人α1-蛋白酶抑制剂与人类白细胞弹性蛋白酶的抑制复合物是一种中性粒细胞趋化因子。
The inhibitory complex of human alpha 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant.
作者信息
Banda M J, Rice A G, Griffin G L, Senior R M
机构信息
Laboratory of Radiobiology and Environmental Health, University of California, San Francisco 94143.
出版信息
J Exp Med. 1988 May 1;167(5):1608-15. doi: 10.1084/jem.167.5.1608.
An inhibitor-proteinase complex consisting of human alpha 1-PI and human leukocyte elastase is chemotactic for human neutrophils. The chemotactic activity is optimal at 1 nM and is associated only with the alpha 1-PI portion of the complex. Neither HLE in the complex, free HLE, nor native alpha 1-PI possesses chemotactic activity for human neutrophils. alpha 1-PI in complex is hydrolyzed at the Met-358-Ser-359 bond. The chemotactic activity is associated with the Mr 4,200 fragment of alpha 1-PI that has Ser-359 as its NH2 terminus. The region of the HLE-alpha 1-PI complex that stimulates chemotaxis appears to be the same as that of the Mr 4,200 fragment generated by hydrolysis of the Pro-357-Met-358 bond during proteolytic inactivation of alpha 1-PI. The data suggest the presence of a neutrophil surface receptor bound by alpha 1-PI after the formation of a complex with HLE or after proteolytic degradation. This receptor may play a role in clearance of these modified alpha 1-PI molecules.
由人α1 - 抗胰蛋白酶（α1 - PI）和人白细胞弹性蛋白酶组成的抑制剂 - 蛋白酶复合物对人中性粒细胞具有趋化作用。趋化活性在1 nM时最佳，且仅与复合物的α1 - PI部分相关。复合物中的人白细胞弹性蛋白酶（HLE）、游离的HLE以及天然的α1 - PI对人中性粒细胞均不具有趋化活性。复合物中的α1 - PI在甲硫氨酸358 - 丝氨酸359键处被水解。趋化活性与以丝氨酸359为氨基末端的α1 - PI的4200道尔顿片段相关。HLE - α1 - PI复合物中刺激趋化作用的区域似乎与α1 - PI在蛋白水解失活过程中因脯氨酸357 - 甲硫氨酸358键水解产生的4200道尔顿片段的区域相同。数据表明在与HLE形成复合物后或蛋白水解降解后，存在一种与α1 - PI结合的中性粒细胞表面受体。该受体可能在清除这些修饰的α1 - PI分子中发挥作用。
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