MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway
MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway
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DOI：
10.1016/s1074-7613(01)00161-3
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发表时间：
2001-07-01
期刊：
影响因子：
32.4
通讯作者：
Jensenius, JC
中科院分区：
文献类型：
--
作者：
Dahl, MR;Thiel, S;Jensenius, JC
甘露聚糖结合凝集素（MBL）途径的补体激活是先天免疫防御的一部分。MBL与微生物碳水化合物结合激活MBL相关丝氨酸蛋白酶（MASPs）， MASPs招募补体因子C4和C2，产生C3转化酶或直接激活C3。我们提出了MBL复合体的一个系统发育高度保守的成员，MASP-3，它是通过对MASP-1/3基因的选择性剪接产生的。将MASP-3命名为蛋白酶是基于与已知的masp的同源性。发现不同的MBL低聚物具有不同的MASP组成和生物活性。MASP-1、MAp19和直接切割c3的活性与较小的低聚物有关，而MASP-3与MASP-2一起出现在较大的低聚物上。MASP-3下调了MASP-2的C4和C2切割活性。
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.