Binding of C3 molecules to membranes via the SH-residue generated by the cleavage of a thioester bond can initiate complement activation.
Dithiopyridine (DTP)-dipalmitoylphosphatidylethanolamine (DTP-DPPE) was incorporated into liposome membranes to prepare DTP-liposomes. The DTP-liposomes could be lysed by reaction with the alternative complement pathway of any kind of serum tested. Activation of the alternative complement pathway has been shown to be mediated by the binding of C3 molecules to DTP on the liposomes via the SH-residue generated by the cleavage of thioester bond in the alpha-chain of the molecules.
Okada
N
N
Department of Microbiology, Fukuoka University School of Medicine, Japan.
Yasuda
T
T
Okada
H
H
D000818:Animals; D002784:Cholesterol; D003167:Complement Activation; D003176:Complement C3 / Q000378:metabolism*; D003170:Complement Pathway, Alternative; D004134:Dimyristoylphosphatidylcholine; D006168:Guinea Pigs; D006801:Humans; D008081:Liposomes; D008252:Macaca fascicularis; D051379:Mice; D008807:Mice, Inbred BALB C; D010714:Phosphatidylethanolamines; D011485:Protein Binding; D011725:Pyridines; D051381:Rats; D011919:Rats, Inbred Strains; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents
D003176:Complement C3; D008081:Liposomes; D010714:Phosphatidylethanolamines; D011725:Pyridines; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; C007510:1,2-dipalmitoyl-3-phosphatidylethanolamine; D002784:Cholesterol; D004134:Dimyristoylphosphatidylcholine