| First Author | Dahl MR | Year | 2001 |
| Journal | Immunity | Volume | 15 |
| Issue | 1 | Pages | 127-35 |
| PubMed ID | 11485744 | Mgi Jnum | J:70596 |
| Mgi Id | MGI:2137823 | Doi | 10.1016/s1074-7613(01)00161-3 |
| Citation | Dahl MR, et al. (2001) Masp-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway. Immunity 15(1):127-35 |
| abstractText | The mannan-binding lectin (MBL) pathway of complement activation is part of the innate immune defense. The binding of MBL to microbial carbohydrates activates the MBL-associated serine proteases (MASPs), which recruit the complement factors, C4 and C2, to generate the C3 convertase or directly activate C3. We present a phylogenetically highly conserved member of the MBL complex, 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 known MASPs. Different MBL oligomers were found to have distinct MASP composition and biological activities. MASP-1, MAp19, and direct C3-cleaving activity 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. |
