Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene

被引：0
作者：
Stover, CM
Thiel, S
Thelen, M
Lynch, NJ
Vorup-Jensen, T
Jensenius, JC
Schwaeble, WJ
机构：
[1] Univ Leicester, Dept Microbiol & Immunol, Leicester LE1 9HN, Leics, England
[2] Univ Aarhus, Dept Med Microbiol & Immunol, Aarhus, Denmark
[3] Univ Bern, Theodor Kocher Inst, Bern, Switzerland
[4] Univ Marburg, Inst Anat & Cell Biol, Marburg, Germany
来源：
JOURNAL OF IMMUNOLOGY | 1999年 / 162卷 / 06期
基金：
英国惠康基金;
关键词：
D O I：
暂无
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MEL-associated serine proteases, MASP-1 and MASP-2, This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses, MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s, Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2, protein is consistently detected as part of the MBL/MASP complex, In this study, we present the primary structure of this novel MEL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
引用
收藏
页码：3481 / 3490
页数：10
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