金黄色葡萄球菌丝氨酸蛋白酶修饰的人血浆α-1-蛋白酶抑制剂的趋化活性
Chemoattractant activity of Staphylococcus aureus serine proteinase modified human plasma alpha-1-proteinase inhibitor.
作者信息
Baran K, Górka M, Potempa J, Porwit-Bóbr Z
机构信息
Department of Microbiology and Immunology, Jan Zurzycki Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.
出版信息
Antonie Van Leeuwenhoek. 1989 Nov;56(4):361-5. doi: 10.1007/BF00443750.
S. aureus serine proteinase inactivates human alpha-1-proteinase inhibitor (alpha-1-PI) by attacking a single peptide bond between Glu354 and Ala355 giving a modified inhibitor which is a tight complex of Mr = 4,000 and 48,000 fragments. In the present paper we show that this proteolytically inactivated alpha-1-PI is a potent chemotactic factor for human neutrophiles at a nanomolar concentration, and we discuss its potential involvement in the inflammatory reaction due to S. aureus infections.
金黄色葡萄球菌丝氨酸蛋白酶通过攻击Glu354和Ala355之间的单个肽键来使人类α-1-蛋白酶抑制剂（α-1-PI）失活，产生一种修饰后的抑制剂，它是分子量为4000和48000片段的紧密复合物。在本文中，我们表明这种经蛋白水解失活的α-1-PI在纳摩尔浓度下是人类嗜中性粒细胞的一种强效趋化因子，并且我们讨论了它在金黄色葡萄球菌感染引起的炎症反应中的潜在作用。
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