Complement C2 Receptor Inhibitor Trispanning: A Novel Human Complement Inhibitory Receptor
نویسندگان
چکیده
منابع مشابه
Complement C2 receptor inhibitor trispanning: a novel human complement inhibitory receptor.
The complement system presents a powerful defense against infection and is tightly regulated to prevent damage to self by functionally equivalent soluble and membrane regulators. We describe complement C2 receptor inhibitor trispanning (CRIT), a novel human complement regulatory receptor, expressed on hemopoietic cells and a wide range of tissues throughout the body. CRIT is present in human pa...
متن کاملComplement C2 receptor inhibitor trispanning and the beta-chain of C4 share a binding site for complement C2.
Complement C2 receptor inhibitor trispanning (CRIT) of the Schistosoma parasite binds human C2 via the C2a segment. The receptor in vivo functions as C2 decoy receptor by directly competing with C4b for binding to C2. As a result, CRIT is able to limit the extent of classical pathway (CP) C3 convertase formation. We report that the CRIT-extracellular domain 1 (ed1) peptide inhibits CP-mediated ...
متن کاملComplement C2 receptor inhibitor trispanning confers an increased ability to resist complement-mediated lysis in Trypanosoma cruzi.
The ability to resist complement differs between the Y and Colombiana Trypanosoma cruzi strains. We found that the Y strain of T. cruzi was more able to resist the classical and lectin pathways of complement activation than the Colombiana strain. The complement C2 receptor inhibitor trispanning gene (CRIT) is highly conserved in both strains. At the protein level, CRIT is expressed only in stat...
متن کاملComplement receptor is an inhibitor of the complement cascade
A glycoprotein from the membrane of human erythrocytes has been identified as a receptor for C3b (CR1). It promotes the dissociation of the alternative pathway C3 convertase C3b,Bb and the cleavage of C3b by C3b/C4b inactivator. We find that CR1 also inactivates the C3 and C5 convertases of the classical pathway. CR1 inhibits the consumption of C3 by C3 convertase EAC142 and enhances the decay ...
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ژورنال
عنوان ژورنال: The Journal of Immunology
سال: 2004
ISSN: 0022-1767,1550-6606
DOI: 10.4049/jimmunol.174.1.356