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.
The presence of free HEMOGLOBIN in the URINE, indicating hemolysis of ERYTHROCYTES within the vascular system. After saturating the hemoglobin-binding proteins (HAPTOGLOBINS), free hemoglobin begins to appear in the urine.
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)
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.
Compounds containing carbohydrate or glycosyl groups linked to phosphatidylinositols. They anchor GPI-LINKED PROTEINS or polysaccharides to cell membranes.
The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.
A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements.
A radiation-protective agent that can inhibit DNA damage by binding to the DNA. It also increases the susceptibility of blood cells to complement-mediated lysis.
Care of a highly technical and specialized nature, provided in a medical center, usually one affiliated with a university, for patients with unusually severe, complex, or uncommon health problems.
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.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
A complication of MALARIA, FALCIPARUM characterized by the passage of dark red to black urine.
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.
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 condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).
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.
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.
Hemosiderin is an iron-containing pigment that originates from the breakdown of hemoglobin and accumulates in tissues, primarily in macrophages, as a result of various pathological conditions such as hemorrhage, inflammation, or certain storage diseases.
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.
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.
Leukocytes with abundant granules in the cytoplasm. They are divided into three groups according to the staining properties of the granules: neutrophilic, eosinophilic, and basophilic. Mature granulocytes are the NEUTROPHILS; EOSINOPHILS; and BASOPHILS.
A clinical manifestation of HYPERBILIRUBINEMIA, characterized by the yellowish staining of the SKIN; MUCOUS MEMBRANE; and SCLERA. Clinical jaundice usually is a sign of LIVER dysfunction.
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.
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.
Deficiency of all three cell elements of the blood, erythrocytes, leukocytes and platelets.
A condition in which the hepatic venous outflow is obstructed anywhere from the small HEPATIC VEINS to the junction of the INFERIOR VENA CAVA and the RIGHT ATRIUM. Usually the blockage is extrahepatic and caused by blood clots (THROMBUS) or fibrous webs. Parenchymal FIBROSIS is uncommon.
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 group of genetically identical cells all descended from a single common ancestral cell by mitosis in eukaryotes or by binary fission in prokaryotes. Clone cells also include populations of recombinant DNA molecules all carrying the same inserted sequence. (From King & Stansfield, Dictionary of Genetics, 4th ed)
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 semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
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.
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 introduction of whole blood or blood component directly into the blood stream. (Dorland, 27th ed)
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.
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.
Progenitor cells from which all blood cells derive.
Antibodies from non-human species whose protein sequences have been modified to make them nearly identical with human antibodies. If the constant region and part of the variable region are replaced, they are called humanized. If only the constant region is modified they are called chimeric. INN names for humanized antibodies end in -zumab.
Separation of one or more kinds of cells from whole blood with the return of other blood cell constituents to the patient or donor. This is accomplished with an instrument that uses centrifugation to separate the cells into different layers based on the differences in cell density (displacement) or drag coefficients in a current (elutriation). The procedure is commonly used in adoptive transfer to isolate NK cells, lymphocytes, or monocytes.
A blood group related both to the ABO and P systems that includes several different antigens found in most people on erythrocytes, in milk, and in saliva. The antibodies react only at low temperatures.
Oxygen-carrying RED BLOOD CELLS in mammalian blood that are abnormal in structure or function.
Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)
Clonal hematopoietic stem cell disorders characterized by dysplasia in one or more hematopoietic cell lineages. They predominantly affect patients over 60, are considered preleukemic conditions, and have high probability of transformation into ACUTE MYELOID LEUKEMIA.
Bone marrow diseases, also known as hematologic or blood disorders, refer to conditions that affect the production and function of blood cells within the bone marrow, such as leukemia, lymphoma, myeloma, and aplastic anemia, potentially leading to complications like anemia, neutropenia, thrombocytopenia, and increased susceptibility to infections or bleeding.
A phosphorus-oxygen lyase found primarily in BACTERIA. The enzyme catalyzes the cleavage of a phosphoester linkage in 1-phosphatidyl-1D-myo-inositol to form 1D-myo-inositol 1,2-cyclic phosphate and diacylglycerol. The enzyme was formerly classified as a phosphoric diester hydrolase (EC 3.1.4.10) and is often referred to as a TYPE C PHOSPHOLIPASES. However it is now known that a cyclic phosphate is the final product of this enzyme and that water does not enter into the reaction.
Glycoproteins found on the membrane or surface of cells.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.
Antibodies produced by a single clone of cells.
The senescence of RED BLOOD CELLS. Lacking the organelles that make protein synthesis possible, the mature erythrocyte is incapable of self-repair, reproduction, and carrying out certain functions performed by other cells. This limits the average life span of an erythrocyte to 120 days.
Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
The co-occurrence of pregnancy and a blood disease (HEMATOLOGIC DISEASES) which involves BLOOD CELLS or COAGULATION FACTORS. The hematologic disease may precede or follow FERTILIZATION and it may or may not have a deleterious effect on the pregnant woman or FETUS.
Serum containing GAMMA-GLOBULINS which are antibodies for lymphocyte ANTIGENS. It is used both as a test for HISTOCOMPATIBILITY and therapeutically in TRANSPLANTATION.
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.
The development and formation of various types of BLOOD CELLS. Hematopoiesis can take place in the BONE MARROW (medullary) or outside the bone marrow (HEMATOPOIESIS, EXTRAMEDULLARY).
Glycoproteins with a wide distribution on hematopoietic and non-hematopoietic cells and strongly expressed on macrophages. CD58 mediates cell adhesion by binding to CD2; (ANTIGENS, CD2); and this enhances antigen-specific T-cell activation.
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.
The cells found in the body fluid circulating throughout the CARDIOVASCULAR SYSTEM.
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.
Formation and development of a thrombus or blood clot in the blood vessel.
A type of mutation in which a number of NUCLEOTIDES deleted from or inserted into a protein coding sequence is not divisible by three, thereby causing an alteration in the READING FRAMES of the entire coding sequence downstream of the mutation. These mutations may be induced by certain types of MUTAGENS or may occur spontaneously.
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.
White blood cells. These include granular leukocytes (BASOPHILS; EOSINOPHILS; and NEUTROPHILS) as well as non-granular leukocytes (LYMPHOCYTES and MONOCYTES).
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.
A disorder of HEMOSTASIS in which there is a tendency for the occurrence of THROMBOSIS.

Resistance of paroxysmal nocturnal hemoglobinuria cells to the glycosylphosphatidylinositol-binding toxin aerolysin. (1/413)

Paroxysmal nocturnal hemoglobinuria (PNH) is a clonal stem cell disorder caused by a somatic mutation of the PIGA gene. The product of this gene is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; therefore, the phenotypic hallmark of PNH cells is an absence or marked deficiency of all GPI-anchored proteins. Aerolysin is a toxin secreted by the bacterial pathogen Aeromonas hydrophila and is capable of killing target cells by forming channels in their membranes after binding to GPI-anchored receptors. We found that PNH blood cells (erythrocytes, lymphocytes, and granulocytes), but not blood cells from normals or other hematologic disorders, are resistant to the cytotoxic effects of aerolysin. The percentage of lysis of PNH cells after aerolysin exposure paralleled the percentage of CD59(+) cells in the samples measured by flow cytometry. The kinetics of red blood cell lysis correlated with the type of PNH erythrocytes. PNH type III cells were completely resistant to aerolysin, whereas PNH type II cells displayed intermediate sensitivity. Importantly, the use of aerolysin allowed us to detect PNH populations that could not be detected by standard flow cytometry. Resistance of PNH cells to aerolysin allows for a simple, inexpensive assay for PNH that is sensitive and specific. Aerolysin should also be useful in studying PNH biology.  (+info)

Clonal populations of hematopoietic cells with paroxysmal nocturnal hemoglobinuria genotype and phenotype are present in normal individuals. (2/413)

In paroxysmal nocturnal hemoglobinuria (PNH), acquired somatic mutations in the PIG-A gene give rise to clonal populations of red blood cells unable to express proteins linked to the membrane by a glycosylphosphatidylinositol anchor. These proteins include the complement inhibitors CD55 and CD59, and this explains the hypersensitivity to complement of red cells in PNH patients, manifested by intravascular hemolysis. The factors that determine to what extent mutant clones expand have not yet been pinpointed; it has been suggested that existing PNH clones may have a conditional growth advantage depending on some factor (e.g., autoimmune) present in the marrow environment of PNH patients. Using flow cytometric analysis of granulocytes, we now have identified cells that have the PNH phenotype, at an average frequency of 22 per million (range 10-51 per million) in nine normal individuals. These rare cells were collected by flow sorting, and exons 2 and 6 of the PIG-A gene were amplified by nested PCR. We found PIG-A mutations in six cases: four missense, one frameshift, and one nonsense mutation. PNH red blood cells also were identified at a frequency of eight per million. Thus, small clones with PIG-A mutations exist commonly in normal individuals, showing clearly that PIG-A gene mutations are not sufficient for the development of PNH. Because PIG-A encodes an enzyme essential for the expression of a host of surface proteins, the PIG-A gene provides a highly sensitive system for the study of somatic mutations in hematopoietic cells.  (+info)

Elevated levels of circulating procoagulant microparticles in patients with paroxysmal nocturnal hemoglobinuria and aplastic anemia. (3/413)

Paroxysmal nocturnal hemoglobinuria (PNH), frequently occurring during suppressed hematopoiesis including aplastic anemia (AA), is a clonal disorder associated with an increased incidence of thrombotic events. Complement-mediated hemolysis, impairment of the fibrinolytic system, or platelet activation are thought to be responsible for the associated thrombotic risk. We investigated here the elevation of membrane-derived procoagulant microparticles in the blood flow of such patients. Elevated levels of circulating microparticles were in fact detected in both de novo PNH patients and AA subjects with a PNH clone, but not in those with AA without a PNH clone. The cellular origin of the microparticles was determined in PNH samples; most stemmed from platelets. Glycophorin A+ particles were rarely detected. Therefore, platelet activation, resulting in the dissemination of procoagulant phospholipids in the blood flow, could be one of the main causes for the elevated thrombotic risk associated with PNH. These observations suggest that shed membrane particles can be considered a valuable biological parameter for the assessment of possible thrombotic complications in patients with PNH.  (+info)

X inactivation and somatic cell selection rescue female mice carrying a Piga-null mutation. (4/413)

A somatic mutation in the X linked PIGA gene is responsible for the deficiency of glycosyl phosphatidylinositol (GPI)-anchored proteins on blood cells from patients with paroxysmal nocturnal hemoglobinuria. No inherited form of GPI-anchor deficiency has been described. Because conventional Piga gene knockout is associated with high embryonic lethality in chimeric mice, we used the Cre/loxP system. We generated mice in which two loxP sites flank part of Piga exon 2. After crossbreeding with female mice of the EIIa-cre strain, the floxed allele undergoes Cre-mediated recombination with high efficiency during early embryonic development. Because of X chromosome inactivation, female offspring are mosaic for cells that express or lack GPI-linked proteins. Analysis of mosaic mice showed that in heart, lung, kidney, brain, and liver, mainly wild-type Piga is active, suggesting that these tissues require GPI-linked proteins. The salient exceptions were spleen, thymus, and red blood cells, which had almost equal numbers of cells expressing the wild-type or the recombined allele, implying that GPI-linked proteins are not essential for the derivation of these tissues. PIGA(-) cells had no growth advantage, suggesting that other factors are needed for their clonal dominance in patients with paroxysmal nocturnal hemoglobinuria.  (+info)

Defective TCR signaling events in glycosylphosphatidylinositol-deficient T cells derived from paroxysmal nocturnal hemoglobinuria patients. (5/413)

Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired hemolytic disorder characterized by the presence of abnormal cells of various hematopoietic cell lineages deficient in surface expression of glycosylphosphatidylinositol (GPI)-anchored molecules. By analyzing T cells isolated from patients affected with PNH, it was found that ex vivo GPI-deficient CD4(+) and CD8(+) peripheral T cells display a more naive phenotype as compared to wild-type cells. In addition, in vitro proliferative responses to allogeneic antigen-presenting cells were shown to be reduced in mutant T cells. To investigate the molecular basis responsible for defective T cell activation in GPI-deficient T cells, T cell lines and T cell clones were generated from patients affected with PNH. When stimulated with anti-CD3epsilon mAb, mutant cells displayed a significantly decreased activation of protein tyrosine kinase p56(lck). The decreased kinase activity was accompanied by a delayed TCR capping and internalization. Interestingly, protein tyrosine phosphorylation is not only quantitatively but also qualitatively affected, with one substrate being more intensively phosphorylated in mutant than in wild-type cells. These observations suggest that a defective activation of p56(lck) contributes to the depressed immune responses observed in GPI-deficient T cells derived from PNH patients.  (+info)

Analysis of T cells in paroxysmal nocturnal hemoglobinuria provides direct evidence that thymic T-cell production declines with age. (6/413)

Peripheral blood T cells in patients with paroxysmal nocturnal hemoglobinuria (PNH) comprise a mixture of residual normal and glycosylphosphatidylinositol (GPI)-deficient PNH cells. Using multicolor flow cytometry, we demonstrated significant differences between the proportions of naive and memory cells within these populations. PNH T cells comprise mainly naive cells (CD45RA(+)CD45R0(-)), whereas normal T cells in the same patients were predominantly memory (CD45RA(-)CD45R0(+)) cells. Functional analyses showed that GPI-deficient CD45RA(+) T cells can convert to a CD45R0(+) phenotype. We present data from a PNH patient in remission for 20 years who still had significant numbers of GPI-deficient T cells; these showed a normal distribution of naive and memory components. The predominantly naive phenotype of GPI-deficient T cells seen in PNH patients with active disease likely reflects the phenotype of recent normal thymic emigrants. In patients where hematopoiesis was predominantly derived from the PNH stem cell, absolute numbers of both naive PNH CD4(+) cells and CD8(+) cells show an inverse correlation with patient age, implying this age-related decline in T-cell production is secondary to a decrease in thymic activity rather than a stem cell defect.  (+info)

Increased sensitivity to complement and a decreased red blood cell life span in mice mosaic for a nonfunctional Piga gene. (7/413)

The gene PIGA encodes one of the protein subunits of the alpha1-6-N acetylglucosaminyltransferase complex, which catalyses an early step in the biosynthesis of glycosyl phosphatidylinositol (GPI) anchors. PIGA is somatically mutated in blood cells from patients with paroxysmal nocturnal hemoglobinuria (PNH), leading to deficiency of GPI-linked proteins on the cell surface. To investigate in detail how inactivating mutations of the PIGA gene affect hematopoiesis, we generated a mouse line, in which loxP-mediated excision of part of exon 2 occurs on the expression of Cre. After crossbreeding with EIIa-cre transgenic mice, recombination occurs early in embryonic life. Mice that are mosaics for the recombined Piga gene are viable and lack GPI-linked proteins on a proportion of circulating blood cells. This resembles the coexistence of normal cells and PNH cells in patients with an established PNH clone. PIGA(-) blood cells in mosaic mice have biologic features characteristic of those classically seen in patients with PNH, including an increased sensitivity toward complement mediated lysis and a decreased life span in circulation. However, during the 12-month follow-up, the PIGA(-) cell population did not increase, clearly showing that a Piga gene mutation is not sufficient to cause the human disease, PNH.  (+info)

Different roles of glycosylphosphatidylinositol in various hematopoietic cells as revealed by a mouse model of paroxysmal nocturnal hemoglobinuria. (8/413)

Patients with paroxysmal nocturnal hemoglobinuria (PNH) have one or a few clones of mutant hematopoietic stem cells defective in glycosylphosphatidylinositol (GPI) synthesis as a result of somatic mutation in the X-linked gene PIG-A. The mutant stem cell clone dominates hematopoiesis by a mechanism that is unclear. To test whether a lack of multiple GPI-anchored proteins results in dysregulation and expansion of stem cells, we generated mice in which GPI-anchor negative cells are present only in the hematopoietic system. We transplanted lethally irradiated mice with female fetal liver cells bearing one allele of the Piga gene disrupted by conditional gene targeting. Because of the X-chromosome inactivation, a significant fraction of the hematopoietic stem cells in fetal livers was GPI-anchor negative. In the transplanted mice, cells of all hematopoietic lineages contained GPI-anchor negative cells. The percentage of GPI-anchor negative cells was much higher in T lymphocytes including immature thymocytes than in other cell types, suggesting a regulatory role for GPI-anchored proteins at an early stage of T-lymphocyte development. However, the proportions of GPI-anchor negative cells in various blood cell lineages were stable over a period of 42 weeks, indicating that Piga mutation alone does not account for the dominance of the mutant stem cells and that other phenotypic changes are involved in pathogenesis of PNH.  (+info)

Paroxysmal nocturnal hemoglobinuria (PNH) is a rare, acquired disorder of the blood characterized by the destruction of red blood cells (hemolysis), which can cause symptoms such as fatigue, dark colored urine (especially in the morning), chest pain, shortness of breath, and an increased risk of blood clots. The hemoglobin from the lysed red blood cells appears in the urine, hence the term "hemoglobinuria."

The paroxysmal nature of the disorder refers to the sudden and recurring episodes of hemolysis that can occur at any time, although they may be more frequent at night. The condition is caused by mutations in a gene called PIG-A, which leads to the production of defective red blood cell membranes that are sensitive to destruction by complement, a component of the immune system.

PNH is a serious and potentially life-threatening condition that can lead to complications such as kidney damage, pulmonary hypertension, and thrombosis. Treatment typically involves supportive care, such as blood transfusions, and medications to manage symptoms and prevent complications. In some cases, stem cell transplantation may be considered as a curative treatment option.

Hemoglobinuria 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. Normally, when red blood cells die, they are broken down and their hemoglobin is recycled. However, in certain conditions such as intravascular hemolysis (the destruction of red blood cells inside blood vessels), hemoglobin can be released into the bloodstream and then filtered by the kidneys into the urine.

Hemoglobinuria can be a symptom of various underlying medical conditions, including hemolytic anemias, disseminated intravascular coagulation (DIC), severe infections, snake bites, and exposure to certain toxins or medications. It is important to identify the underlying cause of hemoglobinuria, as treatment will depend on the specific condition.

In some cases, hemoglobinuria can lead to kidney damage due to the toxic effects of free hemoglobin on the renal tubules. This can result in acute or chronic kidney injury, and in severe cases, it may require dialysis or transplantation.

CD59 is a type of protein found on the surface of many cells in the human body, including red and white blood cells, that functions as an inhibitor of the complement system. The complement system is a part of the immune system that helps to eliminate pathogens such as bacteria and viruses from the body.

CD59 specifically inhibits the formation of the membrane attack complex (MAC), which is a protein structure that forms pores in the cell membrane and can lead to cell lysis or death. By preventing the formation of the MAC, CD59 helps to protect cells from complement-mediated damage.

As an antigen, CD59 is a molecule that can be recognized by the immune system and stimulate an immune response. However, because it is a self-protein found on normal human cells, CD59 is not typically targeted by the immune system unless there is some kind of dysregulation or abnormality.

In certain medical conditions, such as autoimmune disorders or transplant rejection, the immune system may mistakenly target CD59 or other self-proteins, leading to damage to healthy cells and tissues. In these cases, treatments may be necessary to modulate or suppress the immune response and prevent further harm.

CD55, also known as Decay-accelerating factor (DAF), is a protein that acts as an inhibitor of the complement system, which is a part of the immune system. It prevents the formation of the membrane attack complex (MAC) on host cells and tissues, thereby protecting them from damage caused by the complement activation. CD55 is found on the surface of many types of cells in the body, including red blood cells, white blood cells, and cells lining the blood vessels.

As an antigen, CD55 is a molecule that can be recognized by the immune system and stimulate an immune response. However, unlike some other antigens, CD55 does not typically elicit a strong immune response because it is a self-antigen, meaning it is normally present in the body and should not be targeted by the immune system.

In certain medical conditions, such as autoimmune disorders or transplant rejection, the immune system may mistakenly attack cells expressing CD55. In these cases, measuring the levels of CD55 antigens can provide valuable diagnostic information and help guide treatment decisions.

Glycosylphosphatidylinositols (GPIs) are complex glycolipids that are attached to the outer leaflet of the cell membrane. They play a role in anchoring proteins to the cell surface by serving as a post-translational modification site for certain proteins, known as GPI-anchored proteins.

The structure of GPIs consists of a core glycan backbone made up of three mannose and one glucosamine residue, which is linked to a phosphatidylinositol (PI) anchor via a glycosylphosphatidylinositol anchor addition site. The PI anchor is composed of a diacylglycerol moiety and a phosphatidylinositol headgroup.

GPIs are involved in various cellular processes, including signal transduction, protein targeting, and cell adhesion. They have also been implicated in several diseases, such as cancer and neurodegenerative disorders.

Hemolysis is the destruction or breakdown of red blood cells, resulting in the release of hemoglobin into the surrounding fluid (plasma). This process can occur due to various reasons such as chemical agents, infections, autoimmune disorders, mechanical trauma, or genetic abnormalities. Hemolysis may lead to anemia and jaundice, among other complications. It is essential to monitor hemolysis levels in patients undergoing medical treatments that might cause this condition.

Aplastic anemia is a medical condition characterized by pancytopenia (a decrease in all three types of blood cells: red blood cells, white blood cells, and platelets) due to the failure of bone marrow to produce new cells. It is called "aplastic" because the bone marrow becomes hypocellular or "aplastic," meaning it contains few or no blood-forming stem cells.

The condition can be acquired or inherited, with acquired aplastic anemia being more common. Acquired aplastic anemia can result from exposure to toxic chemicals, radiation, drugs, viral infections, or autoimmune disorders. Inherited forms of the disease include Fanconi anemia and dyskeratosis congenita.

Symptoms of aplastic anemia may include fatigue, weakness, shortness of breath, pale skin, easy bruising or bleeding, frequent infections, and fever. Treatment options for aplastic anemia depend on the severity of the condition and its underlying cause. They may include blood transfusions, immunosuppressive therapy, and stem cell transplantation.

Beta-Aminoethyl Isothiourea is not a medical term, but a chemical compound. Its systematic name is (betaine) N-(β-aminoethyl)-isothiouronium bromide. It is used in research and pharmaceutical industry as a tool for studying various biochemical processes, particularly related to enzyme inhibition.

It acts as a potent and irreversible inhibitor of several enzymes such as carboxylesterases, cholinesterases, and proteases. It is not used in clinical medicine or approved for human use.

Tertiary healthcare is a level of health services delivery that involves highly specialized care, often provided by tertiary care hospitals or centers. These facilities typically have advanced diagnostic and treatment capabilities, including access to specialized medical professionals such as surgeons, oncologists, neurologists, and other specialists who provide complex medical and surgical interventions.

Tertiary healthcare services are designed to address the needs of patients with more severe or complicated medical conditions that cannot be managed at primary or secondary care levels. These services often involve highly specialized procedures, such as organ transplants, cancer treatments, advanced neurosurgical procedures, and other complex interventions. Tertiary care facilities may also serve as referral centers for smaller hospitals and clinics, providing consultation, diagnosis, and treatment recommendations for patients with rare or difficult-to-diagnose conditions.

It's important to note that tertiary healthcare is not always accessible to everyone due to factors such as cost, location, and availability of specialized services. Access to tertiary care can vary widely depending on the healthcare system and resources available in a given region or country.

Complement inactivator proteins are a group of regulatory proteins that help to control and limit the activation of the complement system, which is a part of the immune system. The complement system is a complex series of biochemical reactions that help to eliminate pathogens and damaged cells from the body. However, if not properly regulated, the complement system can also cause damage to healthy tissues and contribute to the development of various diseases.

Complement inactivator proteins work by inhibiting specific components of the complement system, preventing them from activating and causing an immune response. Some examples of complement inactivator proteins include:

1. C1 inhibitor (C1INH): This protein regulates the activation of the classical pathway of the complement system by inhibiting the C1 complex, which is a group of proteins that initiate this pathway.
2. Decay-accelerating factor (DAF or CD55): This protein regulates the activation of both the classical and alternative pathways of the complement system by accelerating the decay of the C3/C5 convertases, which are enzymes that activate the complement components C3 and C5.
3. Membrane cofactor protein (MCP or CD46): This protein regulates the activation of the alternative pathway of the complement system by serving as a cofactor for the cleavage and inactivation of C3b, a component of the C3 convertase.
4. Factor H: This protein also regulates the activation of the alternative pathway of the complement system by acting as a cofactor for the cleavage and inactivation of C3b, and by preventing the formation of the C3 convertase.

Deficiencies or dysfunction of complement inactivator proteins can lead to various diseases, including hereditary angioedema (C1INH deficiency), atypical hemolytic uremic syndrome (factor H deficiency or dysfunction), and age-related macular degeneration (complement component overactivation).

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Blackwater fever is a severe and potentially life-threatening complication of malaria, typically caused by the Plasmodium falciparum parasite. The term "blackwater" refers to the dark colored urine that can occur in this condition due to the presence of hemoglobin, which is released into the bloodstream when red blood cells are destroyed (hemolysis) in large numbers.

In blackwater fever, the malarial parasites infect and multiply within red blood cells, causing them to become fragile and rupture. This leads to the release of hemoglobin into the bloodstream, which is then filtered by the kidneys and excreted in the urine. The excessive breakdown of red blood cells can also cause anemia, jaundice, and kidney failure.

Symptoms of blackwater fever may include high fever, chills, severe muscle and joint pain, nausea and vomiting, dark colored urine, and signs of kidney failure such as decreased urine output and swelling in the legs and feet. Treatment typically involves the use of antimalarial medications to eliminate the parasites from the bloodstream, as well as supportive care to manage symptoms and prevent complications. In severe cases, hospitalization may be necessary for close monitoring and treatment of complications such as kidney failure or respiratory distress.

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.

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.

Hemolytic anemia is a type of anemia that occurs when red blood cells are destroyed (hemolysis) faster than they can be produced. Red blood cells are essential for carrying oxygen throughout the body. When they are destroyed, hemoglobin and other cellular components are released into the bloodstream, which can lead to complications such as kidney damage and gallstones.

Hemolytic anemia can be inherited or acquired. Inherited forms of the condition may result from genetic defects that affect the structure or function of red blood cells. Acquired forms of hemolytic anemia can be caused by various factors, including infections, medications, autoimmune disorders, and certain medical conditions such as cancer or blood disorders.

Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, pale skin, jaundice (yellowing of the skin and eyes), dark urine, and a rapid heartbeat. Treatment for hemolytic anemia depends on the underlying cause and may include medications, blood transfusions, or surgery.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Complement C8 is a protein component of the complement system, which is a part of the immune system that helps to eliminate pathogens and damaged cells from the body. Specifically, C8 is a part of the membrane attack complex (MAC), which forms a pore in the membrane of target cells, leading to their lysis or destruction.

C8 is composed of three subunits: alpha, beta, and gamma. It is activated when it binds to the complement component C5b67 complex on the surface of a target cell. Once activated, C8 undergoes a conformational change that allows it to insert into the target cell membrane and form a pore, which disrupts the cell's membrane integrity and can lead to its death.

Deficiencies in complement components, including C8, can make individuals more susceptible to certain infections and autoimmune diseases. Additionally, mutations in the genes encoding complement proteins have been associated with various inherited disorders, such as atypical hemolytic uremic syndrome (aHUS), which is characterized by thrombotic microangiopathy and kidney failure.

Hemosiderin is a golden-brown pigment that consists of iron-containing protein complexes called ferritin and ferrikinase. It is insoluble in water and forms as a result of the breakdown of hemoglobin in the reticuloendothelial system, primarily in macrophages. Hemosiderin deposits can be found in various tissues and organs, such as the spleen, liver, and brain, under conditions of increased red blood cell destruction or impaired iron metabolism. These deposits are often associated with diseases such as hemochromatosis, thalassemia, and chronic inflammation.

Complement C9 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. Specifically, C9 is one of the components of the membrane attack complex (MAC), which is a protein structure that forms pores in the membranes of target cells, leading to their lysis or destruction.

When activated, C9 polymerizes and inserts itself into the cell membrane, forming a transmembrane pore that disrupts the membrane's integrity and causes the cell to lyse. This process is an essential part of the complement system's ability to destroy pathogens and clear damaged cells from the body.

Defects in the C9 gene can lead to a rare genetic disorder called complement component 9 deficiency, which is characterized by recurrent bacterial infections and immune complex-mediated diseases. Additionally, mutations in the C9 gene have been associated with an increased risk of age-related macular degeneration (AMD), a leading cause of blindness in older adults.

Complement C3-C5 convertases are proteins that play a crucial role in 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.

The C3-C5 convertases are formed during the activation of the complement component 3 (C3) protein, which is a central player in the complement system. The formation of the C3-C5 convertase involves two main steps:

1. C3 convertase formation: In this step, a complex of proteins called the C3 convertase is formed by the cleavage of C3 into C3a and C3b fragments. This complex can then cleave additional C3 molecules into C3a and C3b fragments, amplifying the complement response.
2. C5 convertase formation: In this step, the C3b fragment from the C3 convertase binds to another protein called C4b2a, forming a new complex called the C5 convertase. The C5 convertase can then cleave the C5 protein into C5a and C5b fragments.

The C5b fragment goes on to form the membrane attack complex (MAC), which creates a pore in the membrane of the target cell, leading to its lysis or destruction. The C3a and C5a fragments are small proteins called anaphylatoxins that can cause inflammation and attract immune cells to the site of infection or injury.

Overall, the formation of Complement C3-C5 convertases is a critical step in the activation of the complement system and plays a key role in the body's defense against pathogens and damaged cells.

Granulocytes are a type of white blood cell that plays a crucial role in the body's immune system. They are called granulocytes because they contain small granules in their cytoplasm, which are filled with various enzymes and proteins that help them fight off infections and destroy foreign substances.

There are three types of granulocytes: neutrophils, eosinophils, and basophils. Neutrophils are the most abundant type and are primarily responsible for fighting bacterial infections. Eosinophils play a role in defending against parasitic infections and regulating immune responses. Basophils are involved in inflammatory reactions and allergic responses.

Granulocytes are produced in the bone marrow and released into the bloodstream, where they circulate and patrol for any signs of infection or foreign substances. When they encounter a threat, they quickly move to the site of infection or injury and release their granules to destroy the invading organisms or substances.

Abnormal levels of granulocytes in the blood can indicate an underlying medical condition, such as an infection, inflammation, or a bone marrow disorder.

Jaundice is a medical condition characterized by the yellowing of the skin, sclera (whites of the eyes), and mucous membranes due to an excess of bilirubin in the bloodstream. Bilirubin is a yellow-orange pigment produced when hemoglobin from red blood cells is broken down. Normally, bilirubin is processed by the liver and excreted through bile into the digestive system. However, if there's an issue with bilirubin metabolism or elimination, it can accumulate in the body, leading to jaundice.

Jaundice can be a symptom of various underlying conditions, such as liver diseases (hepatitis, cirrhosis), gallbladder issues (gallstones, tumors), or blood disorders (hemolysis). It is essential to consult a healthcare professional if jaundice is observed, as it may indicate a severe health problem requiring prompt medical attention.

Complement C7 is a protein that plays a role in the complement system, which is a part of the immune system that helps to clear pathogens and damaged cells from the body. Specifically, C7 is a component of the membrane attack complex (MAC), which is a group of proteins that forms a pore in the membrane of target cells, leading to their lysis or destruction.

C7 is activated when it binds to the C5b-7 complex, which is formed by the cleavage of C5 and C6 by the C5 convertase. Once bound to the C5b-7 complex, C7 undergoes a conformational change that allows it to insert into the target cell membrane. This forms the basis for the formation of the MAC and subsequent lysis of the target cell.

Deficiencies in complement components, including C7, can lead to increased susceptibility to certain infections and autoimmune disorders. Additionally, abnormal regulation of the complement system has been implicated in a variety of diseases, including inflammatory and degenerative conditions.

Glucose-6-Phosphate Dehydrogenase (G6PD) deficiency is a genetic disorder that affects the normal functioning of an enzyme called G6PD. This enzyme is found in red blood cells and plays a crucial role in protecting them from damage.

In people with G6PD deficiency, the enzyme's activity is reduced or absent, making their red blood cells more susceptible to damage and destruction, particularly when they are exposed to certain triggers such as certain medications, infections, or foods. This can lead to a condition called hemolysis, where the red blood cells break down prematurely, leading to anemia, jaundice, and in severe cases, kidney failure.

G6PD deficiency is typically inherited from one's parents in an X-linked recessive pattern, meaning that males are more likely to be affected than females. While there is no cure for G6PD deficiency, avoiding triggers and managing symptoms can help prevent complications.

Pancytopenia is a medical condition characterized by a reduction in the number of all three types of blood cells in the peripheral blood: red blood cells (anemia), white blood cells (leukopenia), and platelets (thrombocytopenia). This condition can be caused by various underlying diseases, including bone marrow disorders, viral infections, exposure to toxic substances or radiation, vitamin deficiencies, and certain medications. Symptoms of pancytopenia may include fatigue, weakness, increased susceptibility to infections, and easy bruising or bleeding.

Budd-Chiari syndrome is a rare condition characterized by the obstruction of the hepatic veins, which are the blood vessels that carry blood from the liver to the heart. This obstruction can be caused by blood clots, tumors, or other abnormalities, and it can lead to a backflow of blood in the liver, resulting in various symptoms such as abdominal pain, swelling, and liver enlargement. In severe cases, Budd-Chiari syndrome can cause liver failure and other complications if left untreated. The diagnosis of this condition typically involves imaging tests such as ultrasound, CT scan, or MRI, and treatment may include anticoagulation therapy, thrombolytic therapy, or surgical intervention to remove the obstruction.

The Complement Membrane Attack Complex (MAC), also known as the Terminal Complement Complex (TCC), is a protein structure that forms in the final stages of the complement system's immune response. The complement system is a part of the innate immune system that helps to eliminate pathogens and damaged cells from the body.

The MAC is composed of several proteins, including C5b, C6, C7, C8, and multiple subunits of C9, which assemble on the surface of target cells. The formation of the MAC creates a pore-like structure in the cell membrane, leading to disruption of the membrane's integrity and ultimately causing cell lysis or damage.

The MAC plays an important role in the immune response by helping to eliminate pathogens that have evaded other immune defenses. However, uncontrolled activation of the complement system and formation of the MAC can also contribute to tissue damage and inflammation in various diseases, such as autoimmune disorders, age-related macular degeneration, and ischemia-reperfusion injury.

A clone is a group of cells that are genetically identical to each other because they are derived from a common ancestor cell through processes such as mitosis or asexual reproduction. Therefore, the term "clone cells" refers to a population of cells that are genetic copies of a single parent cell.

In the context of laboratory research, cells can be cloned by isolating a single cell and allowing it to divide in culture, creating a population of genetically identical cells. This is useful for studying the behavior and characteristics of individual cell types, as well as for generating large quantities of cells for use in experiments.

It's important to note that while clone cells are genetically identical, they may still exhibit differences in their phenotype (physical traits) due to epigenetic factors or environmental influences.

Flow cytometry is a medical and research technique used to measure physical and chemical characteristics of cells or particles, one cell at a time, as they flow in a fluid stream through a beam of light. The properties measured include:

* Cell size (light scatter)
* Cell internal complexity (granularity, also light scatter)
* Presence or absence of specific proteins or other molecules on the cell surface or inside the cell (using fluorescent antibodies or other fluorescent probes)

The technique is widely used in cell counting, cell sorting, protein engineering, biomarker discovery and monitoring disease progression, particularly in hematology, immunology, and cancer research.

An erythrocyte, also known as a red blood cell, is a type of cell that circulates in the blood and is responsible for transporting oxygen throughout the body. The erythrocyte membrane refers to the thin, flexible barrier that surrounds the erythrocyte and helps to maintain its shape and stability.

The erythrocyte membrane is composed of a lipid bilayer, which contains various proteins and carbohydrates. These components help to regulate the movement of molecules into and out of the erythrocyte, as well as provide structural support and protection for the cell.

The main lipids found in the erythrocyte membrane are phospholipids and cholesterol, which are arranged in a bilayer structure with the hydrophilic (water-loving) heads facing outward and the hydrophobic (water-fearing) tails facing inward. This arrangement helps to maintain the integrity of the membrane and prevent the leakage of cellular components.

The proteins found in the erythrocyte membrane include integral proteins, which span the entire width of the membrane, and peripheral proteins, which are attached to the inner or outer surface of the membrane. These proteins play a variety of roles, such as transporting molecules across the membrane, maintaining the shape of the erythrocyte, and interacting with other cells and proteins in the body.

The carbohydrates found in the erythrocyte membrane are attached to the outer surface of the membrane and help to identify the cell as part of the body's own immune system. They also play a role in cell-cell recognition and adhesion.

Overall, the erythrocyte membrane is a complex and dynamic structure that plays a critical role in maintaining the function and integrity of red blood cells.

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.

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.

A blood transfusion is a medical procedure in which blood or its components are transferred from one individual (donor) to another (recipient) through a vein. The donated blood can be fresh whole blood, packed red blood cells, platelets, plasma, or cryoprecipitate, depending on the recipient's needs. Blood transfusions are performed to replace lost blood due to severe bleeding, treat anemia, support patients undergoing major surgeries, or manage various medical conditions such as hemophilia, thalassemia, and leukemia. The donated blood must be carefully cross-matched with the recipient's blood type to minimize the risk of transfusion reactions.

CD (cluster of differentiation) antigens are cell-surface proteins that are expressed on leukocytes (white blood cells) and can be used to identify and distinguish different subsets of these cells. They are important markers in the field of immunology and hematology, and are commonly used to diagnose and monitor various diseases, including cancer, autoimmune disorders, and infectious diseases.

CD antigens are designated by numbers, such as CD4, CD8, CD19, etc., which refer to specific proteins found on the surface of different types of leukocytes. For example, CD4 is a protein found on the surface of helper T cells, while CD8 is found on cytotoxic T cells.

CD antigens can be used as targets for immunotherapy, such as monoclonal antibody therapy, in which antibodies are designed to bind to specific CD antigens and trigger an immune response against cancer cells or infected cells. They can also be used as markers to monitor the effectiveness of treatments and to detect minimal residual disease (MRD) after treatment.

It's important to note that not all CD antigens are exclusive to leukocytes, some can be found on other cell types as well, and their expression can vary depending on the activation state or differentiation stage of the cells.

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.

Hematopoietic stem cells (HSCs) are immature, self-renewing cells that give rise to all the mature blood and immune cells in the body. They are capable of both producing more hematopoietic stem cells (self-renewal) and differentiating into early progenitor cells that eventually develop into red blood cells, white blood cells, and platelets. HSCs are found in the bone marrow, umbilical cord blood, and peripheral blood. They have the ability to repair damaged tissues and offer significant therapeutic potential for treating various diseases, including hematological disorders, genetic diseases, and cancer.

Monoclonal antibodies are laboratory-produced proteins that mimic the immune system's ability to fight off harmful antigens such as viruses and cancer cells. They are created by fusing a single B cell (the type of white blood cell responsible for producing antibodies) with a tumor cell, resulting in a hybrid cell called a hybridoma. This hybridoma can then be cloned to produce a large number of identical cells, all producing the same antibody, hence "monoclonal."

Humanized monoclonal antibodies are a type of monoclonal antibody that have been genetically engineered to include human components. This is done to reduce the risk of an adverse immune response in patients receiving the treatment. In this process, the variable region of the mouse monoclonal antibody, which contains the antigen-binding site, is grafted onto a human constant region. The resulting humanized monoclonal antibody retains the ability to bind to the target antigen while minimizing the immunogenicity associated with murine (mouse) antibodies.

In summary, "antibodies, monoclonal, humanized" refers to a type of laboratory-produced protein that mimics the immune system's ability to fight off harmful antigens, but with reduced immunogenicity due to the inclusion of human components in their structure.

Cytapheresis is a medical procedure that involves the separation and removal of specific types of blood cells or particles from a donor or patient's blood, while returning the remaining components back to the circulation. The term "cytapheresis" comes from the Greek words "kytos," meaning cell, and "apherein," meaning to transfer or remove.

There are several types of cytapheresis, including:

1. Erythrocytapheresis (Red Cell Exchange): This procedure is used to reduce the number of red blood cells in patients with severe sickle cell disease or other hemoglobinopathies during a vaso-occlusive crisis or to prevent stroke in children with sickle cell disease.
2. Leukapheresis: It is used to collect large numbers of white blood cells (leukocytes) from donors for the production of immunotherapeutic agents, such as monoclonal antibodies and dendritic cell vaccines. Additionally, it can be employed to reduce the number of white blood cells in patients with leukemia or other hematological disorders.
3. Plateletapheresis: This procedure is used to collect platelets from donors for transfusion purposes or to reduce the number of platelets in patients with thrombocytopenia or thrombocytosis.
4. Lymphapheresis: It is used to collect lymphocytes, mainly T- and B-cells, from donors for immunotherapy or to deplete malignant lymphocytes in patients with certain types of cancer, such as Hodgkin's lymphoma.
5. Lipoproteinapheresis: This procedure is used to lower the levels of low-density lipoproteins (LDL) and lipids in patients with familial hypercholesterolemia or other severe forms of dyslipidemia.

Cytapheresis can be performed using a centrifugation method, where blood is spun in a special machine to separate the components based on their density, or a filtration method, where blood passes through a filter that captures the target cells or particles. The procedure typically takes 1-3 hours and may require the use of anticoagulants to prevent clotting during the process.

The ABO blood group system is a classification system for human blood based on the presence or absence of two antigens, A and B, on the surface of red blood cells (RBCs). The system also includes the Rh factor, which is a separate protein found on the surface of some RBCs.

In the ABO system, there are four main blood groups: A, B, AB, and O. These groups are determined by the type of antigens present on the surface of the RBCs. Group A individuals have A antigens on their RBCs, group B individuals have B antigens, group AB individuals have both A and B antigens, and group O individuals have neither A nor B antigens on their RBCs.

In addition to the antigens on the surface of RBCs, the ABO system also involves the presence of antibodies in the plasma. Individuals with type A blood have anti-B antibodies in their plasma, those with type B blood have anti-A antibodies, those with type AB blood have neither anti-A nor anti-B antibodies, and those with type O blood have both anti-A and anti-B antibodies.

The ABO blood group system is important in blood transfusions and organ transplantation because of the potential for an immune response if there is a mismatch between the antigens on the donor's RBCs and the recipient's plasma antibodies. For example, if a type A individual receives a transfusion of type B blood, their anti-B antibodies will attack and destroy the donated RBCs, potentially causing a serious or life-threatening reaction.

It is important to note that there are many other blood group systems in addition to the ABO system, but the ABO system is one of the most well-known and clinically significant.

Abnormal erythrocytes refer to red blood cells that have an abnormal shape, size, or other characteristics. This can include various types of abnormalities such as:

1. Anisocytosis: Variation in the size of erythrocytes.
2. Poikilocytosis: Variation in the shape of erythrocytes, including but not limited to teardrop-shaped cells (dacrocytes), crescent-shaped cells (sickle cells), and spherical cells (spherocytes).
3. Anemia: A decrease in the total number of erythrocytes or a reduction in hemoglobin concentration, which can result from various underlying conditions such as iron deficiency, chronic disease, or blood loss.
4. Hemoglobinopathies: Abnormalities in the structure or function of hemoglobin, the protein responsible for carrying oxygen in erythrocytes, such as sickle cell anemia and thalassemia.
5. Inclusion bodies: Abnormal structures within erythrocytes, such as Heinz bodies (denatured hemoglobin) or Howell-Jolly bodies (nuclear remnants).

These abnormalities can be detected through a complete blood count (CBC) and peripheral blood smear examination. The presence of abnormal erythrocytes may indicate an underlying medical condition, and further evaluation is often necessary to determine the cause and appropriate treatment.

Glycolipids are a type of lipid (fat) molecule that contain one or more sugar molecules attached to them. They are important components of cell membranes, where they play a role in cell recognition and signaling. Glycolipids are also found on the surface of some viruses and bacteria, where they can be recognized by the immune system as foreign invaders.

There are several different types of glycolipids, including cerebrosides, gangliosides, and globosides. These molecules differ in the number and type of sugar molecules they contain, as well as the structure of their lipid tails. Glycolipids are synthesized in the endoplasmic reticulum and Golgi apparatus of cells, and they are transported to the cell membrane through vesicles.

Abnormalities in glycolipid metabolism or structure have been implicated in a number of diseases, including certain types of cancer, neurological disorders, and autoimmune diseases. For example, mutations in genes involved in the synthesis of glycolipids can lead to conditions such as Tay-Sachs disease and Gaucher's disease, which are characterized by the accumulation of abnormal glycolipids in cells.

Myelodysplastic syndromes (MDS) are a group of diverse bone marrow disorders characterized by dysplasia (abnormal development or maturation) of one or more types of blood cells or by ineffective hematopoiesis, resulting in cytopenias (lower than normal levels of one or more types of blood cells). MDS can be classified into various subtypes based on the number and type of cytopenias, the degree of dysplasia, the presence of ring sideroblasts, and cytogenetic abnormalities.

The condition primarily affects older adults, with a median age at diagnosis of around 70 years. MDS can evolve into acute myeloid leukemia (AML) in approximately 30-40% of cases. The pathophysiology of MDS involves genetic mutations and chromosomal abnormalities that lead to impaired differentiation and increased apoptosis of hematopoietic stem and progenitor cells, ultimately resulting in cytopenias and an increased risk of developing AML.

The diagnosis of MDS typically requires a bone marrow aspiration and biopsy, along with cytogenetic and molecular analyses to identify specific genetic mutations and chromosomal abnormalities. Treatment options for MDS depend on the subtype, severity of cytopenias, and individual patient factors. These may include supportive care measures, such as transfusions and growth factor therapy, or more aggressive treatments, such as chemotherapy and stem cell transplantation.

Bone marrow diseases, also known as hematologic disorders, are conditions that affect the production and function of blood cells in the bone marrow. The bone marrow is the spongy tissue inside bones where all blood cells are produced. There are various types of bone marrow diseases, including:

1. Leukemia: A cancer of the blood-forming tissues, including the bone marrow. Leukemia causes the body to produce large numbers of abnormal white blood cells, which can crowd out healthy blood cells and impair their function.
2. Lymphoma: A cancer that starts in the lymphatic system, which is part of the immune system. Lymphoma can affect the bone marrow and cause an overproduction of abnormal white blood cells.
3. Multiple myeloma: A cancer of the plasma cells, a type of white blood cell found in the bone marrow. Multiple myeloma causes an overproduction of abnormal plasma cells, which can lead to bone pain, fractures, and other complications.
4. Aplastic anemia: A condition in which the bone marrow does not produce enough new blood cells. This can lead to symptoms such as fatigue, weakness, and an increased risk of infection.
5. Myelodysplastic syndromes (MDS): A group of disorders in which the bone marrow does not produce enough healthy blood cells. MDS can lead to anemia, infections, and bleeding.
6. Myeloproliferative neoplasms (MPNs): A group of disorders in which the bone marrow produces too many abnormal white or red blood cells, or platelets. MPNs can lead to symptoms such as fatigue, itching, and an increased risk of blood clots.

Treatment for bone marrow diseases depends on the specific condition and its severity. Treatment options may include chemotherapy, radiation therapy, stem cell transplantation, or targeted therapies that target specific genetic mutations.

Phosphatidylinositol Diacylglycerol-Lyase is an enzyme that plays a crucial role in the breakdown and metabolism of certain lipids known as phosphoinositides. These are important components of cell membranes and are involved in various cellular processes such as signal transduction.

The systematic name for this enzyme is 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate D-3-phosphoinositide phospholipase C. Its function is to cleave 1,2-diacylglycerol and inositol 1,3,4,5-tetrakisphosphate from 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate. This reaction is a key step in the phosphoinositide signaling pathway, which is involved in regulating various cellular functions such as cell growth, differentiation, and metabolism.

Defects in this enzyme have been associated with certain diseases, including neurological disorders and cancer. Therefore, understanding its function and regulation is an important area of research in biology and medicine.

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

Phosphatidylinositols (PIs) are a type of phospholipid that are abundant in the cell membrane. They contain a glycerol backbone, two fatty acid chains, and a head group consisting of myo-inositol, a cyclic sugar molecule, linked to a phosphate group.

Phosphatidylinositols can be phosphorylated at one or more of the hydroxyl groups on the inositol ring, forming various phosphoinositides (PtdInsPs) with different functions. These signaling molecules play crucial roles in regulating cellular processes such as membrane trafficking, cytoskeletal organization, and signal transduction pathways that control cell growth, differentiation, and survival.

Phosphatidylinositol 4,5-bisphosphate (PIP2) is a prominent phosphoinositide involved in the regulation of ion channels, enzymes, and cytoskeletal proteins. Upon activation of certain receptors, PIP2 can be cleaved by the enzyme phospholipase C into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (InsP3), which act as second messengers to trigger downstream signaling events.

Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.

Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.

Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.

Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.

Erythrocyte aging, also known as red cell aging, is the natural process of changes and senescence that occur in red blood cells (erythrocytes) over time. In humans, mature erythrocytes are devoid of nuclei and organelles, and have a lifespan of approximately 120 days.

During aging, several biochemical and structural modifications take place in the erythrocyte, including:

1. Loss of membrane phospholipids and proteins, leading to increased rigidity and decreased deformability.
2. Oxidative damage to hemoglobin, resulting in the formation of methemoglobin and heinz bodies.
3. Accumulation of denatured proteins and aggregates, which can impair cellular functions.
4. Changes in the cytoskeleton, affecting the shape and stability of the erythrocyte.
5. Increased expression of surface markers, such as Band 3 and CD47, that signal the spleen to remove aged erythrocytes from circulation.

The spleen plays a crucial role in removing senescent erythrocytes by recognizing and phagocytosing those with altered membrane composition or increased expression of surface markers. This process helps maintain the overall health and functionality of the circulatory system.

Blood proteins, also known as serum proteins, are a group of complex molecules present in the blood that are essential for various physiological functions. These proteins include albumin, globulins (alpha, beta, and gamma), and fibrinogen. They play crucial roles in maintaining oncotic pressure, transporting hormones, enzymes, vitamins, and minerals, providing immune defense, and contributing to blood clotting.

Albumin is the most abundant protein in the blood, accounting for about 60% of the total protein mass. It functions as a transporter of various substances, such as hormones, fatty acids, and drugs, and helps maintain oncotic pressure, which is essential for fluid balance between the blood vessels and surrounding tissues.

Globulins are divided into three main categories: alpha, beta, and gamma globulins. Alpha and beta globulins consist of transport proteins like lipoproteins, hormone-binding proteins, and enzymes. Gamma globulins, also known as immunoglobulins or antibodies, are essential for the immune system's defense against pathogens.

Fibrinogen is a protein involved in blood clotting. When an injury occurs, fibrinogen is converted into fibrin, which forms a mesh to trap platelets and form a clot, preventing excessive bleeding.

Abnormal levels of these proteins can indicate various medical conditions, such as liver or kidney disease, malnutrition, infections, inflammation, or autoimmune disorders. Blood protein levels are typically measured through laboratory tests like serum protein electrophoresis (SPE) and immunoelectrophoresis (IEP).

Hematologic pregnancy complications refer to disorders related to the blood and blood-forming tissues that occur during pregnancy. These complications can have serious consequences for both the mother and the fetus if not properly managed. Some common hematologic pregnancy complications include:

1. Anemia: A condition characterized by a decrease in the number of red blood cells or hemoglobin in the blood, which can lead to fatigue, weakness, and shortness of breath. Iron-deficiency anemia is the most common type of anemia during pregnancy.
2. Thrombocytopenia: A condition characterized by a decrease in the number of platelets (cells that help blood clot) in the blood. Mild thrombocytopenia is relatively common during pregnancy, but severe thrombocytopenia can increase the risk of bleeding during delivery.
3. Gestational thrombotic thrombocytopenic purpura (GTTP): A rare but serious disorder that can cause blood clots to form in small blood vessels throughout the body, leading to a decrease in the number of platelets and red blood cells. GTTP can cause serious complications such as stroke, kidney failure, and even death if not promptly diagnosed and treated.
4. Disseminated intravascular coagulation (DIC): A condition characterized by abnormal clotting and bleeding throughout the body. DIC can be triggered by various conditions such as severe infections, pregnancy complications, or cancer.
5. Hemolysis, elevated liver enzymes, and low platelets (HELLP) syndrome: A serious complication of pregnancy that can cause damage to the liver and lead to bleeding. HELLP syndrome is often associated with preeclampsia, a condition characterized by high blood pressure and damage to organs such as the liver and kidneys.

It's important for pregnant women to receive regular prenatal care to monitor for these and other potential complications, and to seek prompt medical attention if any concerning symptoms arise.

Antilymphocyte serum (ALS) is a type of immune serum that contains antibodies against human lymphocytes. It is produced by immunizing animals, such as horses or rabbits, with human lymphocytes to stimulate an immune response and the production of anti-lymphocyte antibodies. The resulting serum is then collected and can be used as a therapeutic agent to suppress the activity of the immune system in certain medical conditions.

ALS is primarily used in the treatment of transplant rejection, particularly in organ transplantation, where it helps to prevent the recipient's immune system from attacking and rejecting the transplanted organ. It can also be used in the management of autoimmune diseases, such as rheumatoid arthritis and lupus, to suppress the overactive immune response that contributes to these conditions.

It is important to note that the use of ALS carries a risk of side effects, including allergic reactions, fever, and decreased white blood cell counts. Close monitoring and appropriate management of these potential adverse events are essential during treatment with ALS.

Acetylcholinesterase (AChE) is an enzyme that catalyzes the hydrolysis of acetylcholine (ACh), a neurotransmitter, into choline and acetic acid. This enzyme plays a crucial role in regulating the transmission of nerve impulses across the synapse, the junction between two neurons or between a neuron and a muscle fiber.

Acetylcholinesterase is located in the synaptic cleft, the narrow gap between the presynaptic and postsynaptic membranes. When ACh is released from the presynaptic membrane and binds to receptors on the postsynaptic membrane, it triggers a response in the target cell. Acetylcholinesterase rapidly breaks down ACh, terminating its action and allowing for rapid cycling of neurotransmission.

Inhibition of acetylcholinesterase leads to an accumulation of ACh in the synaptic cleft, prolonging its effects on the postsynaptic membrane. This can result in excessive stimulation of cholinergic receptors and overactivation of the cholinergic system, which may cause a range of symptoms, including muscle weakness, fasciculations, sweating, salivation, lacrimation, urination, defecation, bradycardia, and bronchoconstriction.

Acetylcholinesterase inhibitors are used in the treatment of various medical conditions, such as Alzheimer's disease, myasthenia gravis, and glaucoma. However, they can also be used as chemical weapons, such as nerve agents, due to their ability to disrupt the nervous system and cause severe toxicity.

Hemoglobin (Hb or Hgb) is the main oxygen-carrying protein in the red blood cells, which are responsible for delivering oxygen throughout the body. It is a complex molecule made up of four globin proteins and four heme groups. Each heme group contains an iron atom that binds to one molecule of oxygen. Hemoglobin plays a crucial role in the transport of oxygen from the lungs to the body's tissues, and also helps to carry carbon dioxide back to the lungs for exhalation.

There are several types of hemoglobin present in the human body, including:

* Hemoglobin A (HbA): This is the most common type of hemoglobin, making up about 95-98% of total hemoglobin in adults. It consists of two alpha and two beta globin chains.
* Hemoglobin A2 (HbA2): This makes up about 1.5-3.5% of total hemoglobin in adults. It consists of two alpha and two delta globin chains.
* Hemoglobin F (HbF): This is the main type of hemoglobin present in fetal life, but it persists at low levels in adults. It consists of two alpha and two gamma globin chains.
* Hemoglobin S (HbS): This is an abnormal form of hemoglobin that can cause sickle cell disease when it occurs in the homozygous state (i.e., both copies of the gene are affected). It results from a single amino acid substitution in the beta globin chain.
* Hemoglobin C (HbC): This is another abnormal form of hemoglobin that can cause mild to moderate hemolytic anemia when it occurs in the homozygous state. It results from a different single amino acid substitution in the beta globin chain than HbS.

Abnormal forms of hemoglobin, such as HbS and HbC, can lead to various clinical disorders, including sickle cell disease, thalassemia, and other hemoglobinopathies.

Hematopoiesis is the process of forming and developing blood cells. It occurs in the bone marrow and includes the production of red blood cells (erythropoiesis), white blood cells (leukopoiesis), and platelets (thrombopoiesis). This process is regulated by various growth factors, hormones, and cytokines. Hematopoiesis begins early in fetal development and continues throughout a person's life. Disorders of hematopoiesis can result in conditions such as anemia, leukopenia, leukocytosis, thrombocytopenia, or thrombocytosis.

CD58 (also known as LFA-3) is a cell surface glycoprotein that functions as a co-stimulatory molecule in the immune system. It is found on various cells, including antigen presenting cells such as dendritic cells and B cells. CD58 interacts with its receptor, CD2, which is found on T cells, natural killer (NK) cells, and some other leukocytes. This interaction provides a costimulatory signal that helps to activate T cells and NK cells, enhancing their immune responses against pathogens or infected cells.

In the context of antigens, CD58 may be involved in presenting antigenic peptides to T cells during an adaptive immune response. The interaction between CD58 on antigen-presenting cells and CD2 on T cells contributes to the activation and proliferation of T cells specific to that particular antigen. This process is crucial for the development of effective immunity against infections and cancer.

It's important to note that while CD58 plays a role in immune responses, it is not an antigen itself. An antigen is typically defined as a molecule (usually a protein or polysaccharide) that is recognized by the adaptive immune system and can stimulate an immune response.

Complement activating enzymes are proteins that play a crucial role in the activation of the complement system, which is a part of the immune system. The complement system is a complex series of biochemical reactions that help to eliminate pathogens and damaged cells from the body.

There are several types of complement activating enzymes, including:

1. Classical pathway activators: These include the C1, C4, and C2 components of the complement system. When activated, they trigger a series of reactions that lead to the formation of the membrane attack complex (MAC), which creates a pore in the membrane of the target cell, leading to its lysis.
2. Alternative pathway activators: These include factors B, D, and P. They are constantly active at low levels and can be activated by surfaces that are not normally found in the body, such as bacterial cell walls. Once activated, they also trigger the formation of the MAC.
3. Lectin pathway activators: These include mannose-binding lectin (MBL) and ficolins. They bind to carbohydrates on the surface of microbes and activate the complement system through the MBL-associated serine proteases (MASPs).

Overall, complement activating enzymes play a critical role in the immune response by helping to identify and eliminate pathogens and damaged cells from the body.

Blood cells are the formed elements in the blood, including red blood cells (erythrocytes), white blood cells (leukocytes), and platelets (thrombocytes). These cells are produced in the bone marrow and play crucial roles in the body's functions. Red blood cells are responsible for carrying oxygen to tissues and carbon dioxide away from them, while white blood cells are part of the immune system and help defend against infection and disease. Platelets are cell fragments that are essential for normal blood clotting.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Thrombosis is the formation of a blood clot (thrombus) inside a blood vessel, obstructing the flow of blood through the circulatory system. When a clot forms in an artery, it can cut off the supply of oxygen and nutrients to the tissues served by that artery, leading to damage or tissue death. If a thrombus forms in the heart, it can cause a heart attack. If a thrombus breaks off and travels through the bloodstream, it can lodge in a smaller vessel, causing blockage and potentially leading to damage in the organ that the vessel supplies. This is known as an embolism.

Thrombosis can occur due to various factors such as injury to the blood vessel wall, abnormalities in blood flow, or changes in the composition of the blood. Certain medical conditions, medications, and lifestyle factors can increase the risk of thrombosis. Treatment typically involves anticoagulant or thrombolytic therapy to dissolve or prevent further growth of the clot, as well as addressing any underlying causes.

A frameshift mutation is a type of genetic mutation that occurs when the addition or deletion of nucleotides in a DNA sequence is not divisible by three. Since DNA is read in groups of three nucleotides (codons), which each specify an amino acid, this can shift the "reading frame," leading to the insertion or deletion of one or more amino acids in the resulting protein. This can cause a protein to be significantly different from the normal protein, often resulting in a nonfunctional protein and potentially causing disease. Frameshift mutations are typically caused by insertions or deletions of nucleotides, but they can also result from more complex genetic rearrangements.

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.

Leukocytes, also known as white blood cells (WBCs), are a crucial component of the human immune system. They are responsible for protecting the body against infections and foreign substances. Leukocytes are produced in the bone marrow and circulate throughout the body in the bloodstream and lymphatic system.

There are several types of leukocytes, including:

1. Neutrophils - These are the most abundant type of leukocyte and are primarily responsible for fighting bacterial infections. They contain enzymes that can destroy bacteria.
2. Lymphocytes - These are responsible for producing antibodies and destroying virus-infected cells, as well as cancer cells. There are two main types of lymphocytes: B-lymphocytes and T-lymphocytes.
3. Monocytes - These are the largest type of leukocyte and help to break down and remove dead or damaged tissues, as well as microorganisms.
4. Eosinophils - These play a role in fighting parasitic infections and are also involved in allergic reactions and inflammation.
5. Basophils - These release histamine and other chemicals that cause inflammation in response to allergens or irritants.

An abnormal increase or decrease in the number of leukocytes can indicate an underlying medical condition, such as an infection, inflammation, or a blood disorder.

The alternative complement pathway is one of the three initiating pathways of the complement system, which is a part of the innate immune system that helps to clear pathogens and damaged cells from the body. The other two pathways are the classical and lectin pathways.

The alternative pathway is continuously activated at a low level, even in the absence of infection or injury, through the spontaneous cleavage of complement component C3 into C3a and C3b by the protease factor D in the presence of magnesium ions. The generated C3b can then bind covalently to nearby surfaces, including pathogens and host cells.

On self-surfaces, regulatory proteins like decay-accelerating factor (DAF) or complement receptor 1 (CR1) help to prevent the formation of the alternative pathway convertase and thus further activation of the complement system. However, on foreign surfaces, the C3b can recruit more complement components, forming a complex called the alternative pathway convertase (C3bBb), which cleaves additional C3 molecules into C3a and C3b.

The generated C3b can then bind to the surface and participate in the formation of the membrane attack complex (MAC), leading to the lysis of the target cell. The alternative pathway plays a crucial role in the defense against gram-negative bacteria, fungi, and parasites, as well as in the clearance of immune complexes and apoptotic cells. Dysregulation of the alternative complement pathway has been implicated in several diseases, including autoimmune disorders and atypical hemolytic uremic syndrome (aHUS).

Thrombophilia is a medical condition characterized by an increased tendency to form blood clots (thrombi) due to various genetic or acquired abnormalities in the coagulation system. These abnormalities can lead to a hypercoagulable state, which can cause thrombosis in both veins and arteries. Commonly identified thrombophilias include factor V Leiden mutation, prothrombin G20210A mutation, antithrombin deficiency, protein C deficiency, and protein S deficiency.

Acquired thrombophilias can be caused by various factors such as antiphospholipid antibody syndrome (APS), malignancies, pregnancy, oral contraceptive use, hormone replacement therapy, and certain medical conditions like inflammatory bowel disease or nephrotic syndrome.

It is essential to diagnose thrombophilia accurately, as it may influence the management of venous thromboembolism (VTE) events and guide decisions regarding prophylactic anticoagulation in high-risk situations.

... can refer to: Paroxysmal nocturnal hemoglobinuria Paroxysmal cold hemoglobinuria Hemoglobinuria This ... disambiguation page lists articles associated with the title Paroxysmal hemoglobinuria. If an internal link led you here, you ...
... (PCH) is an autoimmune hemolytic anemia featured by complement-mediated intravascular hemolysis ... 259 Paroxysmal cold hemoglobinuria: 259 Idiopathic Secondary Acute, transient (Infections other than syphilis): 259 Chronic ( ... which includes cold agglutinin disease and paroxysmal cold hemoglobinuria. These classifications are based on the ... Chronic relapsing PCH manifests as episodic hemoglobinuria and anemic symptoms, usually milder than the acute form. While the ...
The Dutch physician Enneking coined the term "paroxysmal nocturnal hemoglobinuria" (or haemoglobinuria paroxysmalis nocturna in ... Paroxysmal nocturnal hemoglobinuria (PNH) is a rare, acquired, life-threatening disease of the blood characterized by ... "Paroxysmal Nocturnal Hemoglobinuria". The Lecturio Medical Concept Library. Retrieved 2 September 2021. Rother RP, Bell L, ... "Paroxysmal Nocturnal Hemoglobinuria - NORD (National Organization for Rare Disorders)". NORD. 2016. Retrieved 3 July 2017. ...
Paroxysmal nocturnal hemoglobinuria; the mechanism of hemolysis and its relation to the coagulation mechanism. Blood. 1950 Sep; ...
... hemoglobinuria). When restricted to the morning hemoglobinuria may suggest paroxysmal nocturnal haemoglobinuria. Direct ... Brodsky, Robert A. (2014-10-30). "Paroxysmal nocturnal hemoglobinuria". Blood. 124 (18): 2804-2811. doi:10.1182/blood-2014-02- ... "Paroxysmal Nocturnal Hemoglobinuria with Glucose-6-Phosphate Dehydrogenase Deficiency: A Case Report and Review of the ... Paroxysmal nocturnal hemoglobinuria (PNH), sometimes referred to as Marchiafava-Micheli syndrome, is a rare, acquired, ...
Brodsky RA (2009). "Paroxysmal nocturnal hemoglobinuria". In Hoffman R, Benz Jr EJ, Shatill SJ (eds.). Hematology: Basic ... and paroxysmal nocturnal hemoglobinuria (PNH). For people with PNH, it improves quality of life and decreases the need for ... paroxysmal nocturnal hemoglobinuria (PNH), through a bulk-buy deal reached by the provincial premiers in 2011." In February ... intended for the treatment of adults and children in paroxysmal nocturnal hemoglobinuria. The applicant for this medicinal ...
Bird, GW (1977). "Paroxysmal cold haemoglobinuria". British Journal of Haematology. 37 (2): 167-71. doi:10.1111/j.1365- ... Taylor, CJ; Neilson, JR; Chandra, D; Ibrahim, Z (2003). "Recurrent paroxysmal cold haemoglobinuria in a 3-year-old child: a ... Sivakumaran, M; Murphy, PT; Booker, DJ; Wood, JK; Stamps, R; Sokol, RJ (1999). "Paroxysmal cold haemoglobinuria caused by non- ... Sharara, AI; Hillsley, RE; Wax, TD; Rosse, WF (1994). "Paroxysmal cold hemoglobinuria associated with non-Hodgkin's lymphoma". ...
SLC6A3 Paroxysmal extreme pain disorder; 167400; SCN9A Paroxysmal nocturnal hemoglobinuria, somatic; 300818; PIGA Paroxysmal ... paroxysmal familial, 2; 612956; DPP6 Ventricular tachycardia, catecholaminergic polymorphic, 1; 604772; RYR2 Ventricular ... ADAMTSL2 Generalized epilepsy and paroxysmal dyskinesia; 609446; KCNMA1 Generalized epilepsy with febrile seizures plus; 604233 ...
"Paroxysmal cold hemoglobinuria (PCH) e". Medline Plus. U.S. Department of Health and Human Services, National Institutes of ...
The sucrose lysis test is a diagnostic laboratory test used for diagnosing paroxysmal nocturnal hemoglobinuria (PNH), as well ... Hartmann, Robert C.; Jenkins, David E. (1966-07-21). "The Sugar-Water Test for Paroxysmal Nocturnal Hemoglobinuria". New ... Krauss, Jonathan S. (2012). "The Laboratory Diagnosis of Paroxysmal Nocturnal Hemoglobinuria (PNH): Update 2010". Laboratory ... Krauss, Jonathan S (2003-10-01). "Laboratory Diagnosis of Paroxysmal Nocturnal Hemoglobinuria". Annals of Clinical & Laboratory ...
People who have paroxysmal nocturnal hemoglobinuria (PNH) appear to be especially at risk for Budd-Chiari syndrome, more than ... Aug 1996). "Paroxysmal nocturnal haemoglobinuria: long-term follow-up and prognostic factors. French Society of Haematology". ... Hillmen P, Lewis SM, Bessler M, Luzzatto L, Dacie JV (Nov 1995). "Natural history of paroxysmal nocturnal hemoglobinuria". N ... disorders that may result in Budd-Chiari syndrome include antiphospholipid syndrome and paroxysmal nocturnal hemoglobinuria, ...
... (FLAER) is used in a flow cytometric assay to diagnose paroxysmal nocturnal hemoglobinuria ( ... Brodsky, RA (2009). "How I treat paroxysmal nocturnal hemoglobinuria". Blood. 113 (26): 6522-7. doi:10.1182/blood-2009-03- ... 2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood. 106 (12): 3699-709. doi:10.1182/blood-2005-04- ...
December 2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood. 106 (12): 3699-709. doi:10.1182/blood ... Paroxysmal nocturnal hemoglobinuria is caused by complement breakdown of RBCs due to an inability to make GPI. Thus the RBCs ... paroxysmal nocturnal hemoglobinuria, atypical hemolytic uremic syndrome and ischemia-reperfusion injuries, and rejection of ...
Paroxysmal nocturnal hemoglobinuria Winkelstein, Jerry A. (2004). "Complement Deficiencies". In Crocetti, Michael; Barone, ...
The Ham test is a blood test used in the diagnosis of paroxysmal nocturnal hemoglobinuria (PNH). Patient red blood cells (RBCs ... Ham, Thomas H. (1937). "Chronic Hemolytic Anemia with Paroxysmal Nocturnal Hemoglobinuria". New England Journal of Medicine. ... MedlinePlus Encyclopedia: Ham test "Paroxysmal Nocturnal Hemoglobinuria - PNH". ARUP. Ferri, Fred F. (2015). Ferri's Clinical ...
... like Paroxysmal Nocturnal Hemoglobinuria 4. Sickle Cell Anemia's, 5. Thalassemia 6.Immune Deficiencies disease 7. Metabolic ...
Riley AL, Ryan LM, Roth DA (1977). "Renal proximal tubular dysfunction and paroxysmal nocturnal hemoglobinuria". Am. J. Med. 62 ... Lowe syndrome Tyrosinemia Wilson's disease Acquired disorders Amyloidosis Multiple myeloma Paroxysmal nocturnal hemoglobinuria ...
2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood. 106 (12): 3699-709. doi:10.1182/blood-2005-04- ... expression is reduced in persons with mutations that reduce GPI levels such as those with paroxysmal nocturnal hemoglobinuria ( ...
Motoyama N, Okada N, Yamashina M, Okada H (1992). "Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in ... 2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood. 106 (12): 3699-709. doi:10.1182/blood-2005-04- ... as a cause of paroxysmal nocturnal hemoglobinuria". N. Engl. J. Med. 323 (17): 1184-1189. doi:10.1056/NEJM199010253231707. PMID ... that reduce expression of CD59 and decay-accelerating factor on red blood cells result in paroxysmal nocturnal hemoglobinuria. ...
Paroxysmal Nocturnal Hemoglobinuria and the Glycosylphosphatidylinositol-Linked Proteins. San Diego: Academic Press, 2000. ...
"Comparison of paroxysmal cold hemoglobinuria, cold agglutinin disease, and cryoglobulinemia". UpToDate. Retrieved 2023-05-01. ... paroxysmal cold hemoglobinuria in the process of Donath-Landsteiner hemolytic anemia, and vasculitis, respectively. Cold ... and paroxysmal cold hemoglobinuria (PCH) are entirely complement-dependent disorders. Hemolysis induced by cold agglutinin ... "Two Different Serologic Mechanisms of Paroxysmal Cold Hemoglobinuria, Illustrated by Three Cases" (PDF). Blood. Archived from ...
1995) Defective glycosyl-phosphatidylinositol anchor synthesis and paroxysmal nocturnal hemoglobinuria. Adv Immunol. 60, 57-103 ...
"Red-cell Survival in Paroxysmal Nocturnal Haemoglobinuria". Br Med J. 2 (5056): 1277-1279. doi:10.1136/bmj.2.5056.1277. PMC ...
All of these, except paroxysmal nocturnal hemoglobinuria, are hereditary genetic disorders. Hereditary spherocytosis is a ... Hemoglobinopathies Sickle cell anemia Hemoglobinopathies causing unstable hemoglobins Paroxysmal nocturnal hemoglobinuria ...
1994). "Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene". EMBO J. 13 (1): 110-7. ... Paroxysmal nocturnal hemoglobinuria, an acquired hematologic disorder, has been shown to result from somatic mutations in this ... 1994). "Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a ... 2003). "The spectrum of PIG-A gene mutations in aplastic anemia/paroxysmal nocturnal hemoglobinuria (AA/PNH): a high incidence ...
June 2015). "Screening of patients with idiopathic venous thromboembolism for paroxysmal nocturnal hemoglobinuria clones". ... paroxysmal nocturnal hemoglobinuria, nephrotic syndrome, chronic kidney disease, polycythemia vera, essential thrombocythemia, ...
Paroxysmal nocturnal hemoglobinuria (PNH) is a rare condition resulting from acquired alterations in the PIGA gene, which plays ... Brodsky RA (April 2008). "Narrative review: paroxysmal nocturnal hemoglobinuria: the physiology of complement-related hemolytic ...
It is designed to bind to and prevent the activation of Complement component 5 (C5). Paroxysmal nocturnal hemoglobinuria is ... Stern RM, Connell NT (2019). "Ravulizumab: a novel C5 inhibitor for the treatment of paroxysmal nocturnal hemoglobinuria". Ther ... September 2018). "Ravulizumab (ALXN1210) in patients with paroxysmal nocturnal hemoglobinuria: results of 2 phase 1b/2 studies ... In paroxysmal nocturnal hemoglobinuria, proteins known as the 'complement system', which is part of the immune system, become ...
Parker, C. J. (2002). "Historical aspects of paroxysmal nocturnal haemoglobinuria: 'defining the disease'". British Journal of ... Sir Dacie is credited with characterizing the relationship between paroxysmal nocturnal hemoglobinuria and bone marrow failure ...
CHAPLE syndrome is characterized by complement-mediated autoimmune hemolysis and paroxysmal nocturnal hemoglobinuria. The ... "Paroxysmal Nocturnal Hemoglobinuria (PNH) - NORD (National Organization for Rare Disorders)". NORD (National Organization for ...
Paroxysmal hemoglobinuria can refer to: Paroxysmal nocturnal hemoglobinuria Paroxysmal cold hemoglobinuria Hemoglobinuria This ... disambiguation page lists articles associated with the title Paroxysmal hemoglobinuria. If an internal link led you here, you ...
Paroxysmal nocturnal hemoglobinuria (PNH) is a disorder that leads to the premature death and impaired production of blood ... medlineplus.gov/genetics/condition/paroxysmal-nocturnal-hemoglobinuria/ Paroxysmal nocturnal hemoglobinuria. ... Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired (not inherited) disorder that leads to the premature death and ... Luzzatto L. Paroxysmal nocturnal hemoglobinuria: an acquired X-linked genetic disease with somatic-cell mosaicism. Curr Opin ...
... These quiz questions about paroxysmal nocturnal hemoglobinuria (PNH) are ...
... including severe anemia and hemoglobinuria, occurring upon exposure to cold temperatures and resultin... ... Paroxysmal cold hemoglobinuria (PCH) has the distinction of being the first, albeit rarest, type of autoimmune hemolytic anemia ... encoded search term (Paroxysmal Cold Hemoglobinuria) and Paroxysmal Cold Hemoglobinuria What to Read Next on Medscape ... Paroxysmal cold haemoglobinuria in an adult with chicken pox. Br J Haematol. 2000 May. 109(2):328-9. [QxMD MEDLINE Link]. ...
Paroxysmal nocturnal hemoglobinuria (PNH) is a rare, chronic, debilitating disorder that most frequently presents in early ... encoded search term (Paroxysmal Nocturnal Hemoglobinuria) and Paroxysmal Nocturnal Hemoglobinuria What to Read Next on Medscape ... Paroxysmal Nocturnal Hemoglobinuria. Updated: Jun 06, 2023 * Author: Emmanuel C Besa, MD; Chief Editor: Sara J Grethlein, MD, ... For some time, paroxysmal nocturnal hemoglobinuria (PNH) has been known to result from somatic mutations in the PIGA gene, ...
Nahla Heikal discuss Paroxysmal Nocturnal Hemoglobinuria in this December 2016 Pearl of Laboratory Medicine. ... Welcome to this Pearl of Laboratory Medicine on Paroxysmal Nocturnal Hemoglobinuria. Slide 2:. Paroxysmal nocturnal ... Hemoglobinuria is part of the name but it is a less commonly seen complication, and approximately 75% of patients present ... Although the disease is called paroxysmal, there is ongoing destructive progressive hemolysis even in the absence of symptoms. ...
In non-severe aplastic anemia, the presence of a paroxysmal nocturnal hemoglobinuria (PNH) clone was positively associated with ... We aimed to determine whether small paroxysmal nocturnal hemoglobinuria (PNH) clones detected by flow cytometry (FCM) harbor ... 5-Point Change on FACIT-Fatigue "Clinically Important" in Paroxysmal Nocturnal Hemoglobinuria Oct 3, 2023 ... 5-Point Change on FACIT-Fatigue "Clinically Important" in Paroxysmal Nocturnal Hemoglobinuria Sep 14, 2023 ...
... an investigational oral treatment for paroxysmal nocturnal hemoglobinuria (PNH), presented at the virtually held 2020 European ... Paroxysmal nocturnal haemoglobinuria. Nat Rev Dis Primers 2017;3:17028.. 7. Risitano AM and Rotoli B. Paroxysmal nocturnal ... Anti-Complement Treatment in Paroxysmal Nocturnal Hemoglobinuria: Where we Stand and Where we are Going. Transl Med UniSa 2014; ... Novartis announces positive results from Phase II study of LNP023 in patients with paroxysmal nocturnal hemoglobinuria (PNH) ...
Paroxysmal nocturnal hemoglobinuria (PNH) is a rare, chronic, debilitating disorder that most frequently presents in early ... encoded search term (Paroxysmal Nocturnal Hemoglobinuria) and Paroxysmal Nocturnal Hemoglobinuria What to Read Next on Medscape ... Paroxysmal Nocturnal Hemoglobinuria. Updated: Jun 06, 2023 * Author: Emmanuel C Besa, MD; Chief Editor: Sara J Grethlein, MD, ... For some time, paroxysmal nocturnal hemoglobinuria (PNH) has been known to result from somatic mutations in the PIGA gene, ...
... the diagnosis of paroxysmal nocturnal hemoglobinuria (PNH) is straightforward when flow cytometric analysis of the peripheral ... Update on the diagnosis and management of paroxysmal nocturnal hemoglobinuria. Journal Title: Hematology Am Soc Hematol Educ ... Once suspected, the diagnosis of paroxysmal nocturnal hemoglobinuria (PNH) is straightforward when flow cytometric analysis of ... Update on the diagnosis and management of paroxysmal nocturnal hemoglobinuria. ...
Danicopan Gets Breakthrough Therapy Status for Paroxysmal Nocturnal Hemoglobinuria. *Ultomiris Approved for Paroxysmal ... Pegcetacoplan Superior to Eculizumab in Paroxysmal Nocturnal Hemoglobinuria Trial. Brian Park, PharmD ... Close more info about Pegcetacoplan Superior to Eculizumab in Paroxysmal Nocturnal Hemoglobinuria Trial ... Close more info about Pegcetacoplan Superior to Eculizumab in Paroxysmal Nocturnal Hemoglobinuria Trial ...
... eculizumab is not the cure for Paroxysmal nocturnal hemoglobinuria (PNH), and room for improvement remains. Indeed, the ... The treatment of paroxysmal nocturnal hemoglobinuria has been revolutionized by the introduction of the anti-C5 agent ... The treatment of paroxysmal nocturnal hemoglobinuria has been revolutionized by the introduction of the anti-C5 agent ... Coversin in Paroxysmal Nocturnal Haemoglobinuria (PNH) in Patients With Resistance to Eculizumab Due to Complement C5 ...
Did you know that intravascular and extravascular hemolyses are the 2 hemolytic pathways underlying paroxysmal nocturnal ... Multidisciplinary Conversations on Paroxysmal Nocturnal Hemoglobinuria: How to Involve Patients in the Management of Their ... Multidisciplinary Conversations on Paroxysmal Nocturnal Hemoglobinuria: How to Involve Patients in the Management of Their ...
Use this form to apply for initial grandfathered PBS-subsidised treatment with pegcetacoplan for paroxysmal nocturnal ... Paroxysmal nocturnal haemoglobinuria - pegcetacoplan - initial grandfather authority application form (PB345). Use this form to ... Download and complete the paroxysmal nocturnal haemoglobinuria - pegcetacoplan - initial grandfather authority application form ... apply for initial grandfathered PBS-subsidised treatment with pegcetacoplan for paroxysmal nocturnal haemoglobinuria. ...
Pathology: paroxysmal nocturnal hemoglobinuria +311770 OMIM record - By selecting the cell line name, you will receive the ...
... including severe anemia and hemoglobinuria, occurring upon exposure to cold temperatures and resultin... ... Paroxysmal cold hemoglobinuria (PCH) has the distinction of being the first, albeit rarest, type of autoimmune hemolytic anemia ... encoded search term (Paroxysmal Cold Hemoglobinuria) and Paroxysmal Cold Hemoglobinuria What to Read Next on Medscape ... Paroxysmal Cold Hemoglobinuria Medication. Updated: Apr 01, 2015 * Author: Neetu Radhakrishnan, MD; Chief Editor: Emmanuel C ...
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Study Name: Paroxysmal Nocturnal Hemoglobinuria (PNH) Registry. Condition: Paroxysmal Nocturnal Hemoglobinuria. Date: 2011-04- ... Study Name: Coversin in Paroxysmal Nocturnal Haemoglobinuria (PNH). Condition: Paroxysmal Nocturnal Haemoglobinuria (PNH). Date ... Study Name: A Treatment Study of ACH-0144471 in Patients With Paroxysmal Nocturnal Hemoglobinuria (PNH). Condition: Paroxysmal ... Safety and Pharmacokinetics of TT30 in Subjects With Paroxysmal Nocturnal Hemoglobinuria (PNH). Condition: Paroxysmal Nocturnal ...
Topic: Paroxysmal Nocturnal Hemoglobinuria. Paroxysmal Nocturnal Hemoglobinuria. Feb 2024 , Assessment Interventions of ...
... including severe anemia and hemoglobinuria, occurring upon exposure to cold temperatures and resultin... ... Paroxysmal cold hemoglobinuria (PCH) has the distinction of being the first, albeit rarest, type of autoimmune hemolytic anemia ... encoded search term (Paroxysmal Cold Hemoglobinuria) and Paroxysmal Cold Hemoglobinuria What to Read Next on Medscape ... Paroxysmal Cold Hemoglobinuria. Updated: Apr 01, 2015 * Author: Neetu Radhakrishnan, MD; Chief Editor: Emmanuel C Besa, MD more ...
More in Taking Control of Paroxysmal Nocturnal Hemoglobinuria. *. What You Need to Know About Paroxysmal Nocturnal ... Paroxysmal nocturnal hemoglobinuria. (2007,May). http://ghr.nlm.nih.gov/condition/paroxysmal-nocturnal-hemoglobinuria. ... Paroxysmal nocturnal hemoglobinuria PNH is a rare, acquired disease, which means its not genetic. It causes the red blood ... Paroxysmal nocturnal hemoglobinuria (PNH) is a rare disorder that causes red blood cells to break down sooner than they should. ...
Paroxysmal Nocturnal Hemoglobinuria. The efficacy and safety of EMPAVELI in patients with PNH were assessed in two open label, ... Paroxysmal Nocturnal Hemoglobinuria. Study in Complement-Inhibitor Experienced Adult Patients with PNH (Study APL2-302). The ... Empaveli (pegcetacoplan) is a complement inhibitor used to treat adult patients with paroxysmal nocturnal hemoglobinuria (PNH). ... EMPAVELI is a prescription medicine used to treat adults with a disease called paroxysmal nocturnal hemoglobinuria (PNH). ...
New life-saving treatments for PNH in clinical trial on Paroxysmal nocturnal hemoglobinuria (PNH) Registry ...
A patient with certain clinical or laboratory findings should be tested for presence of paroxysmal nocturnal hemoglobinuria ... Paroxysmal Nocturnal Hemoglobinuria Indications. Purpose: To determine if a patient should be tested for paroxysmal nocturnal ... Purpose: To determine if a patient should be tested for paroxysmal nocturnal hemoglobinuria (PNH). ...
New life-saving treatments for PNH in clinical trial on Paroxysmal nocturnal hemoglobinuria (PNH) Registry ...
PEGASUS Findings Reveal Sustained Benefits With Pegcetacoplan That Outperform Eculizumab in Paroxysmal Nocturnal Hemoglobinuria ...
Paroxysmal nocturnal hemoglobinuria: a complement-mediated hemolytic anemia.. Amy E DeZern, Robert A Brodsky. Hematology/ ... Paroxysmal nocturnal hemoglobinuria is manifests with a chronic hemolytic anemia from uncontrolled complement activation, a ...
Paroxysmal Nocturnal Hemoglobinuria (PNH) - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD ... Paroxysmal nocturnal hemoglobinuria is most common among men in their 20s, but it occurs in both sexes and at any age. ... Paroxysmal nocturnal hemoglobinuria is a clonal disorder caused by an acquired mutation in the PIGA gene in hematopoietic stem ... Paroxysmal nocturnal hemoglobinuria is suspected in patients who have typical symptoms of anemia (eg, pallor, fatigue, ...
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1. Recent advance in the diagnosis and treatment of paroxysmal nocturnal hemoglobinuria (PNH). Add to wishlist ... Enquiry about 1. Recent advance in the diagnosis and treatment of paroxysmal nocturnal hemoglobinuria (PNH). ... 1. Recent advance in the diagnosis and treatment of paroxysmal nocturnal hemoglobinuria (PNH). ... 1. Recent advance in the diagnosis and treatment of paroxysmal nocturnal hemoglobinuria (PNH) ...
  • however, eculizumab is not the cure for Paroxysmal nocturnal hemoglobinuria (PNH), and room for improvement remains. (frontiersin.org)
  • [ 45 ] A review of the literature did not show any benefit with eculizumab in this condition (unlike in paroxysmal nocturnal hemoglobinuria). (medscape.com)
  • Patients with paroxysmal nocturnal hemoglobinuria (PNH) undergoing treatment with eculizumab or ravulizumab have a high illness burden and relatively low quality of life (QoL), suggesting a need for improved treatments, according to research published in Annals of Hematology . (hematologyadvisor.com)
  • BUSINESS WIRE )-- A prespecified interim analysis of the ALPHA Phase III trial evaluating danicopan (ALXN2040), an investigational, oral factor D inhibitor, as an add-on to C5 inhibitor therapy ULTOMIRIS ® (ravulizumab-cwvz) or SOLIRIS ® (eculizumab) showed positive high-level results in patients with paroxysmal nocturnal hemoglobinuria (PNH) who experience clinically significant extravascular hemolysis (EVH). (biospace.com)
  • Paroxysmal nocturnal hemoglobinuria patients who have not received eculizumab treatment due to mild hemolysis may benefit from eculizumab treatment. (elsevierpure.com)
  • The terminal complement inhibitor eculizumab was recently shown to be effective and well tolerated in patients with paroxysmal nocturnal hemoglobinuria (PNH). (ashpublications.org)
  • Eculizumab is most commonly prescribed for treatment of 2 rare blood disorders: atypical hemolytic uremic syndrome (aHUS) and paroxysmal nocturnal hemoglobinuria (PNH). (cdc.gov)
  • Paroxysmal hemoglobinuria can refer to: Paroxysmal nocturnal hemoglobinuria Paroxysmal cold hemoglobinuria Hemoglobinuria This disambiguation page lists articles associated with the title Paroxysmal hemoglobinuria. (wikipedia.org)
  • Hemoglobinuria is part of the name but it is a less commonly seen complication, and approximately 75% of patients present without hemoglobinuria. (aacc.org)
  • We aimed to determine whether small paroxysmal nocturnal hemoglobinuria (PNH) clones detected by flow cytometry (FCM) harbor PIG gene mutations with quantitative correlation.We analyzed 89 specimens from 63 patients whose PNH. (physiciansweekly.com)
  • Study establishes 5-point change as clinically important for FACIT-Fatigue in patients with paroxysmal nocturnal hemoglobinuria (PNH). (physiciansweekly.com)
  • Among patients with aplastic anemia (AA), the presence of a positive pre-treatment paroxysmal nocturnal hemoglobinuria (PNH) clone had a positive impact on response to intensive immunosuppressive therapy (IIST), according to. (physiciansweekly.com)
  • Empaveli (pegcetacoplan) is a complement inhibitor used to treat adult patients with paroxysmal nocturnal hemoglobinuria (PNH). (rxlist.com)
  • Paroxysmal nocturnal hemoglobinuria is suspected in patients who have typical symptoms of anemia (eg, pallor, fatigue, dizziness, possible hypotension) or unexplained normocytic anemia with intravascular hemolysis, particularly if leukopenia or thrombocytopenia and/or thrombotic events are present. (msdmanuals.com)
  • In paroxysmal nocturnal hemoglobinuria (PNH), various symptoms due to intravascular hemolysis exert a negative impact on patients' quality of life (QOL). (elsevierpure.com)
  • In patients with paroxysmal nocturnal hemoglobinuria (PNH), the membrane-attack complex (MAC) formed on red blood cells (RBCs) causes hemolysis due to the patient's own activated complement system by an infection, inflammation, or surgical stress. (biomedcentral.com)
  • I'm Dr. Charles Turck, and joining me to discuss how we can help our patients with the impacts of paroxysmal nocturnal hemoglobinuria, or PNH for short, are Drs. Tim Kubal and Hana Safah. (reachmd.com)
  • Apellis Pharmaceuticals announced positive topline results from the phase 3 PEGASUS trial of pegcetacoplan (APL-2) in the treatment of paroxysmal nocturnal hemoglobinuria (PNH). (empr.com)
  • Use this form to apply for initial grandfathered PBS-subsidised treatment with pegcetacoplan for paroxysmal nocturnal haemoglobinuria. (servicesaustralia.gov.au)
  • The EMPAVELI Injector is a compact, single-use, on-body device designed to enhance self-administration of EMPAVELI (pegcetacoplan), which is approved for adults with paroxysmal nocturnal hemoglobinuria (PNH). (tmcnet.com)
  • Empaveli (pegcetacoplan) (MW, 44 kDa) is used to treat paroxysmal nocturnal hemoglobinuria . (medscape.com)
  • This condition was first described in 1854 as an abrupt onset of systemic manifestations, including severe anemia and hemoglobinuria, occurring upon exposure to cold temperatures and resulting from massive intravascular hemolysis. (medscape.com)
  • This series of containers holds urine of a patient with paroxysmal nocturnal hemoglobinuria, showing the episodic nature of the dark urine (hemoglobinuria) during intravascular hemolysis, usually occurring at night. (medscape.com)
  • Hemolysis has been shown to occur throughout the day and is not actually paroxysmal, but the concentration of urine overnight produces the dramatic change in color. (medscape.com)
  • Although the disease is called paroxysmal, there is ongoing destructive progressive hemolysis even in the absence of symptoms. (aacc.org)
  • PNH is a very rare, life-threatening and debilitating disease characterized by complement-mediated hemolysis with or without hemoglobinuria. (empr.com)
  • Paroxysmal nocturnal hemoglobinuria (PNH) is a rare hematological disorder characterized by complement-mediated intravascular hemolysis, bone marrow failure, and severe thrombophilia ( 1 ). (frontiersin.org)
  • Paroxysmal nocturnal hemoglobinuria (PNH) is a rare acquired disorder characterized by intravascular hemolysis and hemoglobinuria. (msdmanuals.com)
  • Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired clonal hematologic disorder with typical clinical manifestations, including intravascular hemolysis, venous thrombosis, and defective hematopoiesis [ 1 ]. (annexpublishers.co)
  • During the first 4 months after diagnosis, the patient nal hemoglobinuria (PNH) and atypical hemolytic uremic exhibited mild pancytopenia and compensated hemolysis syndrome. (cdc.gov)
  • The antibody thermal activity range of paroxysmal cold hemoglobinuria is simlar to that of cold hemagglutinin disease (CHD), the more common cold variant of autoimmune hemolytic anemia. (medscape.com)
  • Paroxysmal cold hemoglobinuria shares similar antibody thermal activity range as cold hemagglutinin disease (CHD), the more common cold variant of autoimmune hemolytic anemia. (medscape.com)
  • [ 12 ] Furthermore, because the D-L antibody does not necessarily occur with a specific cold exposure event, nor is it recurrent in nature, renaming paroxysmal cold hemoglobinuria as Donath-Landsteiner hemolytic anemia has been proposed. (medscape.com)
  • Win N, Stamps R, Knight R. Paroxysmal cold haemoglobinuria/Donath-Landsteiner test. (medscape.com)
  • Various factors, including the lactate dehydrogenase (LDH) ratio, can predict risk for thromboembolic events (TE) in people with paroxysmal nocturnal hemoglobinuria (PNH), according to results published in Annals of Hematology. (physiciansweekly.com)
  • He is in charge of the reference center for Aplastic Anemia and Nocturnal Paroxysmal Hemoglobinuria (PNH) and the French network on Hematology-immunology rare diseases (MaRIH). (eurobloodnet.eu)
  • Paroxysmal nocturnal hemoglobinuria (PNH) is a clonal hematopoietic stem cell (HSC) disease. (medscape.com)
  • Paroxysmal nocturnal hemoglobinuria or PNH is a rare benign clonal acquired hematopoietic stem-cell (HSC) disorder that results from somatic mutation of the X- linked phosphatidylinositol glycan class A gene known as the PIGA gene. (aacc.org)
  • Paroxysmal nocturnal hemoglobinuria is a clonal disorder caused by an acquired mutation in the PIGA gene in hematopoietic stem cells. (msdmanuals.com)
  • Paroxysmal nocturnal hemoglobinuria is manifests with a chronic hemolytic anemia from uncontrolled complement activation, a propensity for thrombosis and marrow failure. (qxmd.com)
  • Aside from anemia and thrombosis, PNH is also linked with fatigue, dyspnea, abdominal pain, chest pain , hemoglobinuria, renal insufficiency, and bone marrow failure, each of which presents individual risks for patient health and QoL. (hematologyadvisor.com)
  • His research interests include bone marrow transplantation, bone marrow failure and paroxysmal nocturnal hemoglobinuria. (eurobloodnet.eu)
  • Multiple cerebral infarction and microbleeds associated with adult-onset paroxysmal cold hemoglobinuria. (medscape.com)
  • Ultradeep Sequencing Analysis of Paroxysmal Nocturnal Hemoglobinuria Clones Detected by Flow Cytometry: PIG Mutation in Small PNH Clones. (physiciansweekly.com)
  • The flow cytometry analysis of GPI-linked proteins on red blood cells and leukocytes is crucial for paroxysmal nocturnal hemoglobinuria (PNH) diagnostics. (physiciansweekly.com)
  • Once suspected, the diagnosis of paroxysmal nocturnal hemoglobinuria (PNH) is straightforward when flow cytometric analysis of the peripheral blood reveals a population of glycosyl phosphatidylinositol anchor protein-deficient cells. (aamds.org)
  • Taylor CJ, Neilson JR, Chandra D, Ibrahim Z. Recurrent paroxysmal cold haemoglobinuria in a 3-year-old child: a case report. (medscape.com)
  • Although most cases of paroxysmal cold hemoglobinuria occur as an acute event in children younger than 5 years, recurrent episodes have been reported. (medscape.com)
  • Paroxysmal cold hemoglobinuria (PCH) is a form of autoimmune hemolytic anemia (AIHA) that, while rare, is nevertheless one of the most common causes of acute AIHA in young children. (medscape.com)
  • Paroxysmal cold hemoglobinuria (PCH) has the distinction of being the first, albeit rarest, type of autoimmune hemolytic anemia (AIHA) to be identified. (medscape.com)
  • Paroxysmal nocturnal hemoglobinuria: a complement-mediated hemolytic anemia. (qxmd.com)
  • People with PNH have sudden, recurring episodes of symptoms (paroxysmal symptoms), which may be triggered by stresses on the body, such as infections or physical exertion. (medlineplus.gov)
  • There is a close temporal relationship observed between viral or bacterial agents and the development of paroxysmal cold hemoglobinuria within 2-3 weeks of upper respiratory or gastrointestinal symptoms. (medscape.com)
  • Currently, episodes of paroxysmal cold hemoglobinuria usually occur after a viral infection and are abrupt in onset and transitory. (medscape.com)
  • In this study, we examined the usefulness of various markers on blood cell populations in the diagnosis of paroxysmal nocturnal hemoglobinuria (PNH). (elsevierpure.com)
  • Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in the HRF20 (CD59) gene. (lu.se)
  • Inherited complete deficiency of 20-kilodalton homologous restriction factor (CD59) as a cause of paroxysmal nocturnal hemoglobinuria. (lu.se)
  • Anti-complement Treatment for Paroxysmal Nocturnal Hemoglobinuria: Time for Proximal Complement Inhibition? (frontiersin.org)
  • In the latter half of the 19th century, the most common cause of paroxysmal cold hemoglobinuria was congenital or adult tertiary-stage syphilis. (medscape.com)
  • Your doctor may use this test to help diagnose paroxysmal nocturnal hemoglobinuria (PNH) or congenital dyserythropoietic anemia (CDA). (healthline.com)
  • In non-severe aplastic anemia, the presence of a paroxysmal nocturnal hemoglobinuria (PNH) clone was positively associated with survival, while age was negatively associated with survival, according to results published in. (physiciansweekly.com)
  • Paroxysmal nocturnal haemoglobinuria phenotype cells and leucocyte subset telomere length in childhood acquired aplastic anaemia. (bvsalud.org)
  • The significance of paroxysmal nocturnal haemoglobinuria (PNH(pos) ) cells and leucocyte subset telomere lengths in paediatric aplastic anaemia (AA) is unknown. (bvsalud.org)
  • Acute renal failure secondary to paroxysmal cold hemoglobinuria] [Spanish]. (medscape.com)
  • Basel, August 29, 2020 - Novartis today announced new Phase II data for LNP023, an investigational oral treatment for paroxysmal nocturnal hemoglobinuria (PNH), presented at the virtually held 2020 European Society for Blood and Marrow Transplantation (EBMT) Annual Meeting. (novartis.com)
  • Until recently, no pharmaceutical agents were available for the treatment of paroxysmal cold hemoglobinuria. (medscape.com)
  • It is approved for the treatment of paroxysmal nocturnal hemoglobinuria (PNH) in the United States, European Union, and other countries globally. (tmcnet.com)
  • Severe hemoglobinuria is commonly detected during the acute event, resulting in a red-brown discoloration to the urine. (medscape.com)
  • However, unlike cold hemagglutinin disease, in which the IgM-complement interaction results in the cells' removal (via extravascular phagocytosis), paroxysmal cold hemoglobinuria occurs upon completion of complement lysis within the vascular circulation. (medscape.com)
  • Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired (not inherited) disorder that leads to the premature death and impaired production of blood cells. (medlineplus.gov)
  • Paroxysmal cold haemoglobinuria as a tardive complication of idiopathic myelofibrosis. (medscape.com)
  • Paroxysmal nocturnal hemoglobinuria (PNH) happens when your immune system attacks your red blood cells and platelets. (webmd.com)
  • Somatic, inactivating PIGA mutations in haematopoietic stem cells, followed by an unknown autoimmune selection process in favor of the mutated clone, are thought to be important events in the pathogenesis of paroxysmal nocturnal hemoglobinuria (PNH). (annexpublishers.co)
  • In many, but not all cases, hemoglobinuria is most noticeable early in the morning, upon passing urine that has accumulated in the bladder during the night (nocturnal). (medlineplus.gov)
  • Paroxysmal cold haemoglobinuria in an adult with chicken pox. (medscape.com)
  • Wynn RF, Stevens RF, Bolton-Maggs PH, Schwe K, Will AM. Paroxysmal cold haemoglobinuria of childhood: a review of the management and unusual presenting features of six cases. (medscape.com)
  • Unfortunately, due to the transitory nature of paroxysmal cold hemoglobinuria, lack of awareness may lead to a failure in recognizing and diagnosing this uncommon syndrome. (medscape.com)
  • adults and children 1 month of age and older with a disease called Paroxysmal Nocturnal Hemoglobinuria (PNH). (biospace.com)