Cleavage of the third component of complement (C3) by mannose-binding protein-associated serine protease (MASP) with subsequent complement activation.
We have previously shown that a novel C1s-like serine protease termed MBP-associated serine protease (MASP) is responsible for activation of the complement cascade initiated by mannose-binding protein (MBP). In this communication, we report that MASP is unique in having the proteolytic capacity to cleave C3 with subsequent activation of the alternative pathway, a capacity which C1s lacks.
Matsushita
M
M
Department of Biochemistry, Fukushima Medical College, Japan.
Fujita
T
T
D002352:Carrier Proteins / Q000276:immunology / Q000494:pharmacology*; D003167:Complement Activation / Q000187:drug effects*; D003173:Complement C1s / Q000494:pharmacology; D003176:Complement C3 / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis / Q000187:drug effects; D037102:Lectins / Q000276:immunology*; D008358:Mannose; D037241:Mannose-Binding Lectins; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases / Q000276:immunology / Q000494:pharmacology*
D002352:Carrier Proteins; D003176:Complement C3; D037102:Lectins; D037241:Mannose-Binding Lectins; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases; D003173:Complement C1s; D008358:Mannose