凝集素途径
补体系统
生物
替代补体途径
丝氨酸蛋白酶
甘露聚糖结合凝集素
分子生物学
RNA剪接
基因
补体成分2
凝集素
细胞生物学
生物化学
遗传学
蛋白酶
抗体
酶
核糖核酸
作者
Cordula M. Stover,Steffen Thiel,Nicholas J. Lynch,Wilhelm Schwaeble
出处
期刊:Journal of Immunology
[The American Association of Immunologists]
日期:1999-12-15
卷期号:163 (12): 6848-6859
被引量:23
标识
DOI:10.4049/jimmunol.163.12.6848
摘要
Recently, we described two novel constituents of the multimolecular initiation complex of the mannan-binding lectin (MBL) pathway of complement activation, a serine protease of 76 kDa, termed MASP-2, and a MASP-2 related plasma protein of 19 kDa, termed MAp19. Upon activation of the MBL/MASPs/MAp19 complex, MASP-2 cleaves the fourth complement component C4, while the role of MAp19 within the MBL/MASP-1/MASP-2/MAp19 complex remains to be clarified. In humans, the mRNA species encoding MASP-2 (2.6 kb) and MAp19 (1.0 kb) arise by an alternative polyadenylation/splicing mechanism from a single structural MASP-2 gene. Here, we report the complete primary structures of the rat homologue of MASP-2 and of rat and mouse MAp19. We show that both MASP-2 and MAp19 are part of the rat MBL pathway activation complex and demonstrate their exclusively hepatic biosynthesis. Southern blot and PCR analyses of rat genomic DNA indicate that as in humans, rat MASP-2 and MAp19 are encoded by a single structural gene.
科研通智能强力驱动
Strongly Powered by AbleSci AI