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.
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.
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.
A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.
A G-protein-coupled receptor that signals an increase in intracellular calcium in response to the potent ANAPHYLATOXIN peptide COMPLEMENT C5A.
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.
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.
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).
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 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.
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.
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.
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).
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.
An acute hypersensitivity reaction due to exposure to a previously encountered ANTIGEN. The reaction may include rapidly progressing URTICARIA, respiratory distress, vascular collapse, systemic SHOCK, and death.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
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.
Granulated cells that are found in almost all tissues, most abundantly in the skin and the gastrointestinal tract. Like the BASOPHILS, mast cells contain large amounts of HISTAMINE and HEPARIN. Unlike basophils, mast cells normally remain in the tissues and do not circulate in the blood. Mast cells, derived from the bone marrow stem cells, are regulated by the STEM CELL FACTOR.
Rare, autosomal recessive disorder caused by deficiency of the beta 2 integrin receptors (RECEPTORS, LEUKOCYTE-ADHESION) comprising the CD11/CD18 family of glycoproteins. The syndrome is characterized by abnormal adhesion-dependent functions, especially defective tissue emigration of neutrophils, leading to recurrent infection.
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.
Cell-surface glycoprotein beta-chains that are non-covalently linked to specific alpha-chains of the CD11 family of leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE-ADHESION). A defect in the gene encoding CD18 causes LEUKOCYTE-ADHESION DEFICIENCY SYNDROME.
Protective measures against unauthorized access to or interference with computer operating systems, telecommunications, or data structures, especially the modification, deletion, destruction, or release of data in computers. It includes methods of forestalling interference by computer viruses or so-called computer hackers aiming to compromise stored data.
The privacy of information and its protection against unauthorized disclosure.
The state of being free from intrusion or disturbance in one's private life or affairs. (Random House Unabridged Dictionary, 2d ed, 1993)
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.
A plant genus of the family POLYGONACEAE that is used as an EDIBLE GRAIN. Although the seeds are used as cereal, the plant is not one of the cereal grasses (POACEAE).
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
Professional medical personnel who provide care to patients in an organized facility, institution or agency.

Chimeric receptors of the human C3a receptor and C5a receptor (CD88). (1/117)

Chimeras were generated between the human anaphylatoxin C3a and C5a receptors (C3aR and C5aR, respectively) to define the structural requirements for ligand binding and discrimination. Chimeric receptors were generated by systematically exchanging between the two receptors four receptor modules (the N terminus, transmembrane regions 1 to 4, the second extracellular loop, and transmembrane region 5 to the C terminus). The mutants were transiently expressed in HEK-293 cells (with or without Galpha-16) and analyzed for cell surface expression, binding of C3a and C5a, and functional responsiveness (calcium mobilization) toward C3a, C5a, and a C3a as well as a C5a analogue peptide. The data indicate that in both anaphylatoxin receptors the transmembrane regions and the second extracellular loop act as a functional unit that is disrupted by any reciprocal exchange. N-terminal substitution confirmed the two-binding site model for the human C5aR, in which the receptor N terminus is required for high affinity binding of the native ligand but not a C5a analogue peptide. In contrast, the human C3a receptor did not require the original N terminus for high affinity binding of and activation by C3a, a result that was confirmed by N-terminal deletion mutants. This indicates a completely different binding mode of the anaphylatoxins to their corresponding receptors. The C5a analogue peptide, but not C5a, was an agonist of the C3aR. Replacement of the C3aR N terminus by the C5aR sequence, however, lead to the generation of a true hybrid C3a/C5a receptor, which bound and functionally responded to both ligands, C3a and C5a.  (+info)

C3A binds to the seven transmembrane anaphylatoxin receptor expressed by epithelial cells and triggers the production of IL-8. (2/117)

The complement (C) plays an important role in many acute inflammatory processes. C3a is an inflammatory polypeptide named anaphylatoxin, generated during C activation and which acts through a specific receptor C3aR. In this study, we demonstrated that the epithelial cell line ECV 304 constitutively expressed C3aR (by flow cytometry and immunofluorescence) and that binding of purified C3a to epithelial cells resulted in a time- and dose-dependent upregulation of interleukin-8 (IL-8). Pre-treatment of ECV 304 with pertussis toxin inhibited IL-8 response induced by C3a, indicating that the action of C3a was mediated by a G protein coupled pathway.  (+info)

In-vitro activation of complement system by lactic acidosis in newborn and adults. (3/117)

INTRODUCTION: Complement activation occurs secondary to a variety of external stimuli. Lactic acidosis has been previously shown to activate the complement factors C3a and C5a. In the present investigation we examined the differential effect of lactic acidosis on anaphylatoxin levels in cord and adult blood. Furthermore we aimed to determine if the entire complement cascade could be activated by lactic acidosis. METHODS: Cord and adult blood samples (n = 20 each) were collected and incubated for one hour in either untreated condition or with the addition of lactate in two concentrations (5.5 mmol/l vs. 22 mmol/l). Following incubation, levels of C3a, C5a and sC5b-9, and blood gas parameters were determined. RESULTS: Anaphylatoxin (C3a and C5a) and sC5b-9 levels increased with the addition of lactate in a dose-dependent manner in cord and adult blood (C3a: 1 h, 5.5 mmo/l, 22 mmol/l: 418/498/622 microg/l in cord blood; 1010/1056/1381 microg/l in adult blood, p<0,05; similar results were found for C5a and sC5b-9). CONCLUSION: Lactic acidosis leads to an activation of the entire complement system in neonates and in adults. This activation is dose-dependent and more pronounced in adults as compared to neonates.  (+info)

Application of C1-esterase inhibitor during reperfusion of ischemic myocardium: dose-related beneficial versus detrimental effects. (4/117)

BACKGROUND: Complement activation during reperfusion of ischemic myocardium augments myocardial injury, and complement inhibition with C1-esterase inhibitor (C1-INH) at the time of reperfusion exerts marked cardioprotective effects in experimental studies. Application of C1-INH in newborns, however, was recently reported to have dangerous and even lethal side effects. This study addresses the essential role of dosage in studies using C1-INH. METHODS AND RESULTS: Cardioprotection by C1-INH was examined in a pig model with 60 minutes of coronary occlusion followed by 120 minutes of reperfusion. C1-INH was administered intravenously 5 to 10 minutes before coronary reperfusion without heparin at a dose of 40, 100, and 200 IU/kg body wt. Compared with the NaCl controls, C1-INH 40 IU/kg reduced myocardial injury (44.1+/-13.8% versus 76.7+/-4.6% necrosis of area at risk, P/=100 IU/kg) of C1-INH will provoke detrimental side effects, probably via its procoagulatory action.  (+info)

The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des-Arg(74). (5/117)

The substantial variations in the responses of cells to the anaphylatoxin C5a and its desarginated form, C5adR(74), suggest that more than one type of cell surface receptor for these ligands might exist. However, only a single receptor for C5a and C5adR(74), CD88, has been characterized to date. Here we report that the orphan receptor C5L2/gpr77, which shares 35% amino acid identity with CD88, binds C5a with high affinity but has a 10-fold higher affinity for C5adR(74) than CD88. C5L2 also has a moderate affinity for anaphylatoxin C3a, but cross-competition studies suggest that C3a binds to a distinct site from C5a. C4a was able to displace C3a, suggesting that C5L2, like the C3a receptor, may have a low binding affinity for this anaphylatoxin. Unlike CD88 and C3a receptor, C5L2 transfected into RBL-2H3 cells does not support degranulation or increases in intracellular [Ca(2+)] and is not rapidly internalized in response to ligand binding. However, ligation of C5L2 by anaphylatoxin did potentiate the degranulation response to cross-linkage of the high affinity IgE receptor by a pertussis toxin-sensitive mechanism. These results suggest that C5L2 is an anaphylatoxin-binding protein with unique ligand binding and signaling properties.  (+info)

Effects of human soluble thrombomodulin on experimental glomerulonephritis. (6/117)

BACKGROUND: Coagulation and inflammation are both important processes that contribute to glomerular injury. The present study was performed to evaluate the effects of recombinant human soluble thrombomodulin (RHS-TM) in a lethal model of thrombotic glomerulonephritis and to investigate the possible mechanisms. METHODS: Thrombotic glomerulonephritis was induced in rats by administration of lipopolysaccharide and rabbit anti-rat glomerular basement membrane antibody. One hour later, RHS-TM or heparin was administered, and the histological findings, renal functions, and coagulation parameters were evaluated. To evaluate the contribution of carboxypeptidase R (CPR) to the results obtained in rats treated with RHS-TM, plasma CPR levels were measured. Then, carboxypeptidase inhibitor (CPI), which prevents the function of CPR, was administered. RESULTS: Massive glomerular thrombosis and lung hemorrhage developed within five hours of disease induction, and all rats died within 24 hours. RHS-TM (3 mg/kg) prevented the progression of the disease and all rats survived. Heparin (250 U/kg/h) showed similar anti-thrombotic effect, but induced massive hemorrhage in the lungs or stomach. RHS-TM attenuated leukocyte/neutrophil infiltration in the glomerulus but heparin did not, suggesting that RHS-TM has anti-inflammatory properties. CPR levels in plasma were about threefold higher in rats treated with RHS-TM compared to those in rats treated with heparin. Furthermore, the inhibitory effect of RHS-TM on leukocyte/neutrophil infiltration was significantly diminished by injection of CPI. CONCLUSION: RHS-TM effectively attenuates the injuries of thrombotic glomerulonephritis in rats. The results indicate that RHS-TM, in addition to its anti-thrombotic action, may exert its anti-inflammatory properties by converting proCPR to CPR, which then inactivates anaphylatoxins. RHS-TM is a potential novel therapeutic tool for thrombotic glomerular injury and related disorders.  (+info)

Complement c3a and c5a induce different signal transduction cascades in endothelial cells. (7/117)

In leukocytes, C3a and C5a cause chemotaxis in a G(i)-dependent, pertussis toxin (PT)-sensitive fashion. Because we found that HUVECs and immortalized human dermal microvascular endothelial cells express small numbers of C3aRs and C5aRs, we asked what the function of these receptors was on these cells. Activation of the C3aR caused transient formation of actin stress fibers, which was not PT-sensitive, but depended on rho activation implying coupling to G(alpha12) or G(alpha13). Activation of the C5aR caused a delayed and sustained cytoskeletal response, which was blocked by PT, and resulted in cell retraction, increased paracellular permeability, and facilitated eosinophil transmigration. C5a, but not C3a, was chemotactic for human immortalized dermal microvascular endothelial cells. The response to C5a was blocked by inhibitors of phosphatidylinositol-3-kinase, src kinase, and of the epidermal growth factor (EGF) receptor (EGFR) as well as by neutralizing Abs against the EGFR and heparin-binding EGF-like factor. Furthermore, immune precipitations showed that the EGFR was phosphorylated following stimulation with C5a. The C5aR in endothelial cells thus uses a signaling cascade-transactivation of the EGFR-that does not exist in leukocytes, while the C3aR couples to a different G protein, presumably G(alpha12/13).  (+info)

Complement component anaphylatoxins upregulate chemokine expression by human astrocytes. (8/117)

The complement (C) system, a major component of the innate immune system, has been described as a factor implicated in some brain disorders. C activation leads to the release of anaphylatoxins, two proinflammatory polypeptides acting through specific receptors that have been detected on brain cells. Here, we examined the effect of anaphylatoxins on chemokine expression by human astrocytes. We showed that anaphylatoxins significantly increase chemokine mRNA expression. However, anaphylatoxin-induced chemokine secretion (interleukin-8) was observed only in the presence of interleukin-1beta. Thus, anaphylatoxins could initiate a chemokine cascade and, at least in part, be involved in pathogenesis of the brain.  (+info)

Anaphylatoxins are a group of small protein molecules that are released during an immune response, specifically as a result of the activation of the complement system. The term "anaphylatoxin" comes from their ability to induce anaphylaxis, a severe and rapid allergic reaction. There are three main anaphylatoxins, known as C3a, C4a, and C5a, which are derived from the cleavage of complement components C3, C4, and C5, respectively.

Anaphylatoxins play a crucial role in the immune response by attracting and activating various immune cells, such as neutrophils, eosinophils, and mast cells, to the site of infection or injury. They also increase vascular permeability, causing fluid to leak out of blood vessels and leading to tissue swelling. Additionally, anaphylatoxins can induce smooth muscle contraction, which can result in bronchoconstriction and hypotension.

While anaphylatoxins are important for the immune response, they can also contribute to the pathogenesis of various inflammatory diseases, such as asthma, arthritis, and sepsis. Therefore, therapies that target the complement system and anaphylatoxin production have been developed and are being investigated as potential treatments for these conditions.

Complement C3a is a protein fragment that is generated during the activation of the complement system, which is a part of the immune system. The complement system helps to eliminate pathogens and damaged cells from the body by marking them for destruction and attracting immune cells to the site of infection or injury.

C3a is produced when the third component of the complement system (C3) is cleaved into two smaller fragments, C3a and C3b, during the complement activation cascade. C3a is a potent anaphylatoxin, which means it can cause the release of histamine and other mediators from mast cells and basophils, leading to inflammation, increased vascular permeability, and smooth muscle contraction.

C3a also has chemotactic properties, meaning it can attract immune cells such as neutrophils and monocytes to the site of complement activation. Additionally, C3a can modulate the activity of various immune cells, including dendritic cells, T cells, and B cells, and play a role in the regulation of the adaptive immune response.

It's important to note that while C3a has important functions in the immune response, uncontrolled or excessive activation of the complement system can lead to tissue damage and inflammation, contributing to the pathogenesis of various diseases such as autoimmune disorders, inflammatory diseases, and allergies.

Complement C5a is a protein fragment that is generated during the activation of the complement system, which is a part of the immune system. The complement system helps to eliminate pathogens and damaged cells from the body by tagging them for destruction and attracting immune cells to the site of infection or injury.

C5a is formed when the fifth component of the complement system (C5) is cleaved into two smaller fragments, C5a and C5b, during the complement activation cascade. C5a is a potent pro-inflammatory mediator that can attract and activate various immune cells, such as neutrophils, monocytes, and eosinophils, to the site of infection or injury. It can also increase vascular permeability, promote the release of histamine, and induce the production of reactive oxygen species, all of which contribute to the inflammatory response.

However, excessive or uncontrolled activation of the complement system and generation of C5a can lead to tissue damage and inflammation, contributing to the pathogenesis of various diseases, such as sepsis, acute respiratory distress syndrome (ARDS), and autoimmune disorders. Therefore, targeting C5a or its receptors has been explored as a potential therapeutic strategy for these conditions.

Lysine carboxypeptidase is not a widely recognized or used medical term. However, in biochemistry, carboxypeptidases are enzymes that cleave peptide bonds at the carboxyl-terminal end of a protein or peptide. If there is a specific enzyme named "lysine carboxypeptidase," it would be an enzyme that selectively removes lysine residues from the carboxyl terminus of a protein or peptide.

There are several enzymes that can act as carboxypeptidases, and some of them have specificities for certain amino acids, such as arginine or lysine. These enzymes play important roles in various biological processes, including protein degradation, processing, and regulation.

It's worth noting that the term "lysine carboxypeptidase" may refer to different enzymes depending on the context, such as bacterial or mammalian enzymes, and they may have different properties and functions.

The term "Receptor, Anaphylatoxin C5a" refers to a specific type of receptor found on the surface of various cells in the human body, including immune cells and endothelial cells. This receptor binds to a molecule called C5a, which is a cleavage product of the complement component C5 and is one of the most potent anaphylatoxins.

Anaphylatoxins are inflammatory mediators that play a crucial role in the immune response, particularly in the activation of the complement system and the recruitment of immune cells to sites of infection or injury. C5a is generated during the activation of the complement system and has a wide range of biological activities, including chemotaxis (attracting immune cells to the site of inflammation), increased vascular permeability, and the activation of immune cells such as neutrophils, monocytes, and mast cells.

The C5a receptor, also known as CD88, is a G protein-coupled receptor that belongs to the superfamily of seven transmembrane domain receptors. When C5a binds to the receptor, it triggers a series of intracellular signaling events that lead to the activation of various cellular responses, such as the release of inflammatory mediators and the recruitment of immune cells to the site of inflammation.

Abnormal activation of the C5a/C5a receptor pathway has been implicated in a variety of inflammatory diseases, including sepsis, acute respiratory distress syndrome (ARDS), and autoimmune disorders. Therefore, targeting this pathway with therapeutic agents has emerged as a promising strategy for the treatment of these conditions.

Complement C4a is a protein fragment or cleavage product generated during the activation of the complement system, which is a part of the immune system. The complement system helps to eliminate pathogens and damaged cells by marking them for destruction and direct lysis. Complement component 4 (C4) is one of the key proteins in this cascade, and it gets cleaved into C4a and C4b during the activation process.

C4a is a small anaphylatoxin with a molecular weight of approximately 9 kDa. It has chemotactic properties, meaning it can attract immune cells like neutrophils to the site of complement activation. Additionally, C4a can induce histamine release from mast cells and basophils, contributing to local inflammation. However, its precise physiological role in the immune response is not entirely clear, and dysregulation of C4a production has been implicated in several pathological conditions, such as autoimmune diseases and allergies.

Complement C5 is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to eliminate pathogens and damaged cells from the body. The complement system is a complex series of biochemical reactions that help to identify and destroy foreign substances, such as bacteria and viruses.

Complement C5 is one of several proteins in the complement system that are activated in a cascading manner in response to an activating event, such as the binding of an antibody to a pathogen. Once activated, Complement C5 can be cleaved into two smaller proteins, C5a and C5b.

C5a is a powerful anaphylatoxin, which means it can cause the release of histamine from mast cells and basophils, leading to inflammation and increased vascular permeability. It also acts as a chemoattractant, drawing immune cells to the site of infection or injury.

C5b, on the other hand, plays a role in the formation of the membrane attack complex (MAC), which is a protein structure that can punch holes in the membranes of pathogens, leading to their lysis and destruction.

Overall, Complement C5 is an important component of the immune system's response to infection and injury, helping to eliminate pathogens and damaged cells from the body.

Complement C5a, des-Arginine is a derivative of the complement component C5a. The complement system is a group of proteins that are part of the body's immune defense against foreign invaders such as bacteria and viruses. When activated, the complement system can help to eliminate pathogens by attracting immune cells to the site of infection, promoting inflammation, and directly killing the pathogen.

C5a is a small protein that is generated when the complement component C5 is cleaved during the activation of the complement system. C5a is a potent anaphylatoxin, which means it can cause the release of histamine from mast cells and basophils, leading to increased vascular permeability, smooth muscle contraction, and recruitment of immune cells to the site of infection.

Des-Arginine refers to the removal of an arginine residue from the C-terminus of C5a. This modified form of C5a is known as C5a-desArg and has reduced pro-inflammatory activity compared to intact C5a. However, it can still contribute to the regulation of the immune response by interacting with specific receptors on immune cells.

In summary, Complement C5a, des-Arginine is a derivative of the complement component C5a that has reduced pro-inflammatory activity due to the removal of an arginine residue from its C-terminus.

Complement receptors are proteins found on the surface of various cells in the human body, including immune cells and some non-immune cells. They play a crucial role in the complement system, which is a part of the innate immune response that helps to eliminate pathogens and damaged cells from the body. Complement receptors bind to complement proteins or fragments that are generated during the activation of the complement system. This binding triggers various intracellular signaling events that can lead to diverse cellular responses, such as phagocytosis, inflammation, and immune regulation.

There are several types of complement receptors, including:

1. CR1 (CD35): A receptor found on erythrocytes, B cells, neutrophils, monocytes, macrophages, and glomerular podocytes. It functions in the clearance of immune complexes and regulates complement activation.
2. CR2 (CD21): Expressed mainly on B cells and follicular dendritic cells. It facilitates antigen presentation, B-cell activation, and immune regulation.
3. CR3 (CD11b/CD18, Mac-1): Present on neutrophils, monocytes, macrophages, and some T cells. It mediates cell adhesion, phagocytosis, and intracellular signaling.
4. CR4 (CD11c/CD18, p150,95): Expressed on neutrophils, monocytes, macrophages, and dendritic cells. It is involved in cell adhesion, phagocytosis, and intracellular signaling.
5. C5aR (CD88): Found on various immune cells, including neutrophils, monocytes, macrophages, mast cells, eosinophils, and dendritic cells. It binds to the complement protein C5a and mediates chemotaxis, degranulation, and inflammation.
6. C5L2 (GPR77): Present on various cell types, including immune cells. Its function is not well understood but may involve regulating C5a-mediated responses or acting as a receptor for other ligands.

These receptors play crucial roles in the immune response and inflammation by mediating various functions such as chemotaxis, phagocytosis, cell adhesion, and intracellular signaling. Dysregulation of these receptors has been implicated in several diseases, including autoimmune disorders, infections, and cancer.

Complement C3 is a protein that plays a central role in the complement system, which is a part of the immune system that helps to clear pathogens and damaged cells from the body. Complement C3 can be activated through three different pathways: the classical pathway, the lectin pathway, and the alternative pathway. Once activated, it breaks down into two fragments, C3a and C3b.

C3a is an anaphylatoxin that helps to recruit immune cells to the site of infection or injury, while C3b plays a role in opsonization, which is the process of coating pathogens or damaged cells with proteins to make them more recognizable to the immune system. Additionally, C3b can also activate the membrane attack complex (MAC), which forms a pore in the membrane of target cells leading to their lysis or destruction.

In summary, Complement C3 is an important protein in the complement system that helps to identify and eliminate pathogens and damaged cells from the body through various mechanisms.

Complement activation is the process by which the complement system, a part of the immune system, is activated to help eliminate pathogens and damaged cells from the body. The complement system consists of a group of proteins that work together to recognize and destroy foreign substances.

Activation of the complement system can occur through three different pathways: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of proteolytic reactions that ultimately result in the formation of the membrane attack complex (MAC), which creates a pore in the membrane of the target cell, leading to its lysis and removal.

The classical pathway is typically activated by the binding of antibodies to antigens on the surface of a pathogen or damaged cell. The lectin pathway is activated by the recognition of specific carbohydrate structures on the surface of microorganisms. The alternative pathway can be spontaneously activated and serves as an amplification loop for both the classical and lectin pathways.

Complement activation plays a crucial role in the immune response, but uncontrolled or excessive activation can also lead to tissue damage and inflammation. Dysregulation of complement activation has been implicated in various diseases, including autoimmune disorders, inflammatory conditions, and neurodegenerative diseases.

Complement C4 is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to clear pathogens and damaged cells from the body. Complement C4 is involved in the early stages of the complement activation cascade, where it helps to identify and tag foreign or abnormal cells for destruction by other components of the immune system.

Specifically, Complement C4 can be cleaved into two smaller proteins, C4a and C4b, during the complement activation process. C4b then binds to the surface of the target cell and helps to initiate the formation of the membrane attack complex (MAC), which creates a pore in the cell membrane and leads to lysis or destruction of the target cell.

Deficiencies or mutations in the Complement C4 gene can lead to various immune disorders, including certain forms of autoimmune diseases and susceptibility to certain infections.

The complement system is a group of proteins found in the blood and on the surface of cells that when activated, work together to help eliminate pathogens such as bacteria, viruses, and fungi from the body. The proteins are normally inactive in the bloodstream. When they encounter an invading microorganism or foreign substance, a series of reactions take place leading to the activation of the complement system. Activation results in the production of effector molecules that can punch holes in the cell membranes of pathogens, recruit and activate immune cells, and help remove debris and dead cells from the body.

There are three main pathways that can lead to complement activation: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of proteins that work together in a cascade-like manner to amplify the response and generate effector molecules. The three main effector molecules produced by the complement system are C3b, C4b, and C5b. These molecules can bind to the surface of pathogens, marking them for destruction by other immune cells.

Complement proteins also play a role in the regulation of the immune response. They help to prevent excessive activation of the complement system, which could damage host tissues. Dysregulation of the complement system has been implicated in a number of diseases, including autoimmune disorders and inflammatory conditions.

In summary, Complement System Proteins are a group of proteins that play a crucial role in the immune response by helping to eliminate pathogens and regulate the immune response. They can be activated through three different pathways, leading to the production of effector molecules that mark pathogens for destruction. Dysregulation of the complement system has been linked to various diseases.

Cobra venoms are a type of snake venom that is produced by cobras, which are members of the genus Naja in the family Elapidae. These venoms are complex mixtures of proteins and other molecules that have evolved to help the snake immobilize and digest its prey.

Cobra venoms typically contain a variety of toxic components, including neurotoxins, hemotoxins, and cytotoxins. Neurotoxins target the nervous system and can cause paralysis and respiratory failure. Hemotoxins damage blood vessels and tissues, leading to internal bleeding and organ damage. Cytotoxins destroy cells and can cause tissue necrosis.

The specific composition of cobra venoms can vary widely between different species of cobras, as well as between individual snakes of the same species. Some cobras have venoms that are primarily neurotoxic, while others have venoms that are more hemotoxic or cytotoxic. The potency and effects of cobra venoms can also be influenced by factors such as the age and size of the snake, as well as the temperature and pH of the environment.

Cobra bites can be extremely dangerous and even fatal to humans, depending on the species of cobra, the amount of venom injected, and the location of the bite. Immediate medical attention is required in the event of a cobra bite, including the administration of antivenom therapy to neutralize the effects of the venom.

Anaphylaxis is a severe, life-threatening systemic allergic reaction that occurs suddenly after exposure to an allergen (a substance that triggers an allergic reaction) to which the person has previously been sensitized. The symptoms of anaphylaxis include rapid onset of symptoms such as itching, hives, swelling of the throat and tongue, difficulty breathing, wheezing, cough, chest tightness, rapid heartbeat, hypotension (low blood pressure), shock, and in severe cases, loss of consciousness and death. Anaphylaxis is a medical emergency that requires immediate treatment with epinephrine (adrenaline) and other supportive measures to stabilize the patient's condition.

Carboxypeptidases are a group of enzymes that catalyze the cleavage of peptide bonds at the carboxyl-terminal end of polypeptides or proteins. They specifically remove the last amino acid residue from the protein chain, provided that it has a free carboxyl group and is not blocked by another chemical group. Carboxypeptidases are classified into two main types based on their catalytic mechanism: serine carboxypeptidases and metallo-carboxypeptidases.

Serine carboxypeptidases, also known as chymotrypsin C or carboxypeptidase C, use a serine residue in their active site to catalyze the hydrolysis of peptide bonds. They are found in various organisms, including animals and bacteria.

Metallo-carboxypeptidases, on the other hand, require a metal ion (usually zinc) for their catalytic activity. They can be further divided into several subtypes based on their structure and substrate specificity. For example, carboxypeptidase A prefers to cleave hydrophobic amino acids from the carboxyl-terminal end of proteins, while carboxypeptidase B specifically removes basic residues (lysine or arginine).

Carboxypeptidases have important roles in various biological processes, such as protein maturation, digestion, and regulation of blood pressure. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

An antigen-antibody complex is a type of immune complex that forms when an antibody binds to a specific antigen. An antigen is any substance that triggers an immune response, while an antibody is a protein produced by the immune system to neutralize or destroy foreign substances like antigens.

When an antibody binds to an antigen, it forms a complex that can be either soluble or insoluble. Soluble complexes are formed when the antigen is small and can move freely through the bloodstream. Insoluble complexes, on the other hand, are formed when the antigen is too large to move freely, such as when it is part of a bacterium or virus.

The formation of antigen-antibody complexes plays an important role in the immune response. Once formed, these complexes can be recognized and cleared by other components of the immune system, such as phagocytes, which help to prevent further damage to the body. However, in some cases, the formation of large numbers of antigen-antibody complexes can lead to inflammation and tissue damage, contributing to the development of certain autoimmune diseases.

Mast cells are a type of white blood cell that are found in connective tissues throughout the body, including the skin, respiratory tract, and gastrointestinal tract. They play an important role in the immune system and help to defend the body against pathogens by releasing chemicals such as histamine, heparin, and leukotrienes, which help to attract other immune cells to the site of infection or injury. Mast cells also play a role in allergic reactions, as they release histamine and other chemicals in response to exposure to an allergen, leading to symptoms such as itching, swelling, and redness. They are derived from hematopoietic stem cells in the bone marrow and mature in the tissues where they reside.

Leukocyte Adhesion Deficiency Syndrome (LAD) is a group of rare inherited disorders that affect the ability of white blood cells, specifically neutrophils, to adhere to and migrate into tissues, particularly those involved in immune responses. This results in recurrent bacterial and fungal infections starting in infancy.

There are three types of LAD, each caused by different genetic mutations:

1. LAD I: This is the most common and severe form, caused by a deficiency in the CD18 protein which is crucial for neutrophil adhesion. Symptoms include delayed separation of the umbilical cord, severe periodontal disease, and recurrent skin, lung and gastrointestinal infections.

2. LAD II: Also known as congenital disorder of glycosylation, type Ib, it is caused by a deficiency in the enzyme glucosyltransferase, leading to abnormal sugar chains on cell surfaces. Symptoms are similar to LAD I but less severe, and also include mental retardation and impaired growth.

3. LAD III: This is the least common form, caused by a defect in the integrin-linked kinase (ILK) gene. It results in a more complex phenotype with muscular and cardiac abnormalities, in addition to immune dysfunction.

Treatment typically involves prophylactic antibiotics, granulocyte-colony stimulating factor (G-CSF) to increase neutrophil counts, and sometimes bone marrow transplantation.

Complement receptor 3b (CR3b or CD11b/CD18) is not a medical definition itself, but I can provide you with the relevant information regarding this term.

Complement receptor 3 (CR3) is a heterodimeric receptor consisting of two subunits, CD11b (also known as Mac-1 or CR3 alpha) and CD18 (also known as beta2 integrin). There are two forms of the CD11b/CD18 heterodimer: CR3a (CD11b/CD18) and CR3b (CD11b/CD18'). The difference between these two forms lies in the conformation of the CD11b subunit.

Complement receptor 3b (CR3b or CD11b/CD18') is a less common form of the CR3 receptor, which is primarily expressed on myeloid cells such as monocytes, macrophages, and neutrophils. CR3b has a higher affinity for complement component C3b and its fragments iC3b and C3dg compared to CR3a.

CR3b plays a role in various immune functions, including:

1. Phagocytosis: Binding of C3b or its fragments to CR3b facilitates the recognition and uptake of opsonized pathogens by phagocytes.
2. Adhesion: The integrin component of CR3b mediates cell-cell and cell-matrix interactions, contributing to leukocyte migration and recruitment to sites of inflammation or infection.
3. Intracellular signaling: Activation of CR3b can lead to intracellular signaling events that modulate immune responses, such as the release of pro-inflammatory cytokines and reactive oxygen species.

In summary, Complement receptor 3b (CR3b or CD11b/CD18') is a less common form of CR3 primarily expressed on myeloid cells that binds complement component C3b and its fragments with high affinity, mediating phagocytosis, adhesion, and intracellular signaling.

CD18 is a type of protein called an integrin that is found on the surface of many different types of cells in the human body, including white blood cells (leukocytes). It plays a crucial role in the immune system by helping these cells to migrate through blood vessel walls and into tissues where they can carry out their various functions, such as fighting infection and inflammation.

CD18 forms a complex with another protein called CD11b, and together they are known as Mac-1 or CR3 (complement receptor 3). This complex is involved in the recognition and binding of various molecules, including bacterial proteins and fragments of complement proteins, which help to trigger an immune response.

CD18 has been implicated in a number of diseases, including certain types of cancer, inflammatory bowel disease, and rheumatoid arthritis. Mutations in the gene that encodes CD18 can lead to a rare disorder called leukocyte adhesion deficiency (LAD) type 1, which is characterized by recurrent bacterial infections and impaired wound healing.

Computer security, also known as cybersecurity, is the protection of computer systems and networks from theft, damage, or unauthorized access to their hardware, software, or electronic data. This can include a wide range of measures, such as:

* Using firewalls, intrusion detection systems, and other technical safeguards to prevent unauthorized access to a network
* Encrypting sensitive data to protect it from being intercepted or accessed by unauthorized parties
* Implementing strong password policies and using multi-factor authentication to verify the identity of users
* Regularly updating and patching software to fix known vulnerabilities
* Providing security awareness training to employees to help them understand the risks and best practices for protecting sensitive information
* Having a incident response plan in place to quickly and effectively respond to any potential security incidents.

The goal of computer security is to maintain the confidentiality, integrity, and availability of computer systems and data, in order to protect the privacy and safety of individuals and organizations.

Confidentiality is a legal and ethical principle in medicine that refers to the obligation of healthcare professionals to protect the personal and sensitive information of their patients. This information, which can include medical history, diagnosis, treatment plans, and other private details, is shared between the patient and the healthcare provider with the expectation that it will be kept confidential and not disclosed to third parties without the patient's consent.

Confidentiality is a fundamental component of the trust relationship between patients and healthcare providers, as it helps to ensure that patients feel safe and comfortable sharing sensitive information with their doctors, nurses, and other members of their healthcare team. It also helps to protect patients' privacy rights and uphold their autonomy in making informed decisions about their healthcare.

There are some limited circumstances in which confidentiality may be breached, such as when there is a legal obligation to report certain types of information (e.g., suspected child abuse or neglect), or when the disclosure is necessary to protect the health and safety of the patient or others. However, these exceptions are typically narrowly defined and subject to strict guidelines and safeguards to ensure that confidentiality is protected as much as possible.

In the context of healthcare, privacy is often referred to as the state of being free from unauthorized intrusion or observation in regards to one's personal health information. This includes maintaining confidentiality, restricting access to only those who have a legitimate need for the information, and protecting the information from being shared, disclosed, or used inappropriately. It is a fundamental right of individuals and is essential for maintaining trust in the healthcare system.

Inflammation is a complex biological response of tissues to harmful stimuli, such as pathogens, damaged cells, or irritants. It is characterized by the following signs: rubor (redness), tumor (swelling), calor (heat), dolor (pain), and functio laesa (loss of function). The process involves the activation of the immune system, recruitment of white blood cells, and release of inflammatory mediators, which contribute to the elimination of the injurious stimuli and initiation of the healing process. However, uncontrolled or chronic inflammation can also lead to tissue damage and diseases.

'Fagopyrum' is the genus name for buckwheat plants, which belong to the family Polygonaceae. There are several species within this genus, including Fagopyrum esculentum (common buckwheat) and Fagopyrum tataricum (Tartary buckwheat). These plants are not related to wheat or grasses, despite their name. They are important crops in some parts of the world, particularly in Asia, and their seeds are used as a source of food and flour. Buckwheat is also valued for its high protein content and unique nutritional profile.

I'm sorry for any confusion, but "Internet" is a term that pertains to the global network of interconnected computers and servers that enable the transmission and reception of data via the internet protocol (IP). It is not a medical term and does not have a specific medical definition. If you have any questions related to medicine or health, I'd be happy to try to help answer them for you!

Medical staff, in a hospital or healthcare setting, typically refers to licensed healthcare professionals who are responsible for providing medical care and treatment to patients. This can include physicians (both specialists and general practitioners), surgeons, dentists, podiatrists, and advanced practice nurses (such as nurse practitioners and certified nurse midwives).

The term "medical staff" may also refer to the organized body of such professionals within a healthcare institution, who are responsible for establishing medical policies and procedures, providing clinical leadership, and ensuring quality of care. This group often includes both practicing clinicians and those in administrative or teaching roles. Membership in the medical staff is usually granted through an application and credentialing process, which ensures that each member meets certain professional and educational standards.

Anaphylatoxins, or complement peptides, are fragments (C3a, C4a and C5a) that are produced as part of the activation of the ... Anaphylatoxin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text from the ... Anaphylatoxins are able to trigger degranulation (release of substances) of endothelial cells, mast cells or phagocytes, which ... Anaphylatoxins indirectly mediate: smooth muscle cells contraction, for example bronchospasms increase in the permeability of ...
The anaphylatoxin receptors are a group of G-protein coupled receptors which bind anaphylatoxins. Members of this family ... "Anaphylatoxin Receptors". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology ... "Characterization of receptors to the anaphylatoxins on isolated cells". Dermatologica. 179 Suppl 1: 35-40. doi:10.1159/ ...
The alpha chain may be cleaved to release C4 anaphylatoxin, a mediator of local inflammation. Deficiency of this protein is ... Moon KE, Gorski JP, Hugli TE (Aug 1981). "Complete primary structure of human C4a anaphylatoxin". The Journal of Biological ... Hugli TE (1987). "Biochemistry and biology of anaphylatoxins". Complement. 3 (3): 111-27. doi:10.1159/000467889. PMID 3542363. ...
"Anaphylatoxin Receptors: C5a". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical ... Boulay F, Mery L, Tardif M, Brouchon L, Vignais P (March 1991). "Expression cloning of a receptor for C5a anaphylatoxin on ... Giannini E, Brouchon L, Boulay F (August 1995). "Identification of the major phosphorylation sites in human C5a anaphylatoxin ... Overview of all the structural information available in the PDB for UniProt: P21730 (C5a anaphylatoxin chemotactic receptor 1) ...
Davoust N, Jones J, Stahel PF, Ames RS, Barnum SR (May 1999). "Receptor for the C3a anaphylatoxin is expressed by neurons and ... "Anaphylatoxin Receptors: C3a". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical ... Kirchhoff K, Weinmann O, Zwirner J, Begemann G, Götze O, Kapp A, Werfel T (June 2001). "Detection of anaphylatoxin receptors on ... Sayegh ET, Bloch O, Parsa AT (August 2014). "Complement anaphylatoxins as immune regulators in cancer". Cancer Medicine. 3 (4 ...
C4a is an anaphylatoxin. C3 convertases are unstable (half-life 10 - 20 min) - respectively they are deactivated upon ...
Like other anaphylatoxins, C3a is regulated by cleavage of its carboxy-terminal arginine, which results in a molecule with ... C3a is a 77 residue anaphylatoxin that binds to the C3a receptor (C3aR), a class A G protein-coupled receptor. It plays a large ... C3a, like other anaphylatoxins, has a C-terminal arginine residue. Serum carboxypeptidase B, a protease, cleaves the arginine ... Anaphylatoxins are small complement peptides that induce proinflammatory responses in tissues. C3a is primarily regarded for ...
C5a is a chemotactic agent and an anaphylatoxin; it is essential in the innate immunity but it is also linked with the adaptive ... C5a is an anaphylatoxin, causing increased expression of adhesion molecules on endothelium, contraction of smooth muscle, and ... C5a des-Arg is a much less potent anaphylatoxin. Both C5a and C5a des-Arg can trigger mast cell degranulation, releasing ... Gerard NP, Gerard C (February 1991). "The chemotactic receptor for human C5a anaphylatoxin". Nature. 349 (6310): 614-617. doi: ...
Li R, Coulthard LG, Wu MC, Taylor SM, Woodruff TM (Mar 2013). "C5L2: a controversial receptor of complement anaphylatoxin, C5a ...
"Entrez Gene: P2RY14 purinergic receptor P2Y, G-protein coupled, 14". Gerard C, Gerard NP (1994). "C5A anaphylatoxin and its ...
Li R, Coulthard LG, Wu MC, Taylor SM, Woodruff TM (Mar 2013). "C5L2: a controversial receptor of complement anaphylatoxin, C5a ...
Li R, Coulthard LG, Wu MC, Taylor SM, Woodruff TM (Mar 2013). "C5L2: a controversial receptor of complement anaphylatoxin, C5a ... a second C5a anaphylatoxin chemotactic receptor C5a2 (C5L2), a second C5a receptor of debated function which has the structure ...
Gerard C, Gerard NP (1994). "C5A anaphylatoxin and its seven transmembrane-segment receptor". Annual Review of Immunology. 12 ( ...
Corporale, L. L H.; Tippett, P. S.; Erickson, B. W.; and Hugli, T. E. (1980) The Active Site of C3a Anaphylatoxin. J. Biol. ...
1995). "[Chemico-enzymatic synthesis, cloning and expression of a gene for an analog of human anaphylatoxin C5a]". Bioorg. Khim ... Oppermann M, Götze O (1995). "Plasma clearance of the human C5a anaphylatoxin by binding to leucocyte C5a receptors". ... An activation peptide, C5a, which is an anaphylatoxin that possesses potent spasmogenic and chemotactic activity, is derived ... Fernandez HN, Hugli TE (1978). "Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide ...
It inactivates proteins such as bradykinin and anaphylatoxins in the blood in order to prevent toxic buildup. Lysine ... This enzyme has also proven to be important in inactivating anaphylatoxins which are inflammation-inducing proteins used in ... Skidgel RA, Erdös EG (December 2007). "Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator ... carboxypeptidase is also known as: carboxypeptidase N arginine carboxypeptidase kininase I anaphylatoxin inactivator plasma ...
C5a anaphylatoxin chemotactic receptor 2 is a protein that in humans is encoded by the C5AR2 gene. It's a complement component ... 2007). "Ligand specificity of the anaphylatoxin C5L2 receptor and its regulation on myeloid and epithelial cell lines". J. Biol ... In the case of inappropriate complement activation, anaphylatoxins may be involved in autoimmunity and sepsis. C5a2 is ... "An anti-inflammatory function for the complement anaphylatoxin C5a-binding protein, C5L2". J. Biol. Chem. 280 (48): 39677-80. ...
This enzyme then cleaves C5 to C5a, a potent anaphylatoxin, and C5b. The C5b then recruits and assembles C6, C7, C8 and ... Both C3a and C5a have anaphylatoxin activity, directly triggering degranulation of mast cells as well as increasing vascular ...
"Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. ...
"Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. ...
"Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. ...
The alpha chain may be cleaved to release C4 anaphylatoxin, a mediator of local inflammation. Deficiency of this protein is ...
It is caused by the release (degranulation) of substances from mast cells or basophils under the influence of anaphylatoxins. ...
However, there are some differences between the two molecules, for example unlike C3, TEP1 lacks an anaphylatoxin domain. The ...
While the anaphylatoxin C3a interacts with its C3a receptor (C3aR) to recruit leukocytes, C3b contributes to further downstream ... Like C3a, C5a is also an anaphylatoxin that interacts with its cognate C5a receptor (C5aR) to attract leukocytes. Subsequent ...
Subsequent investigation demonstrated that complement, specifically the anaphylatoxin C5a, can drive the Arthus reaction ... "C5a anaphylatoxin is a major regulator of activating versus inhibitory FcγRs in immune complex-induced lung disease". The ...
The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and ... anaphylatoxin inactivator. This enzyme is a tetramer composed of two identical regulatory subunits and two identical catalytic ...
The C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha ...
C5a anaphylatoxin, follicle-stimulating hormone [FSH], gonadotropin-releasing hormone [GnRH], neurokinin, thyrotropin-releasing ...
In 1914 Hirszfeld was made an academic lecturer on the basis of his work on anaphylaxis and anaphylatoxin and their ...
Anaphylatoxins, or complement peptides, are fragments (C3a, C4a and C5a) that are produced as part of the activation of the ... Anaphylatoxin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text from the ... Anaphylatoxins are able to trigger degranulation (release of substances) of endothelial cells, mast cells or phagocytes, which ... Anaphylatoxins indirectly mediate: smooth muscle cells contraction, for example bronchospasms increase in the permeability of ...
Micrurus venoms can activate the complement system, generating a significant amount of anaphylatoxins, which may assist due to ... Anaphylatoxin concentrations were determined from the standard curves, plotting anaphylatoxin calibrator concentration versus ... Complement activation may generate anaphylatoxins and membrane attack complex (MAC). Anaphylatoxins (C3a, C4a, and C5a) are ... Generation of human serum anaphylatoxins induced by Micrurus spp venoms. Samples (50 μl) of normal human serum (NHS), as ...
Dive into the research topics of Site‐specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in ... N2 - To check and clarify existing data on receptor‐interacting residues in the human C5a anaphylatoxin, we tested mutant C5a ... AB - To check and clarify existing data on receptor‐interacting residues in the human C5a anaphylatoxin, we tested mutant C5a ... Site‐specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in possible interaction with the C5a ...
Expression of the complement anaphylatoxin C3a and C5a receptors on bronchial epithelial and smooth muscle cells in models of ... Structure, function and cellular expression of complement anaphylatoxin receptors. Curr Opin Immunol. Feb 1995. 7(1):48-53. [ ...
The anaphylatoxin (C5) has been linked to excitotoxicity and apoptosis activation in the CNS, which is believed to play an ...
The accumulation of anaphylatoxins (such as C5a) from complement activation might also have a role. ...
... leads to the generation of vasoactive substances and anaphylatoxins. Finally, histamine levels may be increased in stored blood ...
Recombinant Human C5a anaphylatoxin chemotactic receptor (C5AR1). 100ug. 3430.4 EUR Recombinant Human C5a anaphylatoxin ...
C5 convertase activates C5 by cleaving the alpha chain, releasing C5a anaphylatoxin & generating C5b (beta chain + alpha chain ...
Detects compound activity against known and/or orphan G
Anaphylatoxin free Internet: years. dangerous lot Drotein. IPB001881B 12 28 5 free 107-208! 11 JL 11 1 price 0 1 1 1 CL L- V4 1 ...
Expression of the complement anaphylatoxin C3a and C5a receptors on bronchial epithelial and smooth muscle cells in models of ... Structure, function and cellular expression of complement anaphylatoxin receptors. Curr Opin Immunol. Feb 1995. 7(1):48-53. [ ...
C5a anaphylatoxin chemotactic receptor 1. C5AR1. P21730. 1 Reference(s). T00QMT. NA. MIR15B. NA. 1 Reference(s). ...
C3a, C5a, and C4a (weakly) have anaphylatoxin activity: They cause mast cell degranulation, leading to increased vascular ...
C5a exerts a pro-inflammatory effect via the G-protein-coupled receptor C5a anaphylatoxin chemotactic receptor 1 (C5aR1, also ... Activation of the complement cascade generates anaphylatoxins including C5a and C3a. ...
... as well as anaphylatoxin receptors C3aR1, and C5r1. Following exposure to BCL, the expression of components C1s, C2, C3, C4b ... and anaphylatoxin receptors (C3aR1, C5r1). Third, we show a decrease in C3-expressing monocytes/microglia to the ONL following ...
Receptor, Anaphylatoxin C5a. Receptor, Macrophage Colony-Stimulating Factor. Receptors, Chemokine. Receptors, Complement 3b ...
Anaphylatoxin C5a D12.776.543.750.100.24 D12.776.543.750.695.24 Receptor, Angiotensin, Type 1 D12.776.543.750.100.47.625 ...
... release of pro-inflammatory anaphylatoxins (C5a, C3a) that attract white blood cells and finally formation of membrane attack ...
Endothelin1 and Anaphylatoxin C3a. This can only be described as an anti-inflammatory action which restrains the excess ...
Receptor, Anaphylatoxin C5a. *Receptor, ErbB-2. *Receptor, Macrophage Colony-Stimulating Factor. *Receptors, Chemokine ...
C5L2 anaphylatoxin chemotactic receptor binding. GO:0031715. IDA. protein binding. GO:0005515. IPI. ...
Receptor, Anaphylatoxin C5a. Receptor da Anafilatoxina C5a. Receptor de Anafilatoxina C5a. Receptor, Angiotensin, Type 1. ...
Receptor, Anaphylatoxin C5a. Receptor de Anafilatoxina C5a. Receptor de Colecistocinina A. Receptor, Cholecystokinin A. ...
35 - Referees report by William Bate Hardy, on a paper Anaphylaxis and anaphylatoxins by Henry Hallett Dale and Charles ... 36 - Referees report by Charles James Martin, on a paper Anaphylaxis and anaphylatoxins by Henry Hallett Dale and Charles ...
  • Anaphylatoxins, or complement peptides, are fragments (C3a, C4a and C5a) that are produced as part of the activation of the complement system. (wikipedia.org)
  • Micrurus venoms can activate the complement system, generating a significant amount of anaphylatoxins, which may assist due to their vasodilatory effects, to enhance the spreading of other venom components during the envenomation process. (biomedcentral.com)
  • Complement activation may generate anaphylatoxins and membrane attack complex (MAC). (biomedcentral.com)
  • The accumulation of anaphylatoxins (such as C5a) from complement activation might also have a role. (medscape.com)
  • Anaphylatoxins indirectly mediate: smooth muscle cells contraction, for example bronchospasms increase in the permeability of blood capillaries C5a indirectly mediates chemotaxis-receptor-mediated movement of leukocytes in the direction of the increasing concentration of anaphylatoxins Important anaphylatoxins: C5a has the highest specific biological activity and is able to act directly on neutrophils and monocytes to speed up the phagocytosis of pathogens. (wikipedia.org)
  • To check and clarify existing data on receptor‐interacting residues in the human C5a anaphylatoxin, we tested mutant C5a proteins obtained by site‐directed mutagenesis of a recombinant human C5a (rhC5a) cDNA clone for structural and functional integrity. (uni-luebeck.de)
  • Anaphylatoxins (C3a, C4a, and C5a) are considered the bridge between the innate and adaptive immunity, and they are responsible for control the local pro-inflammatory response through vasodilatation and the chemotaxis and activation of leukocytes [ 8 - 11 ]. (biomedcentral.com)
  • The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. (wikipedia.org)
  • Anaphylatoxins are able to trigger degranulation (release of substances) of endothelial cells, mast cells or phagocytes, which produce a local inflammatory response. (wikipedia.org)
  • This leads to initiation of cascade of enzymatic cleavages and formation of crucial enzymatic complexes (C3 and C5 convertases), release of pro-inflammatory anaphylatoxins (C5a, C3a) that attract white blood cells and finally formation of membrane attack complex (MAC, pore in a membrane). (lu.se)
  • Recent studies have indicated that small complement peptide ligands may lack selectivity amongst the three anaphylatoxin receptors, however this has not been uniformly confirmed for these commonly used C5a agonists. (nih.gov)
  • One hypothesis was that patients with such variants lacked the ability to regulate the alternate complement pathway once it had become activated, resulting in the formation of anaphylatoxins, a type of protein that mediates inflammation, among other biological functions. (nih.gov)
  • Work from Dr. Kemper's lab, however, has highlighted an equally profound impact of complement on adaptive immunity through direct regulation of CD4 + T cells: signals mediated by T cell-expressed anaphylatoxin receptor C3aR and the complement regulator CD46 (which binds the complement activation fragment C3b) are critical checkpoints in human T cell lineage commitment and control initiation and resolution of inflammatory Th1 responses. (nih.gov)
  • Other small peptides released during complement activation include anaphylatoxins, which induce local inflammation. (cam.ac.uk)
  • The C3a peptide, also known as the C3a anaphylatoxin, modulates inflammation and possesses antimicrobial activity. (nih.gov)
  • Its activation generates the effector cleavage proteins, anaphylatoxins C3a and C5a, that exert activity by interacting with three structurally related seven-transmembrane receptors. (nih.gov)
  • The overall polypeptide fold is similar to that of the sequence related human recombinant anaphylatoxin C5a [(1988) Proteins 3, 139-145]. (nih.gov)
  • Cleavage of the alpha chain by a convertase enzyme results in the formation of the C5a anaphylatoxin, which possesses potent spasmogenic and chemotactic activity, and the C5b macromolecular cleavage product, a subunit of the membrane attack complex (MAC). (nih.gov)
  • The order of anaphylatoxin activity from the strongest to the weakest is C5a, C3a, C4a, and C5a des-arginine. (nih.gov)
  • The strongest proinflammatory anaphylatoxin C5a is normally suggested to try out a particularly essential role in undesirable clinical results during sepsis (18 19 Although TLRs and supplement are often regarded discrete entities an rising body of proof indicates these essential innate protection systems are interconnected by comprehensive MK-3102 cross-talk (20-23). (mdm2-inhibitors.com)
  • The encoded preproprotein is proteolytically processed to generate multiple protein products, including the C5 alpha chain, C5 beta chain, C5a anaphylatoxin and C5b. (nih.gov)
  • Human C3a and C3a desArg anaphylatoxins have conserved structures, in contrast to C5a and C5a desArg. (nih.gov)
  • 8. The active site of human C4a anaphylatoxin. (nih.gov)
  • To test this hypothesis, the researchers exposed 10 iPSC-derived RPE cell lines involving different genetic variants to anaphylatoxins from human serum. (nih.gov)
  • During this process, C3a (anaphylatoxin) is released which causes smooth muscle contraction and has a potent vascular effect. (immunecare.co.nz)