Biochemistry of C3 and related thiolester proteins in infection and inflammation.
Biochemistry of C3 and related thiolester proteins in infection and inflammation.
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DOI：
10.1093/clinids/9.1.97
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
M. Hostetter;D. L. Gordon
中科院分区：
文献类型：
--
作者：
M. Hostetter;D. L. Gordon
人类补体第三组分中活性硫酯键的表征导致了许多蛋白质中同源位点的鉴定。除了C3硫酯参与微生物表面组分的顺声酰化外，新的证据表明，生理性亲核试剂（如氨）对硫酯的破坏是肺、肾和内皮表面局部炎症的有效介质。对这些相关蛋白质中硫酯键的操纵应该使我们能够理解并最终指导炎症的分子机制。
The characterization of the reactive thiolester bond in the third component of human complement has led to the identification of homologous sites in a number of proteins. In addition to the participation of the C3 thiolester in the opsonic acylation of surface components of microorganisms, new evidence is emerging to implicate thiolester disruption by physiologic nucleophiles, such as ammonia, as a potent mediator of local inflammation in the lung, the kidney, and at endothelial surfaces. Manipulation of the thiolester bonds in these related proteins should permit us to understand, and ultimately to direct, the molecular mechanisms of inflammation.