Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors.
There has been rapid progress in determining the mechanism by which complement is activated by the complex formed between Mannose-Binding Lectin and its associated proteases (MASPs). MBL and the MASPs are of low abundance, but are similar to the more abundant C1q-C1r2s2 complex (C1), which has been extensively investigated. In this review we summarise recent findings on MBL-MASPs' structure. enzymic activity and regulation, and compare MBL-MASPs with C1.
Wong
N K
NK
Department of Biochemistry, University of Oxford, UK.
Kojima
M
M
Dobó
J
J
Ambrus
G
G
Sim
R B
RB
D000818:Animals; D003167:Complement Activation / Q000502:physiology; D003174:Complement C1 Inactivator Proteins / Q000378:metabolism; D015922:Complement C1q / Q000378:metabolism; D015923:Complement C1r / Q000378:metabolism; D006801:Humans; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000378:metabolism
D003174:Complement C1 Inactivator Proteins; D015842:Serine Proteinase Inhibitors; D015922:Complement C1q; C105296:MASP2 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases; D015923:Complement C1r