MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway

Citation
Mr. Dahl et al., MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway, IMMUNITY, 15(1), 2001, pp. 127-135
Citations number
41
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Immunology
Journal title
IMMUNITY
ISSN journal
1074-7613 → ACNP
Volume
15
Issue
1
Year of publication
2001
Pages
127 - 135
Database
ISI
SICI code
1074-7613(200107)15:1<127:MAIAWD>2.0.ZU;2-E
Abstract
The mannan-binding lectin (MBL) pathway of complement activation is part of the innate immune defense. The binding of MBL to microbial carbohydrates a ctivates the MBL-associated serine proteases (MASPs) which recruit the comp lement factors, C4 and C2, to generate the C3 convertase or directly activa te C3. We present a phylogenetically highly conserved member of the MBL com plex, MASP-3, which is generated through alternative splicing of the MASP-1 /3 gene. The designation of MASP-3 as a protease is based on homology to kn own MASPs. Different MBL oligomers were found to have distinct MASP composi tion and biological activities. MASP-1, MAp19, and direct C3-cleaving activ ity are associated with smaller oligomers whereas MASP-3 is found together with MASP-2 on larger oligomers. MASP-3 downregulate the C4 and C2 cleaving activity of MASP-2.