. C3b is a larger fragment that binds to the surface of pathogens, marking them for destruction by immune cells. The formation of complement C3 convertase is initiated by the binding of the complement protein C1q to antibodies that are bound to the surface of a pathogen. This binding triggers a series of reactions that ultimately lead to the activation of complement C3 convertase. Overall, the complement C3 convertase, classical pathway plays a critical role in the immune response to infections by activating the complement system and promoting the destruction of pathogens.

CD46 is a protein found on the surface of many different types of cells in the body, including immune cells, epithelial cells, and endothelial cells. It is a member of the complement regulatory protein family and plays a role in regulating the immune system's response to infections and other stimuli. Antigens, CD46 refers to molecules that bind to the CD46 protein on the surface of cells. These antigens can be recognized by the immune system as foreign and trigger an immune response. In some cases, the immune system may mistakenly attack cells that express CD46, leading to autoimmune diseases such as lupus or Goodpasture's syndrome. CD46 is also a target for certain viruses, such as measles virus, which uses it to enter and infect cells. Vaccines against measles virus often contain a small amount of inactivated or weakened measles virus that binds to CD46 on cells, triggering an immune response without causing the disease. Overall, CD46 plays an important role in regulating the immune system and is a target for both the immune system and certain viruses.

Opsonin proteins are a type of immune system protein that play a role in the process of phagocytosis, which is the process by which immune cells called phagocytes engulf and destroy foreign particles, such as bacteria or viruses. Opsonins bind to the surface of these foreign particles, marking them for destruction by phagocytes. This process is known as opsonization. There are several different types of opsonin proteins, including antibodies, complement proteins, and mannose-binding lectin (MBL). Antibodies are proteins produced by the immune system in response to the presence of a foreign substance, such as a virus or bacteria. They bind to specific molecules on the surface of these foreign particles, marking them for destruction by phagocytes. Complement proteins are a group of proteins that are part of the innate immune system. They are produced by the liver and other organs and circulate in the blood. Complement proteins can bind to foreign particles and mark them for destruction by phagocytes. MBL is a protein that is produced by the liver and circulates in the blood. It binds to specific molecules on the surface of foreign particles, marking them for destruction by phagocytes. Opsonin proteins play an important role in the immune system by helping to identify and destroy foreign particles. They are an important part of the body's defense against infection and disease.

Blood proteins are proteins that are found in the blood plasma of humans and other animals. They play a variety of important roles in the body, including transporting oxygen and nutrients, regulating blood pressure, and fighting infections. There are several different types of blood proteins, including albumin, globulins, and fibrinogen. Each type of blood protein has a specific function and is produced by different cells in the body. For example, albumin is produced by the liver and helps to maintain the osmotic pressure of the blood, while globulins are produced by the immune system and help to fight infections. Fibrinogen, on the other hand, is produced by the liver and is involved in the clotting of blood.

Systemic Lupus Erythematosus (SLE) is a chronic autoimmune disorder that affects multiple organs and systems in the body. It is characterized by the production of autoantibodies that attack healthy cells and tissues, leading to inflammation and damage. The symptoms of SLE can vary widely and may include joint pain and swelling, skin rashes, fatigue, fever, and kidney problems. Other possible symptoms may include chest pain, shortness of breath, headaches, and memory problems. SLE can affect people of all ages and ethnicities, but it is more common in women than in men. There is no known cure for SLE, but treatment can help manage symptoms and prevent complications. Treatment may include medications to reduce inflammation, suppress the immune system, and prevent blood clots. In some cases, hospitalization may be necessary to manage severe symptoms or complications.

Complement C5 convertase, alternative pathway is an enzyme that plays a crucial role in the complement system, which is a part of the immune system that helps to defend the body against infections. The complement system is activated when pathogens, such as bacteria or viruses, enter the body. The alternative pathway is one of three pathways that can activate the complement system, and it is activated by the binding of a protein called C3 to the surface of a pathogen. The complement C5 convertase, alternative pathway is responsible for cleaving the complement protein C5 into two fragments, C5a and C5b. C5a is a potent inflammatory mediator that helps to recruit immune cells to the site of infection, while C5b is a key component of the membrane attack complex (MAC), which is a group of proteins that can form pores in the membrane of a pathogen, leading to its destruction. Disruptions in the complement system, including problems with the complement C5 convertase, alternative pathway, can lead to a variety of medical conditions, including autoimmune diseases, infections, and cancer.

In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.

The complement pathway, mannose-binding lectin (MBL) is a part of the innate immune system that helps to defend the body against infections. It is a complex protein that recognizes and binds to specific carbohydrates on the surface of microorganisms, such as bacteria and viruses. When MBL binds to these carbohydrates, it triggers a cascade of chemical reactions that ultimately leads to the destruction of the microorganism. The complement pathway, MBL is an important part of the body's defense against infections and plays a role in the development of certain autoimmune diseases.

Properdin is a protein that plays a crucial role in the innate immune system. It is produced by the liver and circulates in the blood. Properdin is a component of the alternative pathway of complement activation, which is a series of chemical reactions that help to destroy invading pathogens. Properdin enhances the ability of the complement system to activate the alternative pathway by binding to the surface of pathogens and promoting the assembly of a complex called the "membrane attack complex" (MAC). The MAC is a group of proteins that form a pore in the membrane of the pathogen, leading to its destruction. Properdin is also involved in the regulation of the complement system, helping to prevent excessive activation and damage to host cells. It has been implicated in a number of autoimmune and inflammatory diseases, including lupus, rheumatoid arthritis, and vasculitis.

Complement C5a, des-Arginine is a fragment of the complement protein C5 that is generated during the activation of the complement system. It is a potent mediator of inflammation and immune responses, and plays a role in the recruitment of immune cells to sites of infection or injury. Des-Arginine refers to the removal of an arginine residue from the C5a molecule, which can affect its biological activity. Complement C5a, des-Arginine is often used as a biomarker of complement activation in various diseases, including sepsis, autoimmune disorders, and cardiovascular disease.

Macrophage-1 Antigen (Mac-1) is a protein that is expressed on the surface of certain immune cells, including macrophages and neutrophils. It is also known as CD11b/CD18 or CR3 (complement receptor 3). Mac-1 plays a role in the immune system by mediating the adhesion and migration of immune cells to sites of inflammation or infection. It also plays a role in the recognition and phagocytosis of pathogens by immune cells. In the medical field, Mac-1 is often used as a diagnostic marker for certain diseases, such as sepsis, and as a target for the development of new therapies for inflammatory and infectious diseases.

In the medical field, a base sequence refers to the specific order of nucleotides (adenine, thymine, cytosine, and guanine) that make up the genetic material (DNA or RNA) of an organism. The base sequence determines the genetic information encoded within the DNA molecule and ultimately determines the traits and characteristics of an individual. The base sequence can be analyzed using various techniques, such as DNA sequencing, to identify genetic variations or mutations that may be associated with certain diseases or conditions.

Membranoproliferative glomerulonephritis (MPGN) is a type of kidney disease that affects the glomeruli, which are the tiny filtering units in the kidneys. In MPGN, there is inflammation and proliferation of cells in the glomerular basement membrane, which can lead to thickening and scarring of the membrane. This can impair the glomeruli's ability to filter waste products from the blood, leading to a buildup of toxins in the body. MPGN can be caused by a variety of factors, including infections, autoimmune disorders, and certain medications. Treatment typically involves managing symptoms and addressing the underlying cause of the disease.

Immunoglobulin M (IgM) is a type of antibody that is produced by B cells in response to an infection or foreign substance. It is the first antibody to be produced during an immune response and is present in the blood and other body fluids in relatively low concentrations. IgM antibodies are large, Y-shaped molecules that can bind to multiple antigens at once, making them highly effective at neutralizing pathogens and marking them for destruction by other immune cells. They are also able to activate the complement system, a series of proteins that can directly destroy pathogens or mark them for destruction by immune cells. IgM antibodies are often used as a diagnostic tool in medical testing, as they are typically the first antibodies to be produced in response to a new infection. They can also be used to monitor the effectiveness of vaccines and to detect the presence of certain diseases, such as viral or bacterial infections, autoimmune disorders, and certain types of cancer.

Glomerulonephritis is a type of kidney disease that involves inflammation of the glomeruli, which are tiny blood vessels in the kidneys responsible for filtering waste products from the blood. This inflammation can cause damage to the glomeruli, leading to a range of symptoms and complications. There are many different types of glomerulonephritis, which can be classified based on their underlying cause. Some common causes include infections (such as strep throat or hepatitis B), autoimmune disorders (such as lupus or rheumatoid arthritis), and certain medications or toxins. Symptoms of glomerulonephritis can vary depending on the severity and underlying cause of the condition. Common symptoms may include blood in the urine, swelling in the legs or feet, high blood pressure, fatigue, and changes in urine output. Treatment for glomerulonephritis typically involves managing symptoms and addressing the underlying cause of the inflammation. This may include medications to reduce inflammation, control blood pressure, and prevent further damage to the kidneys. In some cases, more aggressive treatments such as dialysis or kidney transplantation may be necessary.

Arteriolosclerosis is a medical condition characterized by the thickening and hardening of the walls of small arteries, known as arterioles. This condition is also referred to as arteriolar sclerosis or arteriolar narrowing. The thickening and hardening of the arterioles can occur due to a variety of factors, including aging, high blood pressure, diabetes, high cholesterol, smoking, and obesity. As the walls of the arterioles become thicker and harder, they can become narrower, which can restrict blood flow to the tissues and organs they supply. Arteriolosclerosis can lead to a range of health problems, including high blood pressure, heart disease, stroke, and kidney disease. Treatment for arteriolosclerosis typically involves managing the underlying risk factors, such as controlling blood pressure, blood sugar, and cholesterol levels, as well as making lifestyle changes such as quitting smoking and exercising regularly. In some cases, medications may also be prescribed to help manage the condition.

Monoclonal antibodies (mAbs) are laboratory-made proteins that can mimic the immune system's ability to fight off harmful pathogens, such as viruses and bacteria. They are produced by genetically engineering cells to produce large quantities of a single type of antibody, which is specific to a particular antigen (a molecule that triggers an immune response). In the medical field, monoclonal antibodies are used to treat a variety of conditions, including cancer, autoimmune diseases, and infectious diseases. They can be administered intravenously, intramuscularly, or subcutaneously, depending on the condition being treated. Monoclonal antibodies work by binding to specific antigens on the surface of cells or pathogens, marking them for destruction by the immune system. They can also block the activity of specific molecules involved in disease processes, such as enzymes or receptors. Overall, monoclonal antibodies have revolutionized the treatment of many diseases, offering targeted and effective therapies with fewer side effects than traditional treatments.

Autoantibodies are antibodies that are produced by the immune system against the body's own cells, tissues, or organs. In other words, they are antibodies that mistakenly target and attack the body's own components instead of foreign invaders like viruses or bacteria. Autoantibodies can be present in people with various medical conditions, including autoimmune diseases such as rheumatoid arthritis, lupus, and multiple sclerosis. They can also be found in people with certain infections, cancer, and other diseases. Autoantibodies can cause damage to the body's own cells, tissues, or organs, leading to inflammation, tissue destruction, and other symptoms. They can also interfere with the normal functioning of the body's systems, such as the nervous system, digestive system, and cardiovascular system. Diagnosis of autoantibodies is typically done through blood tests, which can detect the presence of specific autoantibodies in the blood. Treatment for autoimmune diseases that involve autoantibodies may include medications to suppress the immune system, such as corticosteroids or immunosuppressants, as well as other therapies to manage symptoms and prevent complications.

In the medical field, "Cells, Cultured" refers to cells that have been grown and maintained in a controlled environment outside of their natural biological context, typically in a laboratory setting. This process is known as cell culture and involves the isolation of cells from a tissue or organism, followed by their growth and proliferation in a nutrient-rich medium. Cultured cells can be derived from a variety of sources, including human or animal tissues, and can be used for a wide range of applications in medicine and research. For example, cultured cells can be used to study the behavior and function of specific cell types, to develop new drugs and therapies, and to test the safety and efficacy of medical products. Cultured cells can be grown in various types of containers, such as flasks or Petri dishes, and can be maintained at different temperatures and humidity levels to optimize their growth and survival. The medium used to culture cells typically contains a combination of nutrients, growth factors, and other substances that support cell growth and proliferation. Overall, the use of cultured cells has revolutionized medical research and has led to many important discoveries and advancements in the field of medicine.

In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.

In the medical field, a cell line refers to a group of cells that have been derived from a single parent cell and have the ability to divide and grow indefinitely in culture. These cells are typically grown in a laboratory setting and are used for research purposes, such as studying the effects of drugs or investigating the underlying mechanisms of diseases. Cell lines are often derived from cancerous cells, as these cells tend to divide and grow more rapidly than normal cells. However, they can also be derived from normal cells, such as fibroblasts or epithelial cells. Cell lines are characterized by their unique genetic makeup, which can be used to identify them and compare them to other cell lines. Because cell lines can be grown in large quantities and are relatively easy to maintain, they are a valuable tool in medical research. They allow researchers to study the effects of drugs and other treatments on specific cell types, and to investigate the underlying mechanisms of diseases at the cellular level.

In the medical field, a peptide fragment refers to a short chain of amino acids that are derived from a larger peptide or protein molecule. Peptide fragments can be generated through various techniques, such as enzymatic digestion or chemical cleavage, and are often used in diagnostic and therapeutic applications. Peptide fragments can be used as biomarkers for various diseases, as they may be present in the body at elevated levels in response to specific conditions. For example, certain peptide fragments have been identified as potential biomarkers for cancer, neurodegenerative diseases, and cardiovascular disease. In addition, peptide fragments can be used as therapeutic agents themselves. For example, some peptide fragments have been shown to have anti-inflammatory or anti-cancer properties, and are being investigated as potential treatments for various diseases. Overall, peptide fragments play an important role in the medical field, both as diagnostic tools and as potential therapeutic agents.

In the medical field, "Disease Models, Animal" refers to the use of animals to study and understand human diseases. These models are created by introducing a disease or condition into an animal, either naturally or through experimental manipulation, in order to study its progression, symptoms, and potential treatments. Animal models are used in medical research because they allow scientists to study diseases in a controlled environment and to test potential treatments before they are tested in humans. They can also provide insights into the underlying mechanisms of a disease and help to identify new therapeutic targets. There are many different types of animal models used in medical research, including mice, rats, rabbits, dogs, and monkeys. Each type of animal has its own advantages and disadvantages, and the choice of model depends on the specific disease being studied and the research question being addressed.

Cloning, molecular, in the medical field refers to the process of creating identical copies of a specific DNA sequence or gene. This is achieved through a technique called polymerase chain reaction (PCR), which amplifies a specific DNA sequence to produce multiple copies of it. Molecular cloning is commonly used in medical research to study the function of specific genes, to create genetically modified organisms for therapeutic purposes, and to develop new drugs and treatments. It is also used in forensic science to identify individuals based on their DNA. In the context of human cloning, molecular cloning is used to create identical copies of a specific gene or DNA sequence from one individual and insert it into the genome of another individual. This technique has been used to create transgenic animals, but human cloning is currently illegal in many countries due to ethical concerns.

In the medical field, binding sites refer to specific locations on the surface of a protein molecule where a ligand (a molecule that binds to the protein) can attach. These binding sites are often formed by a specific arrangement of amino acids within the protein, and they are critical for the protein's function. Binding sites can be found on a wide range of proteins, including enzymes, receptors, and transporters. When a ligand binds to a protein's binding site, it can cause a conformational change in the protein, which can alter its activity or function. For example, a hormone may bind to a receptor protein, triggering a signaling cascade that leads to a specific cellular response. Understanding the structure and function of binding sites is important in many areas of medicine, including drug discovery and development, as well as the study of diseases caused by mutations in proteins that affect their binding sites. By targeting specific binding sites on proteins, researchers can develop drugs that modulate protein activity and potentially treat a wide range of diseases.

Blood bactericidal activity refers to the ability of the immune system to destroy and eliminate bacteria present in the bloodstream. This process is primarily carried out by white blood cells, such as neutrophils and monocytes, which release enzymes and other substances that can break down and kill bacteria. The blood bactericidal activity is an important defense mechanism against bacterial infections that can spread throughout the body and cause serious illness or even death. It is also a key factor in determining the outcome of sepsis, a life-threatening condition that occurs when the body's response to an infection leads to widespread inflammation and organ damage. In medical research, blood bactericidal activity is often measured in vitro, using laboratory cultures of bacteria and blood samples from patients. This can help researchers understand how the immune system responds to different types of bacteria and identify potential targets for new treatments.

In the medical field, "Antigens, CD" refers to a group of proteins found on the surface of certain cells in the immune system. These proteins, known as CD antigens, are recognized by other immune cells and play a crucial role in the immune response to infections and diseases. CD antigens are classified into different families based on their structure and function. Some CD antigens are expressed on the surface of immune cells themselves, while others are found on the surface of cells that are targeted by the immune system, such as cancer cells or cells infected with viruses. The identification and characterization of CD antigens has been important for the development of new diagnostic tests and therapies for a variety of diseases, including cancer, autoimmune disorders, and infectious diseases. For example, monoclonal antibodies that target specific CD antigens have been used in cancer immunotherapy to help the immune system recognize and attack cancer cells.

Mannose-binding lectin (MBL) is a protein that plays a role in the innate immune system. It is produced by the liver and circulates in the blood, where it binds to specific carbohydrate structures on the surface of microorganisms, such as bacteria and viruses. This binding triggers a series of immune responses, including the activation of complement proteins and the recruitment of immune cells to the site of infection. MBL is also involved in the clearance of damaged or apoptotic cells from the body. Deficiencies in MBL can increase the risk of infections and autoimmune diseases.

In the medical field, alleles refer to the different forms of a gene that exist at a particular genetic locus (location) on a chromosome. Each gene has two alleles, one inherited from each parent. These alleles can be either dominant or recessive, and their combination determines the expression of the trait associated with that gene. For example, the gene for blood type has three alleles: A, B, and O. A person can inherit one or two copies of each allele, resulting in different blood types (A, B, AB, or O). The dominant allele is the one that is expressed when present in one copy, while the recessive allele is only expressed when present in two copies. Understanding the different alleles of a gene is important in medical genetics because it can help diagnose genetic disorders, predict disease risk, and guide treatment decisions. For example, mutations in certain alleles can cause genetic diseases such as sickle cell anemia or cystic fibrosis. By identifying the specific alleles involved in a genetic disorder, doctors can develop targeted therapies or genetic counseling to help affected individuals and their families.

Antibodies, also known as immunoglobulins, are proteins produced by the immune system in response to the presence of foreign substances, such as viruses, bacteria, and other pathogens. Antibodies are designed to recognize and bind to specific molecules on the surface of these foreign substances, marking them for destruction by other immune cells. There are five main classes of antibodies: IgG, IgA, IgM, IgD, and IgE. Each class of antibody has a unique structure and function, and they are produced by different types of immune cells in response to different types of pathogens. Antibodies play a critical role in the immune response, helping to protect the body against infection and disease. They can neutralize pathogens by binding to them and preventing them from entering cells, or they can mark them for destruction by other immune cells. In some cases, antibodies can also help to stimulate the immune response by activating immune cells or by recruiting other immune cells to the site of infection. Antibodies are often used in medical treatments, such as in the development of vaccines, where they are used to stimulate the immune system to produce a response to a specific pathogen. They are also used in diagnostic tests to detect the presence of specific pathogens or to monitor the immune response to a particular treatment.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Complement C3 nephritic factor (C3NeF) is a protein that plays a role in the complement system, which is a part of the immune system that helps to fight infections. C3NeF is a factor that can cause the complement system to become overactive, leading to inflammation and damage to the kidneys. This can result in a condition called C3 glomerulopathy, which is a type of kidney disease that can cause blood and protein to leak into the urine. C3NeF is also associated with other conditions, such as atypical hemolytic uremic syndrome (aHUS) and dense deposit disease (DDD).

Glycoproteins are a type of protein that contains one or more carbohydrate chains covalently attached to the protein molecule. These carbohydrate chains are made up of sugars and are often referred to as glycans. Glycoproteins play important roles in many biological processes, including cell signaling, cell adhesion, and immune response. They are found in many different types of cells and tissues throughout the body, and are often used as markers for various diseases and conditions. In the medical field, glycoproteins are often studied as potential targets for the development of new drugs and therapies.

Immunoglobulins, also known as antibodies, are proteins produced by the immune system in response to the presence of foreign substances, such as viruses, bacteria, and toxins. They are Y-shaped molecules that recognize and bind to specific antigens, which are molecules found on the surface of pathogens. There are five main classes of immunoglobulins: IgG, IgA, IgM, IgD, and IgE. Each class has a unique structure and function, and they are produced by different types of immune cells in response to different types of pathogens. Immunoglobulins play a critical role in the immune response by neutralizing pathogens, marking them for destruction by other immune cells, and activating the complement system, which helps to destroy pathogens. They are also used in medical treatments, such as immunoglobulin replacement therapy for patients with primary immunodeficiencies, and in the development of vaccines and monoclonal antibodies for the treatment of various diseases.

Haptoglobins are a group of plasma proteins that are primarily responsible for binding and transporting free hemoglobin (Hb) in the bloodstream. Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. When hemoglobin is released from red blood cells due to injury or disease, it can cause oxidative stress and inflammation in the body. Haptoglobins bind to free hemoglobin and form a complex that can be cleared from the bloodstream by the liver and kidneys. There are several different types of haptoglobins, including alpha-1 haptoglobin, alpha-2 haptoglobin, and beta haptoglobin. Alpha-1 haptoglobin is the most abundant type and is primarily responsible for binding to free hemoglobin. Alpha-2 haptoglobin is less abundant and has a different binding affinity for hemoglobin. Beta haptoglobin is also less abundant and is primarily found in people of African descent. Haptoglobin levels can be measured in the blood as a diagnostic tool for various medical conditions, including hemolytic anemia (a condition in which red blood cells are destroyed too quickly), liver disease, and certain types of cancer. Abnormal levels of haptoglobin can also be an indicator of other medical conditions, such as sepsis (a life-threatening infection) and sickle cell disease (a genetic disorder that affects the shape of red blood cells).

DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.

In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. Cyclic peptides are a type of peptide in which the amino acids are linked in a ring-like structure, rather than in a linear chain. These cyclic peptides can have a variety of biological activities, including antimicrobial, antiviral, and anti-inflammatory effects. They are being studied for their potential use in the development of new drugs and therapies.

Lupus nephritis is a type of kidney inflammation that occurs as a complication of systemic lupus erythematosus (SLE), an autoimmune disorder in which the body's immune system attacks healthy cells and tissues. Lupus nephritis is characterized by inflammation and damage to the glomeruli, which are the tiny blood vessels in the kidneys responsible for filtering waste products from the blood. This can lead to a range of symptoms, including protein in the urine, swelling in the legs and feet, high blood pressure, and decreased kidney function. Treatment for lupus nephritis typically involves a combination of medications to reduce inflammation and control blood pressure, as well as lifestyle changes to promote overall health and well-being.

Antibodies, Antinuclear (ANA) are proteins produced by the immune system in response to the presence of foreign substances, such as viruses or bacteria. In the medical field, ANA tests are used to detect the presence of these antibodies in the blood. ANA tests are often used to diagnose autoimmune diseases, which are conditions in which the immune system mistakenly attacks healthy cells and tissues in the body. Some autoimmune diseases that can be diagnosed through ANA testing include lupus, rheumatoid arthritis, and Sjogren's syndrome. ANA tests can also be used to monitor the effectiveness of treatment for autoimmune diseases, as well as to detect the presence of certain infections or other medical conditions. However, it's important to note that a positive ANA test does not necessarily mean that a person has an autoimmune disease, as ANA can also be present in healthy individuals.

Blotting, Western is a laboratory technique used to detect specific proteins in a sample by transferring proteins from a gel to a membrane and then incubating the membrane with a specific antibody that binds to the protein of interest. The antibody is then detected using an enzyme or fluorescent label, which produces a visible signal that can be quantified. This technique is commonly used in molecular biology and biochemistry to study protein expression, localization, and function. It is also used in medical research to diagnose diseases and monitor treatment responses.

Cosmids are a type of artificial DNA cloning vector that was first developed in the 1980s. They are derived from the bacteriophage lambda and contain a bacterial origin of replication, a bacterial antibiotic resistance gene, and a bacterial origin of transfer. Cosmids are typically used to clone and study large DNA fragments, such as those found in the human genome. They are often used in conjunction with other cloning vectors, such as plasmids and phage, to create a library of DNA fragments that can be screened for specific genes or genetic sequences. In the medical field, cosmids have been used to study the genetic basis of various diseases and to identify potential therapeutic targets.

Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.

Biological markers, also known as biomarkers, are measurable indicators of biological processes, pathogenic processes, or responses to therapeutic interventions. In the medical field, biological markers are used to diagnose, monitor, and predict the progression of diseases, as well as to evaluate the effectiveness of treatments. Biological markers can be found in various biological samples, such as blood, urine, tissue, or body fluids. They can be proteins, genes, enzymes, hormones, metabolites, or other molecules that are associated with a specific disease or condition. For example, in cancer, biological markers such as tumor markers can be used to detect the presence of cancer cells or to monitor the response to treatment. In cardiovascular disease, biological markers such as cholesterol levels or blood pressure can be used to assess the risk of heart attack or stroke. Overall, biological markers play a crucial role in medical research and clinical practice, as they provide valuable information about the underlying biology of diseases and help to guide diagnosis, treatment, and monitoring.

Inflammation is a complex biological response of the body to harmful stimuli, such as pathogens, damaged cells, or irritants. It is a protective mechanism that helps to eliminate the cause of injury, remove damaged tissue, and initiate the healing process. Inflammation involves the activation of immune cells, such as white blood cells, and the release of chemical mediators, such as cytokines and prostaglandins. This leads to the characteristic signs and symptoms of inflammation, including redness, heat, swelling, pain, and loss of function. Inflammation can be acute or chronic. Acute inflammation is a short-term response that lasts for a few days to a few weeks and is usually beneficial. Chronic inflammation, on the other hand, is a prolonged response that lasts for months or years and can be harmful if it persists. Chronic inflammation is associated with many diseases, including cancer, cardiovascular disease, and autoimmune disorders.

In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.

Mannose-binding protein-associated serine proteases (MASPs) are a family of proteases that are involved in the complement system, a part of the immune system that helps to protect the body against infections. These proteases are activated by mannose-binding protein (MBP), a protein that is produced by the liver and circulates in the blood.（MBP），。

Adrenal hyperplasia, congenital, is a rare genetic disorder that affects the adrenal glands, which are responsible for producing hormones such as cortisol and aldosterone. In this condition, the adrenal glands do not develop properly during fetal development, leading to an overproduction of certain hormones. There are several types of congenital adrenal hyperplasia, each caused by a different genetic mutation. The most common type is 21-hydroxylase deficiency, which accounts for about 95% of cases. Other types include 11-beta-hydroxylase deficiency, 17-alpha-hydroxylase deficiency, and 3-beta-hydroxysteroid dehydrogenase deficiency. Symptoms of congenital adrenal hyperplasia can vary depending on the severity of the condition and the specific type of deficiency. In some cases, there may be no symptoms at all. However, in more severe cases, symptoms can include ambiguous genitalia in newborns, early puberty, excessive body hair, and irregular menstrual periods in females. Treatment for congenital adrenal hyperplasia typically involves hormone replacement therapy to replace the hormones that are not being produced properly by the adrenal glands. This can help to prevent symptoms and complications associated with the condition. In some cases, surgery may also be necessary to correct ambiguous genitalia in newborns.

Zymosan is a polysaccharide derived from the cell walls of yeasts and other fungi. It is commonly used in medical research as an activator of the immune system, particularly in the study of inflammation and autoimmune diseases. When zymosan is injected into the body, it triggers an immune response that involves the release of various inflammatory mediators, such as cytokines and chemokines. This response can be used to study the function of immune cells and the signaling pathways involved in inflammation. Zymosan has also been used in clinical trials as a potential treatment for various conditions, including rheumatoid arthritis, psoriasis, and sepsis. However, more research is needed to fully understand its therapeutic potential and potential side effects.

Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.

Membrane glycoproteins are proteins that are attached to the cell membrane through a glycosyl group, which is a complex carbohydrate. These proteins play important roles in cell signaling, cell adhesion, and cell recognition. They are involved in a wide range of biological processes, including immune response, cell growth and differentiation, and nerve transmission. Membrane glycoproteins can be classified into two main types: transmembrane glycoproteins, which span the entire cell membrane, and peripheral glycoproteins, which are located on one side of the membrane.

Fibrinogen is a plasma protein that plays a crucial role in the blood clotting process. It is synthesized in the liver and circulates in the bloodstream as a soluble protein. When the blood vessels are damaged, platelets aggregate at the site of injury and release various substances, including thrombin. Thrombin then converts fibrinogen into insoluble fibrin strands, which form a mesh-like structure that stabilizes the platelet plug and prevents further bleeding. This process is known as coagulation and is essential for stopping bleeding and healing wounds. Fibrinogen levels can be measured in the blood as a diagnostic tool for various medical conditions, including bleeding disorders, liver disease, and cardiovascular disease.

B-lymphocytes, also known as B-cells, are a type of white blood cell that plays a crucial role in the immune system. They are responsible for producing antibodies, which are proteins that help the body recognize and fight off foreign substances such as viruses, bacteria, and other pathogens. B-cells are produced in the bone marrow and mature in the spleen and lymph nodes. When a B-cell encounters an antigen (a foreign substance that triggers an immune response), it becomes activated and begins to divide rapidly. The activated B-cell then differentiates into plasma cells, which produce and secrete large amounts of antibodies specific to the antigen. The antibodies produced by B-cells can neutralize pathogens by binding to them and preventing them from infecting cells, or they can mark them for destruction by other immune cells. B-cells also play a role in memory, meaning that they can remember specific antigens and mount a faster and more effective immune response if they encounter the same antigen again in the future. B-cell disorders, such as autoimmune diseases and certain types of cancer, can result from problems with the development, activation, or function of B-cells.

Proteinuria is a medical condition characterized by the presence of excess protein in the urine. Normally, the kidneys filter waste products and excess fluids from the blood, but they also retain most of the protein in the blood. When the kidneys are damaged or diseased, they may not be able to filter the protein properly, leading to proteinuria. Proteinuria can be classified as either microscopic or macroscopic. Microscopic proteinuria refers to the presence of small amounts of protein in the urine, typically less than 150 mg per day. Macroscopic proteinuria, on the other hand, refers to the presence of larger amounts of protein in the urine, typically greater than 150 mg per day. Proteinuria can be caused by a variety of medical conditions, including kidney disease, diabetes, high blood pressure, and certain infections. It is often an indicator of underlying kidney damage or disease and can lead to serious complications if left untreated. Treatment for proteinuria depends on the underlying cause and may include medications, lifestyle changes, and in some cases, dialysis or kidney transplantation.

Antibody formation, also known as immunoglobulin production, is a process in the immune system where specialized cells called B cells produce antibodies in response to the presence of foreign substances, such as bacteria, viruses, or toxins, in the body. When a foreign substance enters the body, it is recognized by the immune system as foreign and triggers an immune response. B cells are activated and begin to divide and differentiate into plasma cells, which are specialized cells that produce antibodies. These antibodies are proteins that are designed to recognize and bind to specific antigens, which are molecules found on the surface of foreign substances. Once the antibodies bind to the antigens, they can neutralize the foreign substance, mark it for destruction by other immune cells, or activate the complement system, which is a group of proteins that work together to destroy the foreign substance. Antibody formation is a crucial part of the immune system's defense against infections and diseases. It is also an important aspect of the development of vaccines, which stimulate the immune system to produce antibodies against specific pathogens before the person is exposed to the actual pathogen.

Serine endopeptidases are a class of enzymes that cleave peptide bonds in proteins, specifically at the carboxyl side of serine residues. These enzymes are involved in a wide range of biological processes, including digestion, blood clotting, and immune response. In the medical field, serine endopeptidases are often studied for their potential therapeutic applications, such as in the treatment of cancer, inflammation, and neurological disorders. They are also used as research tools to study protein function and regulation. Some examples of serine endopeptidases include trypsin, chymotrypsin, and elastase.

Collectins are a family of proteins that are part of the innate immune system. They are found in the extracellular fluid, including the blood, and are involved in the recognition and clearance of pathogens, such as bacteria and viruses. Collectins are characterized by their ability to bind to carbohydrates on the surface of microorganisms, which helps to aggregate them and facilitate their clearance by immune cells. There are several different types of collectins, including mannose-binding lectin (MBL), surfactant protein D (SP-D), and collectin-11 (CL-11). Collectins play an important role in the body's defense against infection and are also involved in the regulation of inflammation.

DNA primers are short, single-stranded DNA molecules that are used in a variety of molecular biology techniques, including polymerase chain reaction (PCR) and DNA sequencing. They are designed to bind to specific regions of a DNA molecule, and are used to initiate the synthesis of new DNA strands. In PCR, DNA primers are used to amplify specific regions of DNA by providing a starting point for the polymerase enzyme to begin synthesizing new DNA strands. The primers are complementary to the target DNA sequence, and are added to the reaction mixture along with the DNA template, nucleotides, and polymerase enzyme. The polymerase enzyme uses the primers as a template to synthesize new DNA strands, which are then extended by the addition of more nucleotides. This process is repeated multiple times, resulting in the amplification of the target DNA sequence. DNA primers are also used in DNA sequencing to identify the order of nucleotides in a DNA molecule. In this application, the primers are designed to bind to specific regions of the DNA molecule, and are used to initiate the synthesis of short DNA fragments. The fragments are then sequenced using a variety of techniques, such as Sanger sequencing or next-generation sequencing. Overall, DNA primers are an important tool in molecular biology, and are used in a wide range of applications to study and manipulate DNA.

C-Reactive Protein (CRP) is a protein that is produced by the liver in response to inflammation or infection in the body. It is a nonspecific marker of inflammation and is often used as a diagnostic tool in the medical field. CRP levels can be measured in the blood using a blood test. Elevated levels of CRP are often seen in people with infections, autoimmune diseases, and certain types of cancer. However, it is important to note that CRP levels can also be elevated in response to other factors such as exercise, injury, and stress. In addition to its diagnostic role, CRP has also been studied as a potential predictor of future health outcomes. For example, high levels of CRP have been associated with an increased risk of cardiovascular disease, stroke, and other chronic conditions. Overall, CRP is an important biomarker in the medical field that can provide valuable information about a person's health and help guide treatment decisions.

Lipopolysaccharides (LPS) are a type of complex carbohydrate found on the surface of gram-negative bacteria. They are composed of a lipid A moiety, a core polysaccharide, and an O-specific polysaccharide. LPS are important components of the bacterial cell wall and play a role in the innate immune response of the host. In the medical field, LPS are often studied in the context of sepsis, a life-threatening condition that occurs when the body's response to an infection causes widespread inflammation. LPS can trigger a strong immune response in the host, leading to the release of pro-inflammatory cytokines and other mediators that can cause tissue damage and organ failure. As a result, LPS are often used as a model for studying the pathophysiology of sepsis and for developing new treatments for this condition. LPS are also used in research as a tool for studying the immune system and for developing vaccines against bacterial infections. They can be purified from bacterial cultures and used to stimulate immune cells in vitro or in animal models, allowing researchers to study the mechanisms of immune responses to bacterial pathogens. Additionally, LPS can be used as an adjuvant in vaccines to enhance the immune response to the vaccine antigen.

Protein precursors are molecules that are converted into proteins through a process called translation. In the medical field, protein precursors are often referred to as amino acids, which are the building blocks of proteins. There are 20 different amino acids that can be combined in various ways to form different proteins, each with its own unique function in the body. Protein precursors are essential for the proper functioning of the body, as proteins are involved in a wide range of biological processes, including metabolism, cell signaling, and immune function. They are also important for tissue repair and growth, and for maintaining the structure and function of organs and tissues. Protein precursors can be obtained from the diet through the consumption of foods that are rich in amino acids, such as meat, fish, eggs, and dairy products. In some cases, protein precursors may also be administered as supplements or medications to individuals who are unable to obtain sufficient amounts of these nutrients through their diet.

Steroid hydroxylases are a group of enzymes that catalyze the hydroxylation of steroids, which are a class of organic compounds that are important in various physiological processes in the body. These enzymes are responsible for modifying the structure of steroids by adding a hydroxyl group to specific positions on the steroid molecule. There are several different types of steroid hydroxylases, each of which is responsible for hydroxylating a specific position on the steroid molecule. For example, the enzyme 11β-hydroxylase is responsible for hydroxylating the 11β position of cortisol, a hormone that is produced by the adrenal gland. This hydroxylation reaction is important for the conversion of cortisol to cortisone, which is a less active form of the hormone. Steroid hydroxylases are important in the regulation of various physiological processes, including the metabolism of cholesterol, the production of sex hormones, and the regulation of the immune system. They are also involved in the synthesis of other important compounds, such as bile acids and vitamin D. In the medical field, steroid hydroxylases are often studied in the context of various diseases and disorders, such as Cushing's syndrome, which is a condition characterized by the overproduction of cortisol. In this condition, the activity of the enzyme 11β-hydroxylase is often increased, leading to an excess of cortisol in the body.

Blotting, Northern is a laboratory technique used to detect and quantify specific RNA molecules in a sample. It involves transferring RNA from a gel onto a membrane, which is then hybridized with a labeled complementary DNA probe. The probe binds to the specific RNA molecules on the membrane, allowing their detection and quantification through autoradiography or other imaging methods. Northern blotting is commonly used to study gene expression patterns in cells or tissues, and to compare the expression levels of different RNA molecules in different samples.

In the medical field, "DNA, Complementary" refers to the property of DNA molecules to pair up with each other in a specific way. Each strand of DNA has a unique sequence of nucleotides (adenine, thymine, guanine, and cytosine), and the nucleotides on one strand can only pair up with specific nucleotides on the other strand in a complementary manner. For example, adenine (A) always pairs up with thymine (T), and guanine (G) always pairs up with cytosine (C). This complementary pairing is essential for DNA replication and transcription, as it ensures that the genetic information encoded in one strand of DNA can be accurately copied onto a new strand. The complementary nature of DNA also plays a crucial role in genetic engineering and biotechnology, as scientists can use complementary DNA strands to create specific genetic sequences or modify existing ones.

Blotting, Southern is a laboratory technique used to detect specific DNA sequences in a sample. It is named after Edwin Southern, who developed the technique in the 1970s. The technique involves transferring DNA from a gel onto a membrane, such as nitrocellulose or nylon, and then using labeled probes to detect specific DNA sequences. The blotting process is often used in molecular biology research to study gene expression, genetic variation, and other aspects of DNA biology.

Cytokines are small proteins that are produced by various cells of the immune system, including white blood cells, macrophages, and dendritic cells. They play a crucial role in regulating immune responses and inflammation, and are involved in a wide range of physiological processes, including cell growth, differentiation, and apoptosis. Cytokines can be classified into different groups based on their function, including pro-inflammatory cytokines, anti-inflammatory cytokines, and regulatory cytokines. Pro-inflammatory cytokines, such as tumor necrosis factor-alpha (TNF-alpha) and interleukin-1 (IL-1), promote inflammation and recruit immune cells to the site of infection or injury. Anti-inflammatory cytokines, such as interleukin-10 (IL-10) and transforming growth factor-beta (TGF-beta), help to dampen the immune response and prevent excessive inflammation. Regulatory cytokines, such as interleukin-4 (IL-4) and interleukin-13 (IL-13), help to regulate the balance between pro-inflammatory and anti-inflammatory responses. Cytokines play a critical role in many diseases, including autoimmune disorders, cancer, and infectious diseases. They are also important in the development of vaccines and immunotherapies.

Macular degeneration is a medical condition that affects the macula, which is the central part of the retina in the eye responsible for sharp, central vision. There are two main types of macular degeneration: dry and wet. Dry macular degeneration is the most common form and is characterized by the gradual accumulation of small yellow deposits called drusen in the macula. These deposits can cause the retina to thin and the macula to become damaged, leading to a loss of central vision. Wet macular degeneration is less common but more severe. It occurs when abnormal blood vessels grow beneath the retina and leak fluid or blood, causing damage to the macula and leading to a rapid loss of vision. Both forms of macular degeneration can be treated, but the best course of action depends on the severity of the condition and the individual patient's needs. Treatment options may include lifestyle changes, medications, or surgery.

Disease susceptibility refers to an individual's increased risk of developing a particular disease or condition due to genetic, environmental, or lifestyle factors. Susceptibility to a disease is not the same as having the disease itself, but rather an increased likelihood of developing it compared to someone who is not susceptible. Genetic factors play a significant role in disease susceptibility. Certain genetic mutations or variations can increase an individual's risk of developing certain diseases, such as breast cancer, diabetes, or heart disease. Environmental factors, such as exposure to toxins or pollutants, can also increase an individual's susceptibility to certain diseases. Lifestyle factors, such as diet, exercise, and smoking, can also impact disease susceptibility. For example, a diet high in saturated fats and sugar can increase an individual's risk of developing heart disease, while regular exercise can reduce the risk. Understanding an individual's disease susceptibility can help healthcare providers develop personalized prevention and treatment plans to reduce the risk of developing certain diseases or to manage existing conditions more effectively.

The cell membrane, also known as the plasma membrane, is a thin, flexible barrier that surrounds and encloses the cell. It is composed of a phospholipid bilayer, which consists of two layers of phospholipid molecules arranged tail-to-tail. The hydrophobic tails of the phospholipids face inward, while the hydrophilic heads face outward, forming a barrier that separates the inside of the cell from the outside environment. The cell membrane also contains various proteins, including channels, receptors, and transporters, which allow the cell to communicate with its environment and regulate the movement of substances in and out of the cell. In addition, the cell membrane is studded with cholesterol molecules, which help to maintain the fluidity and stability of the membrane. The cell membrane plays a crucial role in maintaining the integrity and function of the cell, and it is involved in a wide range of cellular processes, including cell signaling, cell adhesion, and cell division.

Case-control studies are a type of observational study used in the medical field to investigate the relationship between an exposure and an outcome. In a case-control study, researchers identify individuals who have experienced a particular outcome (cases) and compare their exposure history to a group of individuals who have not experienced the outcome (controls). The main goal of a case-control study is to determine whether the exposure was a risk factor for the outcome. To do this, researchers collect information about the exposure history of both the cases and the controls and compare the two groups to see if there is a statistically significant difference in the prevalence of the exposure between the two groups. Case-control studies are often used when the outcome of interest is rare, and it is difficult or unethical to conduct a prospective cohort study. However, because case-control studies rely on retrospective data collection, they are subject to recall bias, where participants may not accurately remember their exposure history. Additionally, because case-control studies only provide information about the association between an exposure and an outcome, they cannot establish causality.

Rheumatoid arthritis (RA) is a chronic autoimmune disorder that primarily affects the joints. It is characterized by inflammation and damage to the lining of the joint capsule, which leads to pain, stiffness, and reduced range of motion. RA can also affect other organs, such as the lungs, heart, and eyes. RA is a systemic disease, meaning that it affects the entire body, not just the joints. It is an inflammatory disease, meaning that it is caused by the immune system attacking healthy cells and tissues in the body. RA is a progressive disease, meaning that it can worsen over time if left untreated. However, with proper treatment, it is possible to manage the symptoms and slow down the progression of the disease. The exact cause of RA is not fully understood, but it is believed to be a combination of genetic and environmental factors. Risk factors for RA include being female, having a family history of the disease, and smoking.

Antibodies, Bacterial are proteins produced by the immune system in response to bacterial infections. They are also known as bacterial antibodies or bacterial immunoglobulins. These antibodies are specific to bacterial antigens, which are molecules found on the surface of bacteria that trigger an immune response. When the immune system detects a bacterial infection, it produces antibodies that bind to the bacterial antigens and mark them for destruction by other immune cells. This helps to neutralize the bacteria and prevent them from causing harm to the body. Bacterial antibodies can be detected in the blood or other bodily fluids using laboratory tests. These tests are often used to diagnose bacterial infections and to monitor the effectiveness of antibiotic treatments.

Interleukin-6 (IL-6) is a cytokine, a type of signaling molecule that plays a crucial role in the immune system. It is produced by a variety of cells, including immune cells such as macrophages, monocytes, and T cells, as well as non-immune cells such as fibroblasts and endothelial cells. IL-6 has a wide range of functions in the body, including regulating the immune response, promoting inflammation, and stimulating the growth and differentiation of immune cells. It is also involved in the regulation of metabolism, bone metabolism, and hematopoiesis (the production of blood cells). In the medical field, IL-6 is often measured as a marker of inflammation and is used to diagnose and monitor a variety of conditions, including autoimmune diseases, infections, and cancer. It is also being studied as a potential therapeutic target for the treatment of these conditions, as well as for the management of chronic pain and other conditions.

Genetic predisposition to disease refers to the tendency of an individual to develop a particular disease or condition due to their genetic makeup. It means that certain genes or combinations of genes increase the risk of developing a particular disease or condition. Genetic predisposition to disease is not the same as having the disease itself. It simply means that an individual has a higher likelihood of developing the disease compared to someone without the same genetic predisposition. Genetic predisposition to disease can be inherited from parents or can occur due to spontaneous mutations in genes. Some examples of genetic predisposition to disease include hereditary breast and ovarian cancer, Huntington's disease, cystic fibrosis, and sickle cell anemia. Understanding genetic predisposition to disease is important in medical practice because it can help identify individuals who are at high risk of developing a particular disease and allow for early intervention and prevention strategies to be implemented.

Hemoglobinuria, paroxysmal is a medical condition characterized by the presence of hemoglobin in the urine. Hemoglobin is a protein found in red blood cells that carries oxygen throughout the body. When hemoglobin is present in the urine, it can cause the urine to appear brown or black. Paroxysmal hemoglobinuria is a rare type of hemoglobinuria that is characterized by episodes of hemoglobinuria that occur suddenly and unpredictably. During an episode, the patient may experience symptoms such as dark urine, abdominal pain, and fatigue. The episodes can last for several hours to several days and may be followed by a period of normal urine output. The exact cause of paroxysmal hemoglobinuria is not fully understood, but it is thought to be related to an abnormality in the red blood cells that causes them to break down and release hemoglobin into the urine. This condition is typically diagnosed through a physical examination, blood tests, and urine tests. Treatment for paroxysmal hemoglobinuria may involve medications to manage symptoms and prevent further episodes. In severe cases, a blood transfusion may be necessary to replace damaged red blood cells. It is important for individuals with paroxysmal hemoglobinuria to receive regular medical monitoring and follow-up care to manage their condition and prevent complications.

Immune complex diseases are a group of disorders characterized by the formation of immune complexes, which are aggregates of antibodies and antigens that circulate in the blood and tissues. These immune complexes can deposit in various organs and tissues, leading to inflammation and damage. Examples of immune complex diseases include systemic lupus erythematosus (SLE), rheumatoid arthritis, and vasculitis. In these conditions, the immune system mistakenly attacks healthy cells and tissues, leading to symptoms such as joint pain, fatigue, fever, and skin rashes. The formation of immune complexes is thought to be triggered by a variety of factors, including infections, autoimmune disorders, and exposure to certain drugs or environmental toxins. Treatment for immune complex diseases typically involves the use of immunosuppressive drugs to reduce inflammation and prevent further damage to tissues.

In the medical field, cell adhesion refers to the process by which cells stick to each other or to a surface. This is an essential process for the proper functioning of tissues and organs in the body. There are several types of cell adhesion, including: 1. Homophilic adhesion: This occurs when cells adhere to each other through the interaction of specific molecules on their surface. 2. Heterophilic adhesion: This occurs when cells adhere to each other through the interaction of different molecules on their surface. 3. Heterotypic adhesion: This occurs when cells adhere to each other through the interaction of different types of cells. 4. Intercellular adhesion: This occurs when cells adhere to each other through the interaction of molecules within the cell membrane. 5. Intracellular adhesion: This occurs when cells adhere to each other through the interaction of molecules within the cytoplasm. Cell adhesion is important for a variety of processes, including tissue development, wound healing, and the immune response. Disruptions in cell adhesion can lead to a variety of medical conditions, including cancer, autoimmune diseases, and inflammatory disorders.

Tumor Necrosis Factor-alpha (TNF-alpha) is a cytokine, a type of signaling protein, that plays a crucial role in the immune response and inflammation. It is produced by various cells in the body, including macrophages, monocytes, and T cells, in response to infection, injury, or other stimuli. TNF-alpha has multiple functions in the body, including regulating the immune response, promoting cell growth and differentiation, and mediating inflammation. It can also induce programmed cell death, or apoptosis, in some cells, which can be beneficial in fighting cancer. However, excessive or prolonged TNF-alpha production can lead to chronic inflammation and tissue damage, which can contribute to the development of various diseases, including autoimmune disorders, inflammatory bowel disease, and certain types of cancer. In the medical field, TNF-alpha is often targeted in the treatment of these conditions. For example, drugs called TNF inhibitors, such as infliximab and adalimumab, are used to block the action of TNF-alpha and reduce inflammation in patients with rheumatoid arthritis, Crohn's disease, and other inflammatory conditions.

DNA probes are a specific segment of DNA that is labeled with a fluorescent or radioactive marker. They are used in medical research and diagnostics to detect and identify specific DNA sequences in a sample. DNA probes are commonly used in genetic testing to diagnose genetic disorders, such as cystic fibrosis, sickle cell anemia, and Huntington's disease. They can also be used to detect the presence of specific genes or genetic mutations in cancer cells, to identify bacteria or viruses in a sample, and to study the evolution and diversity of different species. DNA probes are created by isolating a specific DNA sequence of interest and attaching a fluorescent or radioactive label to it. The labeled probe is then hybridized to a sample of DNA, and the presence of the probe can be detected by fluorescence or radioactivity. The specificity of DNA probes allows for accurate and sensitive detection of specific DNA sequences, making them a valuable tool in medical research and diagnostics.

Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.

Cryoglobulins are abnormal proteins that form deposits in the blood vessels when the temperature drops. They are typically found in the blood plasma and can cause a variety of symptoms, including joint pain, skin rashes, and fatigue. Cryoglobulins are often associated with certain medical conditions, such as hepatitis C, lymphoma, and autoimmune disorders. Treatment for cryoglobulinemia typically involves addressing the underlying cause of the condition and managing the symptoms.

Lectins are a class of proteins that are found in many plants, animals, and microorganisms. They are characterized by their ability to bind to specific carbohydrates, such as sugars and starches, on the surface of cells. In the medical field, lectins have been studied for their potential therapeutic applications. For example, some lectins have been shown to have antiviral, antibacterial, and antifungal properties, and may be useful in the development of new drugs to treat infections. Lectins have also been used as research tools to study cell-cell interactions and to identify specific cell surface markers. In addition, some lectins have been used in diagnostic tests to detect specific diseases or conditions, such as cancer or diabetes. However, it is important to note that not all lectins are safe or effective for medical use, and some may even be toxic. Therefore, the use of lectins in medicine requires careful consideration and testing to ensure their safety and efficacy.

Haefliger JA, Peitsch MC, Jenne DE, Tschopp J (1991). "Structural and functional characterization of complement C8 gamma, a ... complement component C8 gamma chain; crustacyanin; epididymal-retinoic acid binding protein (E-RABP); insectacyanin; odorant ...

https://en.wikipedia.org/wiki/Lipocalin

Power, LM; Chua, SC Jr; Leibel, RL (1994). "Locus D1S21 contains exonic sequence from the C8 beta component of complement". ...

https://en.wikipedia.org/wiki/Rudolph_Leibel

... proteins of the complement system (C6, C7, C8α, C8β and C9) and perforin (PF). Members of this protein family are pore-forming ... "Identity of the segment of human complement C8 recognized by complement regulatory protein CD59". J. Biol. Chem. 270 (34): ... Complement proteins C6-C9 all contain a MACPF domain and assemble into the membrane attack complex. C6, C7 and C8β appear to be ... The binding site on C8α is known, however, the precise role of C8γ in the MAC remains to be understood. Deficiency of C9, or ...

https://en.wikipedia.org/wiki/MACPF

Hadders, M. A.; Beringer, D. X.; Gros, P. (2007). "Structure of C8 -MACPF Reveals Mechanism of Membrane Attack in Complement ... This protein is part of the oldest part of the immune system that is present in the human body, the complement system. Using ... Among his findings are the molecular mechanisms that underlie key steps in the human immune defense by the complement system, ... such as the mode of action of complement component 3 and component 8. Other research in his lab has focussed on the adhesion of ...

https://en.wikipedia.org/wiki/Piet_Gros

C9 is one member of the complement membrane attack complex (MAC), which also includes complement components C5b, C6, C7 and C8 ... MAC formation starts with the assembly of a tetrameric complex with the complement components C6, C7, C8, and C5b. The final ... Complement component 9 (C9) is a MACPF protein involved in the complement system, which is part of the innate immune system. ... Complement+9 at the U.S. National Library of Medicine Medical Subject Headings (MeSH) PDBe-KB provides an overview of all the ...

https://en.wikipedia.org/wiki/Complement_component_9

"Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement". J Biol Chem. 286 (20): ... the first crystal structure of a protein containing this type of glycosylation was determined-that of human complement ...

https://en.wikipedia.org/wiki/Glycosylation

"Evidence that C5b recognizes and mediates C8 incorporation into the cytolytic complex of complement". J. Immunol. 139 (6): 1960 ... Complement component 5 is involved in the complement system. It is cleaved into C5a and C5b: C5a plays an important role in ... Complement component 5 is the fifth component of complement, which plays an important role in inflammatory and cell killing ... 2008). "Structure of and influence of a tick complement inhibitor on human complement component 5". Nat Immunol. 9 (7): 753-60 ...

https://en.wikipedia.org/wiki/Complement_component_5

C8 is a complex made of the two proteins C8-beta and C8 alpha-gamma. C8 alpha-gamma has the hydrophobic area that inserts into ... MAC is composed of a complex of four complement proteins (C5b, C6, C7, and C8) that bind to the outer surface of the plasma ... The MAC is composed of the complement components C5b, C6, C7, C8 and several C9 molecules. A number of proteins participate in ... ISBN 978-0-323-54943-1. Media related to Complement membrane attack complex at Wikimedia Commons Complement+Membrane+Attack+ ...

https://en.wikipedia.org/wiki/Complement_membrane_attack_complex

... the four genes for complement C8 gamma chain, prostaglandin-D-synthase, oncogene-24p3, and progestagen-associated endometrial ...

https://en.wikipedia.org/wiki/Lipocalin-2

Complement+C8 at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short description, ... C8 is a heterotrimer; it consists of three different subunits. These are called C8 alpha, beta and gamma chains, encoded by the ... Complement component 8 is a protein involved in the complement system. It is part of the membrane attack complex (MAC). A ... "Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement". The Journal of ...

https://en.wikipedia.org/wiki/C8_complex

C6 C7 C8 C9 Complement pathway inhibitors C1-inhibitor - Classical, Lectin, Alternate Decay-accelerating factor (CD59) - ... system Complement system Classical complement pathway Mannan-binding lectin pathway Alternate complement pathway Complement ... see complement proteins section) Collectins Mannan-binding lectin (MBL) Surfactant protein A (SP-A) Surfactant protein D (SP-D ... Classical complement pathway C1Q complex - C1R / C1S C4 - C4a C2 Mannan-binding lectin pathway MASP1 / MASP2 Mannan-binding ...

https://en.wikipedia.org/wiki/Outline_of_immunology

Ninomiya H, Sims PJ (1992). "The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the "b"domain ... When complement activation leads to deposition of C5b678 on host cells, CD59 can prevent C9 from polymerizing and forming the ... 1992). "Complement regulatory proteins at the feto-maternal interface during human placental development: distribution of CD59 ... Bohana-Kashtan O, Ziporen L, Donin N, Kraus S, Fishelson Z (July 2004). "Cell signals transduced by complement". Mol. Immunol. ...

https://en.wikipedia.org/wiki/CD59

Ninomiya H, Sims PJ (July 1992). "The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the "b" ...

https://en.wikipedia.org/wiki/CD9

... and C8. (While C9 is part of the MAC, and deficiencies have been identified, it is not required for cell lysis.) People with ... Terminal complement pathway deficiency is a genetic condition affecting the complement membrane attack complex (MAC). It ... Suspect terminal complement pathway deficiency in patients with more than one Neisseria infection episode. Initial complement ... Lint TF, Zeitz HJ, Gewurz H (November 1980). "Inherited deficiency of the ninth component of complement in man". J. Immunol. ...

https://en.wikipedia.org/wiki/Terminal_complement_pathway_deficiency

The C5b then recruits and assembles C6, C7, C8 and multiple C9 molecules to assemble the membrane attack complex. This creates ... Polymorphisms of complement component 3, complement factor B, and complement factor I, as well as deletion of complement factor ... The complement system, also known as complement cascade, is a part of the immune system that enhances (complements) the ability ... Three biochemical pathways activate the complement system: the classical complement pathway, the alternative complement pathway ...

https://en.wikipedia.org/wiki/Complement_system

C5b binds sequentially to C6, C7, C8 and then to multiple molecules of C9 to form membrane attack complex. Since C3b is free ... cells from complement-mediated damage. CFHR5 (Complement Factor H-Related protein 5) is able to bind to act as a cofactor for ... there are several different kinds of regulatory proteins that disrupt the complement activation process: Complement Receptor 1 ... The alternative pathway is a type of cascade reaction of the complement system and is a component of the innate immune system, ...

https://en.wikipedia.org/wiki/Alternative_complement_pathway

... three proteins involved in the complement system (part of the immune system) Cervical spinal nerve 8 in human anatomy Carbon-8 ... C8) HMS C8, a 1907 C-class submarine of the Royal Navy USS Raleigh (C-8), an 1892 protected cruiser of the United States Navy ... IATA code Citroën C8, a brand of minivan Sauber C8, a 1985 racing car Spyker C8, a sportscar produced by car manufacturer ... C8, C08, C.VIII or C-8 may refer to: AEG C.VIII, a World War I German armed reconnaissance aircraft AGO C.VIII, a World War I ...

https://en.wikipedia.org/wiki/C8

Subsequent interactions between C5b and other terminal components C6, C7, C8, and C9 form the membrane attack complex or the ... Alternative complement pathway - another complement system pathway Lectin pathway - another complement system pathway Noris, ... The classical complement pathway is one of three pathways which activate the complement system, which is part of the immune ... Activation of the complement pathway through the classical, lectin or alternative complement pathway is followed by a cascade ...

https://en.wikipedia.org/wiki/Classical_complement_pathway

Cases may also arise with complement alone or with IgA, IgM or a combination of these three antibody classes and complement. ... C8, C9) either can form the membrane attack complex (MAC) or can bind the antibody, aiding phagocytosis by macrophages (C3b). ... Antibodies are produced against the RBCs, which leads to complement activation. Complement fragments, such as C3a, C4a and C5a ... IgM is a potent activator of the classical complement pathway, thus, AIHA involving IgM is characterized by complement-mediated ...

https://en.wikipedia.org/wiki/Autoimmune_hemolytic_anemia

Complement amounted to 30. Along with the rest of the Romanian Navy, the class saw service during the Romanian Campaign of the ...

https://en.wikipedia.org/wiki/Bistrița-class_cruiser

The public system is complemented by numerous private clinics. In December 2021, the Ministry of Health signed the contract for ...

https://en.wikipedia.org/wiki/Iași

For decades, the two complemented each other within the same integrated factory. Until 1855, the works belonged to the Treasury ...

https://en.wikipedia.org/wiki/Reșița_Works

The project is complemented by a supermarket, medical center, pharmacy, banks and other complementary commercial functions. ...

https://en.wikipedia.org/wiki/ISHO_Timișoara

The C1 complement complex binds to these antibodies resulting in its activation via cross proteolysis. This activated C1 ... C5b associates with C6, C7, C8, and C9, all of which form a complex that results in a pore through the pathogen's membrane. ... C3b is the larger of two elements formed by the cleavage of complement component 3, and is considered an important part of the ... The key to the success of the complement system in clearing antigens is regulating the effects of C3b to pathogens alone and ...

https://en.wikipedia.org/wiki/C3b

... complement c6 MeSH D12.776.124.486.274.650 - complement c7 MeSH D12.776.124.486.274.750 - complement c8 MeSH D12.776.124.486. ... complement c1 MeSH D12.776.124.486.274.050.270 - complement c1q MeSH D12.776.124.486.274.050.280 - complement c1r MeSH D12.776. ... complement c2 MeSH D12.776.124.486.274.150.500 - complement c2a MeSH D12.776.124.486.274.150.750 - complement c2b MeSH D12.776. ... complement c3c MeSH D12.776.124.486.274.250.260.750 - complement c3d MeSH D12.776.124.486.274.350 - complement c4 MeSH D12.776. ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D12.776.124)

Forests occupy 19.3% of the district and are complemented by oak, ash, lime, hornbeam, acacia and others. Plants include: ...

https://en.wikipedia.org/wiki/Șoldănești_District

Forests of the district are complemented by tree species such as oak, ash, hornbeam, linden, maple, walnut and others. From ...

https://en.wikipedia.org/wiki/Ștefan_Vodă_District

The edifice employs a classical architectural style infused with Baroque influences, complemented by an interior adorned with ...

https://en.wikipedia.org/wiki/Târgoviște_Art_Museum

Contents A B C Ca-Cu D E F G H I K L M N O P R S T U V W X Y Z External links C C2 C3 C4 C5 H C7 C8 C9 C10 C15 C20 Webelements ... This complements alternative listing at list of inorganic compounds. There is no complete list of chemical compounds since by ...

https://en.wikipedia.org/wiki/Glossary_of_chemical_formulae

... complementing it with retail, office and entertainment functions. Iulius Town has the largest shopping area in Romania (120,000 ...

https://en.wikipedia.org/wiki/Timișoara

... of a protein complex called complement component 8. Learn about this gene and related health conditions. ... Chromosomal assignment of genes encoding the alpha, beta, and gamma subunits of human complement protein C8: identification of ... Complement component 8 aids in a part of the bodys immune response known as the complement system. The complement system is a ... Genetic basis of human complement C8 beta deficiency. J Immunol. 1993 Jun 1;150(11):4943-7. Citation on PubMed ...

https://medlineplus.gov/genetics/gene/c8b/

Levels of complement components C2, C3, C6, C7, C8, and H factor were greatly elevated. The cerebrospinal fluid (CSF) sample ...

https://wwwnc.cdc.gov/eid/article/14/10/08-0118_article

Crystal Structure of Human Complement Component C8. 3r6b. Crystal Structure of Thrombospondin-1 TSR Domains 2 and 3. ... Crystal Structure of human Complement Component C6. 3vdj. Crystal structure of circumsporozoite protein aTSR domain, R32 native ... Complement component C6 (P13671) (SMART). OMIM:217050: C6 deficiency ; Combined C6/C7 deficiency. ... Now a number of proteins involved in the complement pathway (properdin, C6, C7, C8A, C8B, C9) [ (PUBMED:2459396) ] as well as ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=TSP1&START=294&END=343&E_VALUE=2.1e-12&TYPE=SMART&BLAST=VEEWSQWSACSVTCGQGSQVRTRTCVSPYGTHCSGPLRESRVCNNTALCP

... implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex. Acta. Crystallogr. ... A prime function of CD59 is during complement activation, when it inhibits the assembly of the terminal membrane attack complex ... 1990) Human protectin (CD59), an 18,000 20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 ...

https://www.sdbonline.org/sites/fly/genebrief/coiled_leaky.htm

C5b activates the terminal complement pathway by associating with C6, C7, and C8 to form macromolecular complexes denoted as ... Homologous restriction factor, C8 binding protein, is a cell membrane protein with significant sequence homology to both C8 and ... Table 3. Proteins of the Human Complement (C) System, Lectin Pathway *Table 4. Proteins of the Human Complement (C) System, C3 ... encoded search term (Complement-Related Disorders) and Complement-Related Disorders What to Read Next on Medscape ...

https://emedicine.medscape.com/article/136368-overview

Discover more about our unique complement depleted seras with applications in EIA and infectious diseases. ... Quidels Complement System is comprised of more than 30 proteins, both in serum and on cell surfaces. By a series of specific ... Quidels depleted sera are specifically depleted of a single complement protein. With the... ... activation steps via either the classical, alternative, or the lectin pathway, the complement proteins mediate a set of ...

https://www.quidel.com/research/complement-depleted-sera

Newhauser, W. D., Williams, J. P., Noska, M. A., Borrás, C., Holahan, E. V., Dewji, S. A., Johnson, T. E., Hiatt, J. W., Poston, J. W., Hertel, N., Gress, D. A., Mills, M. D., Jordan, D. W., Sutlief, S. G., Martin, M. C., Jackson, E., Bluth, E. I., Frush, D. P., Oates, M. E., LaBerge, J., & 26 othersPan, H. Y., Rosenthal, S. A., Townsend, L. W., Brady, L., Lindegard, J., Hall, H. L., McAndrew-Benavides, E., Abelquist, E., Anscher, M. S., Vazquez, M., Kronenberg, A., Willey, J. S., Lawrence, T., Woloschak, G. E., Marples, B., Wong, R., Story, M., Howell, R. W., Hei, T. K., Tolmachev, S. Y., Auxier, J. D., Rucker, T. L., Nilsson, M., Sudowe, R., Powell, B. A. & Jensen, M. P., Dec 2022, In: Journal of applied clinical medical physics. 23, S1, e13846.. Research output: Contribution to journal › Editorial › peer-review ...

https://utsouthwestern.elsevierpure.com/en/organisations/molecular-radiation-biology-2/publications/

This antibody recognizes complement component 8 (C8), a 151 kDa member of the complement C6/C7/C8/C9 family, present in blood ... Defects in the alpha chain of C8 can result in complement C8 deficiency type I. Furthermore, C8 deficiencies can cause ... C8 is a terminal component of the complement system, part of both the complement membrane attack complex (MAC), and important ... Human complement protein C8 gamma.. Schreck SF, Parker C, Plumb ME, Sodetz JM. Biochimica et biophysica acta 2000 Oct 18;1482(1 ...

https://www.antibodypedia.com/gene/19367/C8A/antibody/32265/NB100-64340

Complement component C8 beta chain; C8B; Background. Constituent of the membrane attack complex (MAC) that plays a key role in ... Home › Complement factor 8 beta Polyclonal Antibody Complement factor 8 beta Polyclonal Antibody. ... Raji lysates probed with Complement factor 8 beta Polyclonal Antibody, Unconjugated (bs-13969R) at 1:300 dilution and 4˚C ...

https://www.biossusa.com/products/BS-13969R

complement C8 alpha chain [Source:HGNC.... CA13. 377677. CA13. carbonic anhydrase 13 [Source:HGNC Sym.... ...

https://www.gsea-msigdb.org/gsea/msigdb/human/geneset/GSE17721_PAM3CSK4_VS_CPG_16H_BMDC_DN.html

Levels of complement factors C8 and carboxypeptidases were decreased. Our findings associate the PDA with the renin-angiotensin ... system and immune- and complement systems, indicating that PDA goes beyond the persistence of a fetal circulatory connection of ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=au:Hjortdal,+Vibeke+Elisabeth

Designed to seamlessly complement the Audi S6 / A6 C8, our ... A6 C8 by Bimmer Plug. Crafted with meticulous precision from ... Designed to seamlessly complement the Audi S6 / A6 C8, our trunk spoiler melds aesthetics and aerodynamics seamlessly. The ... M4 Style Carbon Fiber Trunk Spoiler - Audi S6 / A6 C8. No reviews ... Transform your Audi S6 / A6 C8 into an icon of style and sophistication with the M4 Style Carbon Fiber Trunk Spoiler by Bimmer ...

https://bimmerplug.com/products/m4-style-carbon-fiber-trunk-spoiler-audi-s6-a6-c8

The presence/absence of this ligand is linked to alternate conformations of the amino acids implicated in C8/C9 binding. ... In one of these structures the electron-density map shows an as yet unidentified small molecule in the predicted C8/C9-binding ... CD59 is a membrane-bound glycoprotein that protects host cells from lysis by inhibiting the terminal pathway of complement, ... CD59 Antigens, Complement C8, Complement C9, Crystallography, X-Ray, Escherichia coli, Gene Expression Regulation, Bacterial, ...

https://www.neuroscience.ox.ac.uk/publications/28701

The complement system plays an important part in defense against pyogenic organisms. ... The complement system is part of the innate immune system. ... Complement component C8, when entirely absent, results in ... Most complement deficiencies are caused by a genetic defect in one of the genes that code for the various complement proteins. ... The complement protein C3b, along with its cleavage product C3bi, is a potent agent of opsonization in the complement cascade. ...

https://emedicine.dev01.medscape.com/article/135478-clinical

CD59 restricts the cytolytic activity of homologous complement by binding to C8 and C9 and blocking the assembly of the ... CD59 restricts the cytolytic activity of homologous complement by binding to C8 and C9 and blocking the assembly of the ... Complement Inactivating Agents. Inactivadores del Complemento. Inativadores do Complemento. Inhibiteurs du complément. ... El CD59 restringe la actividad citolítica del complemento homólogo mediante la unión al C8 y C9, bloqueando la formación del ...

https://decs.bvsalud.org/en/ths/resource/?id=32839

For example, patients who have deficiencies of the terminal complement components (C5 through C8, perhaps C9) have an increased ... The complement system Complement System The complement system is an enzyme cascade that helps defend against infection. Many ... Complement can also be activated on the surface of some microorganisms via the alternative pathway. ... Antibodies can also promote the deposition of substances known as opsonins (eg, the complement protein C3b) on the surface of ...

https://www.msdmanuals.com/en-jp/professional/infectious-diseases/biology-of-infectious-disease/host-defense-mechanisms-against-infection

Kennedy administration president john f. Kennedy as the tautology full complement.) as a set of 206 tags6 (claws c8 tagset). ...

https://mjr.jour.umt.edu/admission/essays-on-my-pet-dog/1/

It does not react with native C9 or C8 proteins (PubMed ID: 2424021). ... was first reported to bind to a neoepitope exposed on polymerized C9 when incorporated into the human terminal complement ... It was subsequently shown that this antibody also cross reacts with the C5b-8 complex and purified C8 alpha-gamma. ...

https://www.abcam.com/products/primary-antibodies/biotin-c5b-9--c5b-8-antibody-ae11-ab237699.html

... and C5b ultimately binds to complement proteins C6, C7, C8, and C9 to create membrane attack complex (MAC), C5b-9. MAC then ... aHUS is associated with deregulated complement systems, and is treated with eculizumab, a terminal C5 complement inhibitor [1,2 ... Patients with aHUS typically have genetic or acquired defects in the alternative complement pathway (AP). The complement system ... the complement system is up-regulated, and this may unmask defective complement regulation [8]. Originally designed to treat ...

https://clinmedjournals.org/articles/ogcr/obstetrics-and-gynaecology-cases-reviews-ogcr-9-230.php?jid=ogcr

Expression and characterization of recombinant subunits of human complement component C8: further analysis of the function of ... Hughes, D.A.; Gordon, S. 1998: Expression and function of the type 3 complement receptor in tissues of the developing mouse. ...

https://eurekamag.com/research/017/897/

Additionally, C8-deficient serum also abrogated the response, suggesting generation of C5b-7 alone is insufficient to induce ... To test the hypothesis that inflammatory cytokines and complement(C) MACs play a role in the expression of DAF, CD59 and MCP, ... How endothelial cells protect themselves from complement by expressing decay-accelerating factor (DAF). *Frances Williams1 ... How do endothelial cells (ECs) protect themselves against damage by complement, particularly when they are present at the ...

https://arthritis-research.biomedcentral.com/articles/10.1186/ar-1999-66739

C8A; complement C8 alpha chain [KO:K03997]. 732 C8B; complement C8 beta chain [KO:K03998]. ... The combined effects of complement activation, dysregulated neutrophilia, endothelial injury, and hypercoagulability appear to ...

https://www.kegg.jp/entry/pathway+hsa05171

Activation of complement system. The activation of complement system is normally one of the key events in defensive mechanism ... CD59 and C9 compete for a nascent epitope on C8. J Immunol. 1993;151:4941-9. ... Although the major role of complement is protective function for the host through innate immune defense, activated complement ... Since complement activation in sepsis to kill invading pathogen can be inhibited by anti-complement therapy in early immune ...

https://thrombosisjournal.biomedcentral.com/articles/10.1186/s12959-019-0198-4

C8-alpha and C8-beta. The team found that the variants from the four AMD families all affected the ability of the C8 proteins ... Because MAC is the final step in the complement cascade, variants affecting any of the complement proteins may funnel down to ... MAC forms a circular pore, closed at one end by the C8 proteins; the MAC pore permits the flow of ions through the outer ... This pore is the final step in the complement cascade, a part of the immune system that helps the body defend against ...

https://vaccar.biz/health-news/extremely-rare-gene-variants-point-to-a-potential-cause-of-age-related-macular-degeneration/

C5b initiates the membrane attack pathway, which results in the membrane attack complex (MAC), consisting of C5b, C6, C7, C8, ... Three biochemical pathways activate the complement system: the classical complement pathway, the alternative complement pathway ... A complement protein attacking an invader.. The complement system is a biochemical cascade which helps clear pathogens from an ... Main article: Complement deficiency. It is thought that the complement system might play a role in many diseases with an immune ...

https://fr.wikidoc.org/index.php/Complement_system

The chassis is an aluminum spaceframe to complement the hand-beaten aluminum panels, and features fully adjustable suspension ... For a modern car, the C8 is light at 2,800 pounds, and the performance accordingly exciting. Driving the car is a properly ... Despite this fact, this C8 Spyder has covered 27,000 miles, which appear to have been lovingly applied based on the service ...

https://carforcoin.com/product/2007-spyker-c8-spyder-nft/

... such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement ... 9] ; homologous restriction factor (HRF), or C8 binding protein; and membrane inhibitor of reactive lysis (MIRL), or CD59. [10 ... The role of complement components in the increased sensitivity of PNH red cells to immune lysis. J Clin Invest. 1966 May. 45(5 ... The role of complement in the sensitivity of the paroxysmal nocturnal haemoglobinuria red cell to immune lysis. Bibl Haematol. ...

https://reference.medscape.com/article/207468-overview

However, incubation with AChE antibodies in heat-inactivated serum, or serum that was deficient in C3 or C8, caused no ... was also disrupted in ganglia exposed to AChE antibodies in complement-sufficient serum. When complement was eliminated by ... was also disrupted in ganglia exposed to AChE antibodies in complement-sufficient serum. When complement was eliminated by ... was also disrupted in ganglia exposed to AChE antibodies in complement-sufficient serum. When complement was eliminated by ...

https://mayoclinic.elsevierpure.com/en/publications/complement-mediated-lesion-of-sympathetic-ganglia-in-vitro-with-a

This complement system is triggered through the classical pathway via nine glycoproteins (C1, C2, C3, C4, C5, C6, C7, C8, and ... The complement system is activated as part of the immune response. This is a system of plasma proteins that can be activated on ...

https://spermidinelife.com/en-it/blogs/articles/3-2-1-the-fact-countdown-about-immune-cells

The complement system is a group of proteins that work together to destroy foreign invaders, trigger inflammation, and remove debris from cells and tissues. (medlineplus.gov)
Complement component 8 combines with several other complement proteins to form the membrane attack complex (MAC), which inserts itself in the outer membrane of bacterial cells. (medlineplus.gov)
Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex. (sdbonline.org)
The complement system as understood today is a multimolecular system composed of more than 32 proteins and consisting of serum proteins, serosal proteins, and cell membrane receptors that bind to complement fragments. (medscape.com)
The complement system consists of 7 serum and 9 membrane regulatory proteins, 1 serosal regulatory protein, and 8 cell membrane receptors that bind complement fragments. (medscape.com)
Quidel's Complement System is comprised of more than 30 proteins, both in serum and on cell surfaces. (quidel.com)
By a series of specific activation steps via either the classical, alternative, or the lectin pathway, the complement proteins mediate a set of activities ranging from the initiation of inflammation, clearance of immune complexes, disruption of cell membranes, and regulation of the immune response. (quidel.com)
Of all the lectin proteins, only MBL has been shown to have the ability to activate the complement system. (medscape.com)
It does not react with native C9 or C8 proteins (PubMed ID: 2424021). (abcam.com)
Swaroop, Klein and colleagues found that in four families, individuals with AMD have mutations in one of two proteins that form one end of MAC: C8-alpha and C8-beta. (vaccar.biz)
The team found that the variants from the four AMD families all affected the ability of the C8 proteins to stick to each other, which may alter how MAC behaves in the eye's retina. (vaccar.biz)
Genetic data from NEI's Age Related Eye Disease Studies have suggested roles for C8 proteins, as well as other proteins higher up in the complement cascade, in AMD. (vaccar.biz)
Because MAC is the final step in the complement cascade, variants affecting any of the complement proteins may funnel down to alter MAC function. (vaccar.biz)
The complement system consists of a number of small proteins found in the blood, normally circulating as inactive zymogens . (wikidoc.org)
Over 20 proteins and protein fragments make up the complement system, including serum proteins, serosal proteins, and cell membrane receptors. (wikidoc.org)
thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. (medscape.com)
[ 9 ] All of these proteins interact with complement proteins, particularly C3b and C4b, dissociate the convertase complexes of the classic and alternative pathways, and halt the amplification of the activation process. (medscape.com)
The absence of these regulating proteins results in uncontrolled amplification of the complement system. (medscape.com)

The C8B gene provides instructions for making one piece, the beta subunit, of a protein complex called complement component 8. (medlineplus.gov)
The resulting shortage of this protein impairs formation of complement component 8. (medlineplus.gov)
Chromosomal assignment of genes encoding the alpha, beta, and gamma subunits of human complement protein C8: identification of a close physical linkage between the alpha and the beta loci. (medlineplus.gov)
Quidel's depleted sera are specifically depleted of a single complement protein. (quidel.com)
Human complement protein C8 gamma. (antibodypedia.com)
The complement protein C3b, along with its cleavage product C3bi, is a potent agent of opsonization in the complement cascade. (medscape.com)
In order to generate an antibody response, an antigen must bind to the complement receptor (CR2) on B cells and the complement protein C3d. (medscape.com)
The MBL protein can activate the C4 and C2 components of complement by forming a complex with serine proteases known as MASP1 and MASP2. (medscape.com)
A complement protein attacking an invader. (wikidoc.org)
Complement C2 is a protein that in humans is encoded by the C2 gene . (wikidoc.org)
[1] The protein encoded by this gene is part of the classical pathway of the complement system , acting as a multi-domain serine protease. (wikidoc.org)

C8 is a terminal component of the complement system, part of both the complement membrane attack complex (MAC), and important to MAC assembly. (antibodypedia.com)
C8 binds to the C5b-7 complex, anchored to the membrane, creating C5b-8. (antibodypedia.com)
C8 is thought to contain lipid binding sites, facilitating the insertion of MAC into the membrane. (antibodypedia.com)
CD59 is a membrane-bound glycoprotein that protects host cells from lysis by inhibiting the terminal pathway of complement, preventing the formation and insertion of the membrane attack complex (MAC). (ox.ac.uk)
CD59 restricts the cytolytic activity of homologous complement by binding to C8 and C9 and blocking the assembly of the membrane attack complex. (bvsalud.org)
DAF prevents the formation and accelerates the decay of complement 3 (C3) convertases, MCP binds to C3b and C4b promoting their degradation and CD59 inhibits the membrane-attack complex (MAC). (biomedcentral.com)
Complement activation generates membrane attack complex (MAC). (biomedcentral.com)
C5b initiates the membrane attack pathway , which results in the membrane attack complex (MAC), consisting of C5b, C6 , C7 , C8 , and polymeric C9 . (wikidoc.org)
The term "nocturnal" refers to the belief that hemolysis is triggered by acidosis during sleep and activates complement to hemolyze an unprotected and abnormal RBC membrane. (medscape.com)

Properdin is a serum glycoprotein that up-regulates the alternative pathway of complement by stabilizing the C3b-Bb complex. (embl.de)
This antibody recognizes complement component 8 (C8), a 151 kDa member of the complement C6/C7/C8/C9 family, present in blood serum. (antibodypedia.com)
Additionally, C8-deficient serum also abrogated the response, suggesting generation of C5b-7 alone is insufficient to induce DAF. (biomedcentral.com)
Freshly dissected rat superior cervical ganglia (SCG) were incubated 15-20 h at 37°C in fresh human serum (a potent source of complement) with continuous oxygenation. (elsevierpure.com)
Staining for AChE and synaptophysin (a synaptic vesicle marker) was also disrupted in ganglia exposed to AChE antibodies in complement-sufficient serum. (elsevierpure.com)
When complement was eliminated by substituting serum that was heat-inactivated or deficient in C3, synaptic input was retained in 60-90% of neurons incubated with AChE antibodies. (elsevierpure.com)
However, incubation with AChE antibodies in heat-inactivated serum, or serum that was deficient in C3 or C8, caused no measurable loss of ganglionic ChAT activity. (elsevierpure.com)

Three biochemical pathways activate the complement system: the classical complement pathway , the alternative complement pathway , and the mannose-binding lectin pathway . (wikidoc.org)

In the first phase, a series of specific interactions leads to formation of intrinsic complement proteinase, termed C3 convertase. (medscape.com)
Depending on the nature of complement activators, the classic pathway, the alternative pathway, or the more recently discovered lectin pathway is activated predominantly to produce C3 convertase. (medscape.com)

Several mutations in the C8B gene cause complement component 8 deficiency type II. (medlineplus.gov)
Defects in the alpha chain of C8 can result in complement C8 deficiency type I. Furthermore, C8 deficiencies can cause recurring bacterial infections, in particular from Neisseria meningitides. (antibodypedia.com)

The 3 major sequelae of complement deficiencies, based on the pathophysiology of each defect, are (1) defects that result in inadequate opsonization, (2) defects in cell lysis, and (3) the association of complement deficiencies with immune complex diseases. (medscape.com)
The clinical history of patients with classic pathway deficiencies varies slightly from other complement-deficient patients. (medscape.com)

Activation of the complement pathways. (medscape.com)
The classical complement pathway typically requires antibodies for activation (specific immune response), while the alternative and mannose-binding lectin pathways can be activated by C3 hydrolysis or antigens without the presence of antibodies (non-specific immune response). (wikidoc.org)
The classical and alternative complement pathways. (wikidoc.org)

The complement system functions as an interactive sequence, with one reaction leading to another in the form of a cascade. (medscape.com)
This pore is the final step in the 'complement cascade,' a part of the immune system that helps the body defend against pathogens. (vaccar.biz)
The complement system is a biochemical cascade which helps clear pathogens from an organism. (wikidoc.org)
These findings strongly implicate the complement cascade in the destruction of preganglionic sympathetic terminals that follows binding of AChE antibodies. (elsevierpure.com)

1990) Human protectin (CD59), an 18,000 20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers. (sdbonline.org)
El CD59 restringe la actividad citolítica del complemento homólogo mediante la unión al C8 y C9, bloqueando la formación del complejo de ataque a membrana. (bvsalud.org)
To test the hypothesis that inflammatory cytokines and complement(C) MACs play a role in the expression of DAF, CD59 and MCP, and to investigate the intracellular signalling pathway involved in DAF expression. (biomedcentral.com)

Raji lysates probed with Complement factor 8 beta Polyclonal Antibody, Unconjugated (bs-13969R) at 1:300 dilution and 4˚C overnight incubation. (biossusa.com)
It was subsequently shown that this antibody also cross reacts with the C5b-8 complex and purified C8 alpha-gamma. (abcam.com)
To study the effect of MAC on HMEC expression of DAF, EC monolayers were opsonised with IgG2a anti-endoglin monoclonal antibody, thus optimising complement fixation ability. (biomedcentral.com)

The aE11 monoclonal was first reported to bind to a neoepitope exposed on polymerized C9 when incorporated into the human terminal complement complex (PubMed ID: 4035298). (abcam.com)
aHUS is associated with deregulated complement systems, and is treated with eculizumab, a terminal C5 complement inhibitor [ 1 , 2 ]. (clinmedjournals.org)

Ehrlich and Morgan termed this factor complement. (medscape.com)

The presence/absence of this ligand is linked to alternate conformations of the amino acids implicated in C8/C9 binding. (ox.ac.uk)

Now, we know that complement system, protecting the host through innate immune system, could trigger harmful endothelial pathogenesis. (biomedcentral.com)

How do endothelial cells (ECs) protect themselves against damage by complement, particularly when they are present at the interface between blood and inflamed tissue? (biomedcentral.com)
The combined effects of complement activation, dysregulated neutrophilia, endothelial injury, and hypercoagulability appear to be intertwined to drive the severe features of COVID-19. (kegg.jp)

Kupffer cells and other macrophage cell types help clear complement-coated pathogens. (wikidoc.org)

The pathogenesis of pregnancy-associated aHUS associated with defects in complement regulatory systems, which may be unmasked during pregnancy, a compliment-amplifying state [ 5 , 7 ]. (clinmedjournals.org)

In the early 20th century, this controversy was resolved when it was understood that complement can act in combination with specific antibodies, or on its own in a non-specific way. (wikidoc.org)

This dual role of the complement must be nature's rule just like normal hemostasis, which protects human lives in external bodily injury, but also may harm human lives in intravascular injury through thrombogenesis. (biomedcentral.com)
Type I human complement C2 deficiency. (wikidoc.org)
Primary structure of human complement component C2. (wikidoc.org)

Complement component 8 aids in a part of the body's immune response known as the complement system. (medlineplus.gov)
People with complement component 8 deficiency have a significantly increased risk of developing recurrent infections, particularly by Neisseria meningitidis , which causes meningitis, a serious condition that involves inflammation of the membranes surrounding the brain and spinal cord. (medlineplus.gov)
C8B gene mutations involved in complement component 8 deficiency are most often of a type called a C to T transition, in which a DNA building block (nucleotide) called cytosine (C) is changed to the nucleotide thymine (T). Most commonly, this change occurs in a region of the gene called exon 9, but it can occur in other regions. (medlineplus.gov)
Deficiency of the eighth component of complement associated with recurrent meningococcal meningitis--case report and literature review. (medlineplus.gov)
The defect in persons with Leiner disease is usually attributed to a defect of the fifth component of complement (C5). (medscape.com)
However, a child was described by Sonea and associates who had Leiner disease associated with diminished C3, and another was described by Goodyear and Harper with a low level of the fourth component of complement and reduced neutrophil mobility. (medscape.com)
Ehrlich therefore named this heat-labile component "complement", because it is something in the blood which "complements" the cells of the immune system. (wikidoc.org)

Binding of factor H to C3b increases its inactivation by factor I. Properdin stabilizes it, preventing its inactivation by factors H and I. The alternate pathway does not result in a truly nonspecific activation of complement because it requires specific types of compounds for activation. (medscape.com)
The accumulation of anaphylatoxins (such as C5a) from complement activation might also have a role. (medscape.com)

complement C1q A chain [Source:HGNC Sy. (gsea-msigdb.org)
complement C8 alpha chain [Source:HGNC. (gsea-msigdb.org)

The term "complement" was introduced by Paul Ehrlich in the late 1890s, as part of his larger theory of the immune system. (wikidoc.org)
Ehrlich believed that each antigen-specific amboceptor had its own specific complement, while Bordet believed that there is only one type of complement. (wikidoc.org)

Given that MAC is the end of the immune system's complement pathway, and because there's such a strong link between these rare variants and disease, we think that targeting it may be a more effective strategy to control AMD," Swaroop said. (vaccar.biz)
Anand Swaroop et al, Ultra-rare complement factor 8 coding variants in families with age-related macular degeneration, iScience (2023). (vaccar.biz)

The complement system is activated as part of the immune response. (spermidinelife.com)

Experience the perfect fusion of form and function with our Audi S6 / A6 C8 M4 Style Carbon Fiber Trunk Spoiler. (bimmerplug.com)
Each crystal form led to a crystal structure at high resolution (1.15, 1.35 and 1.8 A). In one of these structures the electron-density map shows an as yet unidentified small molecule in the predicted C8/C9-binding site. (ox.ac.uk)

Anatomy15

Organisms10

Diseases16

Chemicals and Drugs101

Analytical, Diagnostic and Therapeutic Techniques and Equipment25

Phenomena and Processes48

Disciplines and Occupations2

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Health Care1

Complement component C8gamma is expressed in human fetal and adult kidney independent of C8alpha. (1/110)

Increased ion permeability of planar lipid bilayer membranes after treatment with the C5b-9 cytolytic attack mechanism of complement. (2/110)

The role of Fcgamma receptor polymorphisms and C3 in the immune defence against Neisseria meningitidis in complement-deficient individuals. (3/110)

Free radicals upregulate complement expression in rabbit isolated heart. (4/110)

CD59 protects rat kidney from complement mediated injury in collaboration with crry. (5/110)

Hypochlorite-induced alterations to canine serum complement. (6/110)

Novel mechanism of antibody-independent complement neutralization of herpes simplex virus type 1. (7/110)

Human complement protein C8 gamma. (8/110)

Complement C3

Complement C4

Complement C4a

Complement C3a

Complement C1q

Complement C5a

Complement Activation

Complement C4b

Complement C5

Complement C3b

Complement System Proteins

Complement C6

Complement C3c

Complement C3d

Complement C2

Complement C9

Receptors, Complement

Complement C1s

Complement Membrane Attack Complex

Complement C1r

Complement Inactivator Proteins

Complement C7

Complement C3-C5 Convertases

Complement Factor B

Complement Pathway, Alternative

Complement Pathway, Classical

Complement C8

Complement C1

Receptors, Complement 3b

Complement Factor H

Complement C5b

Complement C2a

Receptor, Anaphylatoxin C5a

Complement Activating Enzymes

Complement Inactivating Agents

Complement Hemolytic Activity Assay

Complement C1 Inactivator Proteins

Receptors, Complement 3d

Anaphylatoxins

Complement Fixation Tests

Complement Factor D

Complement Factor I

Complement C4b-Binding Protein

Complement C3b Inactivator Proteins

Antigens, CD55

Complement C3-C5 Convertases, Classical Pathway

Complement C2b

Antigens, CD59

Cobra Venoms

Antigen-Antibody Complex

Steroid 21-Hydroxylase

Complement C3-C5 Convertases, Alternative Pathway

Complement C1 Inhibitor Protein

Immunoglobulin G

Hemolysis

Complement C3 Convertase, Alternative Pathway

Complement C5 Convertase, Classical Pathway

Molecular Sequence Data

Complement C3 Convertase, Classical Pathway

Antigens, CD46

Opsonin Proteins

Blood Proteins

Lupus Erythematosus, Systemic

Complement C5 Convertase, Alternative Pathway

Phagocytosis

Amino Acid Sequence

Complement Pathway, Mannose-Binding Lectin

Properdin

Complement C5a, des-Arginine

Mice, Inbred C57BL

Macrophage-1 Antigen

Protein Binding

Neutrophils

Base Sequence

Kidney Glomerulus

Serum

Glomerulonephritis, Membranoproliferative

Immunoglobulin M

Schistosoma

Genetic Complementation Test