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

N. K H Wong, M. Kojima, J. Dobó, G. Ambrus, R. B. Sim

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

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 Clq-Clr(2S2) complex (Cl), 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 Cl. (C) 1999 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)853-861
Number of pages9
JournalMolecular Immunology
Volume36
Issue number13-14
DOIs
Publication statusPublished - Sep 1999

Fingerprint

Mannose-Binding Protein-Associated Serine Proteases
Mannose-Binding Lectin
Peptide Hydrolases

Keywords

  • Cl
  • Cl-inhibitor
  • Complement
  • MASPs
  • MBL

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors. / Wong, N. K H; Kojima, M.; Dobó, J.; Ambrus, G.; Sim, R. B.

In: Molecular Immunology, Vol. 36, No. 13-14, 09.1999, p. 853-861.

Research output: Contribution to journalArticle

Wong, N. K H ; Kojima, M. ; Dobó, J. ; Ambrus, G. ; Sim, R. B. / Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors. In: Molecular Immunology. 1999 ; Vol. 36, No. 13-14. pp. 853-861.
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