Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors

Authors
Wong, NKH Kojima, M Dobo, J Ambrus, G Sim, RB
Citation
Nkh. Wong et al., Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors, MOL IMMUNOL, 36(13-14), 1999, pp. 853-861
Citations number
67
Categorie Soggetti
Immunology
Journal title
MOLECULAR IMMUNOLOGY
ISSN journal
01615890 → ACNP
Volume
36
Issue
13-14
Year of publication
1999
Pages
853 - 861
Database
ISI
SICI code
0161-5890(199909/10)36:13-14<853:AOTMSP>2.0.ZU;2-M
Abstract
There has been rapid progress in determining the mechanism by which complem ent is activated by the complex formed between Mannose-Binding Lectin and i ts associated proteases (MASPs). MBL and the MASPs are of low abundance, bu t are similar to the more abundant Clq-Clr(2)s(2) complex (Cl), which has b een extensively investigated. In this review we summarise recent findings o n MBL-MASPs' structure, enzymic activity and regulation, and compare MBL-MA SPs with Cl. (C) 1999 Elsevier Science Ltd. All rights reserved.