作者: Misao Matsushita , Mikio Kuraya , Naotaka Hamasaki , Mitsushi Tsujimura , Hiroshi Shiraki
DOI: 10.4049/JIMMUNOL.168.7.3502
关键词:
摘要: Ficolins are a group of proteins which consist collagen-like domain and fibrinogen-like domain. In human serum, there two types ficolins named L-ficolin/P35 H-ficolin (Hakata Ag), both have lectin activity. We recently demonstrated that is associated with mannose-binding (MBL)-associated serine proteases (MASP) 1 2 small MBL-associated protein (sMAP), the complex activates pathway. this study, we report characterization in terms its ability to activate complement. Western blotting analysis showed presence MASP-1, MASP-2, MASP-3, sMAP preparations isolated from Cohn Fraction III. The MASPs had proteolytic activities against C4, C2, C3 fluid phase. When were bound anti-H-ficolin Ab been coated on ELISA plates, they activated although no C4 activation was noted when anti-MBL anti-L-ficolin/P35 used. binds PSA, polysaccharide produced by Aerococcus viridans. PSA plates. These results indicate second ficolin sMAP,