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-C1r 2s 2 complex (C1), which has bee...

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Bibliographic Details
Published in:Molecular immunology 1999-09, Vol.36 (13), p.853-861
Main Authors: Wong, N.K.H, Kojima, M, Dobó, J, Ambrus, G, Sim, R.B
Format: Article
Language:English
Subjects:
Animals
C1-inhibitor
Complement
Complement Activation - physiology
Complement C1 Inactivator Proteins - metabolism
Complement C1q - metabolism
Complement C1r - metabolism
complement component C1
Humans
mannose-binding lectin
Mannose-Binding Protein-Associated Serine Proteases
MASPs
MBL
Serine Endopeptidases - chemistry
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
serine proteinase
Serine Proteinase Inhibitors - metabolism
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Summary: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-C1r 2s 2 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.
ISSN:0161-5890
1872-9142
DOI:10.1016/S0161-5890(99)00106-6