Inhibition of classical C5 convertase in the complement system by factor H.
This paper described the influence of factor H on the haemolytic activity of the classical C5 convertase. Factor H showed little effect on the interaction of C5 with EAC1,4b,2a,3b cells bearing low numbers of C3b sites, but displayed the inhibitory effect on the interaction of C5 with the intermediate cells bearing high numbers of C3b sites. The higher the number of C3b sites on the cells, the greater the degree of the inhibition by factor H. The inhibition by factor H was accompanied by the inhibition of consumption of C5 from the fluid phase, indicating that factor H inhibits the activity of C5 convertase, not the binding of activated C5 to the cells.
D000818:Animals; D003166:Complement Activating Enzymes / Q000037:antagonists & inhibitors*; D003167:Complement Activation; D050577:Complement C3-C5 Convertases; D003179:Complement C3b / Q000032:analysis / Q000276:immunology; D003180:Complement C3b Inactivator Proteins / Q000494:pharmacology*; D003182:Complement C5 / Q000276:immunology; D017242:Complement Factor H; D003171:Complement Pathway, Classical; D006168:Guinea Pigs; D006461:Hemolysis; D006801:Humans
C493495:CFH protein, human; D003180:Complement C3b Inactivator Proteins; D003182:Complement C5; D003179:Complement C3b; D017242:Complement Factor H; D003166:Complement Activating Enzymes; D050577:Complement C3-C5 Convertases