In vitro inhibition of the classical pathway of human complement by a natural microbial product, colistin sulphate.
Colistin sulphate was found to be an inhibitor of the classical pathway of the complement system. The main sites of inhibition were the interaction of EAC14 with C2 and EAC142 with C3. It also inhibited EAC14 formation from EA and C2-deficient serum, EAC1-7 formation from EAC1-3, C5, C6 and C7 and the interaction of EAC1-7 with C8 and C9, though less efficiently. It did not inhibit formation of C3/C5 convertase of the alternative pathway. The inhibition of the classical pathway was reversible since hemolytic activity was completely restored after dialysis.
D000818:Animals; D003091:Colistin / Q000494:pharmacology*; D003166:Complement Activating Enzymes / Q000096:biosynthesis; D003167:Complement Activation / Q000187:drug effects*; D003176:Complement C3 / Q000378:metabolism; D050577:Complement C3-C5 Convertases; D003170:Complement Pathway, Alternative / Q000187:drug effects; D003171:Complement Pathway, Classical / Q000187:drug effects*; D006168:Guinea Pigs; D006461:Hemolysis; D006801:Humans; D066298:In Vitro Techniques; D011817:Rabbits; D012756:Sheep
D003176:Complement C3; D003166:Complement Activating Enzymes; D050577:Complement C3-C5 Convertases; D003091:Colistin