Paramyosin inhibits complement C1.
Paramyosin inhibits complement C1.
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DOI：
10.4049/jimmunol.148.1.124
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发表时间：
1992-01
影响因子：
4.4
通讯作者：
J. Laclette;Charles B. Shoemaker;D. Richter;L. Arcos;Nelly Panté;C. Cohen;D. Bing;A. Nicholson‐Weller
中科院分区：
文献类型：
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作者：
J. Laclette;Charles B. Shoemaker;D. Richter;L. Arcos;Nelly Panté;C. Cohen;D. Bing;A. Nicholson‐Weller
我们在这里报告的研究结果表明，抑制C是几种无脊椎动物副肌球蛋白的属性。来自猪带绦虫、曼氏血吸虫和贻贝的副肌球蛋白结合聚合胶原，并且可以通过胶原亲和性从组织的粗提取物中分离。无论C1是分离的还是存在于C2缺乏的血清中，这些副肌球蛋白都会抑制C1的功能。因为T.副肌球蛋白是最好的抑制剂，我们集中在这个分子的进一步研究。T. solium paramyosin在溶液中以类似于C1 r2 S2的剂量/反应结合纯化的C1 q。C1-副肌球蛋白相互作用的进一步研究表明：1）C4未被激活，2）C4 b2 a衰变未受影响，3）对EDTA螯合豚鼠血清中提供的C3-9裂解SRBC的效率无影响。因此，副肌球蛋白抑制作用是针对经典途径的起始。结果表明，副肌球蛋白的蠕虫寄生虫可能有一个调节器的主机免疫反应，通过C抑制在C1的作用。
We report here the results of studies showing that inhibition of C is a property of several invertebrate paramyosins. Paramyosins from Taenia solium, Schistosoma mansoni, and the mussel Mytilus edulis bind polymeric collagen and can be isolated from crude extracts of tissues by collagen affinity. These paramyosins inhibit C1 function whether the C1 is isolated or present in C2-deficient serum. Because T. solium paramyosin was the best inhibitor, we concentrated further studies on this molecule. T. solium paramyosin binds purified C1q in solution with a dose/response similar to C1r2S2. Further studies of the C1-paramyosin interaction indicate that: 1) C4 is not activated, 2) C4b2a decay is not affected, and 3) there is no effect on the efficiency of C3-9, as provided in EDTA-chelated guinea pig serum, in lysing SRBC. Thus, paramyosin inhibition is directed at the initiation of the classical pathway. The results suggest that paramyosins of helminthic parasites may have a role as modulators of the host immune response through C inhibition at C1.