凝集素途径
蛋白酵素
生物
丝氨酸
MASP1公司
补体成分2
C型凝集素
无花果素
川地69
凝集素
生物化学
甘露聚糖结合凝集素
补体系统
基因
分子生物学
替代补体途径
丝氨酸蛋白酶
遗传学
酶
蛋白酶
抗体
细胞毒性T细胞
体外
白细胞介素2受体
作者
Cordula Stover,Nicholas J. Lynch,Mads Ronald Dahl,Steven Hanson,Minoru Takahashi,Marion Frankenberger,Löms Ziegler-Heitbrock,Ian C. Eperon,Steffen Thiel,Wilhelm Schwaeble
标识
DOI:10.1038/sj.gene.6363970
摘要
Activation of the lectin pathway of complement is initiated by the binding to microbial carbohydrate structures of a multimolecular fluid-phase complex composed of a carbohydrate recognition subcomponent that associates with three specific serine proteases and an enzymatically inert protein of 19 kDa. The first carbohydrate recognition subcomponent of the lectin pathway identified was mannan-binding lectin (MBL), hence the serine proteases were named MBL-associated serine proteases (MASPs) and numbered according to the sequence of their discovery. Here we describe the primary structures of the two distinct serine proteases MASP-1 and MASP-3 in the rat (and of MASP-3 in the mouse), show their association with plasma MBL complexes, and demonstrate that in rat and mouse, as in man, MASP-1 and MASP-3 are encoded by a single structural gene. For both species, we present the genomic region and regulatory elements responsible for the processing of either MASP-1 or MASP-3 mRNA by alternative splicing/alternative polyadenylation. Furthermore, we demonstrate the evolutionary conservation of MASP-3 mRNA in cDNA transcripts from guinea pig, rabbit, pufferfish, and cow.
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