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C3b is potent in opsonization: tagging pathogens, immune complexes (antigen-antibody), and apoptotic cells for phagocytosis. Additionally, C3b plays a role in forming a C3 convertase when bound to Factor B (C3bBb complex), or a C5 convertase when bound to C4b and C2b (C4b2b3b complex) or when an additional C3b molecule binds to the C3bBb ...
C4b-binding protein inhibits the haemolytic function of cell-bound C4b. C4b-binding protein and C3b inactivator control the C3 convertase of the classical pathway in a similar way to that described for β1H and C3b inactivator in the alternative pathway. [8] C3b has different binding site for C3bINA, β1H, factor B and properdin.
The C5-convertase of the alternative pathway consists of (C3b) 2 BbP (sometimes referred to as C3b 2 Bb). After the creation of C5 convertase (either as (C3b) 2 BbP or C4b2a3b from the classical pathway), the complement system follows the same path regardless of the means of activation (alternative, classical, or lectin). C5-convertase cleaves ...
The membrane attack complex creates a pore on the target cell's membrane, inducing cell lysis and death. [2] [3] The classical complement pathway can also be activated by apoptotic cells, necrotic cells, and acute phase proteins. [1] [3] [4]
12266 Ensembl ENSG00000125730 ENSMUSG00000024164 UniProt P01024 P01027 RefSeq (mRNA) NM_000064 NM_009778 RefSeq (protein) NP_000055 NP_033908 Location (UCSC) Chr 19: 6.68 – 6.73 Mb Chr 17: 57.51 – 57.54 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Complement component 3, often simply called C3, is a protein of the immune system that is found primarily in the blood. It plays a ...
Cleavage of Arg-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg- bond in complement component C5 alpha-chain to yield C5a and C5b. This enzyme is a bimolecular complex of complement fragment Bb with either C3b or cobra venom factor.
Complement factor I, also known as C3b/C4b inactivator, is a protein that in humans is encoded by the CFI gene. Complement factor I (factor I) is a protein of the complement system , first isolated in 1966 in guinea pig serum , [ 5 ] that regulates complement activation by cleaving cell-bound or fluid phase C3b and C4b. [ 6 ]
Factor H can bind C3b much more easily in the presence of sialic acid, which is a component of most cells in the human body; conversely, in the absence of sialic acid, factor B can bind C3b more easily. This means that if C3b is bound to a "self" cell, the presence of sialic acid and the binding of factor H will prevent the complement cascade ...