Antibacterial activity of antileukoprotease
Antibacterial activity of antileukoprotease
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DOI：
10.1128/iai.64.11.4520-4524.1996
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发表时间：
1996-11-01
影响因子：
3.1
通讯作者：
Dijkman, JH
中科院分区：
文献类型：
--
作者：
Hiemstra, PS;Maassen, RJ;Dijkman, JH
抗白细胞蛋白酶（ALP），或分泌性白细胞蛋白酶抑制剂，是一种丝氨酸蛋白酶的内源性抑制剂，存在于各种外部分泌物中。ALP是存在于人肺中的丝氨酸蛋白酶的主要抑制剂之一，是弹性蛋白酶的有效可逆抑制剂，并且在较小程度上是组织蛋白酶G的有效可逆抑制剂。在马嗜中性粒细胞中，已经鉴定出具有ALP的一些特征的抗微生物多肽（M. A. Couto，S. S. L. Harwig，J. S. Cullor，J. P. Hughes，and R. I.莱勒感染Immun. 60：5042-5047，1992）。这份报告，连同碱性磷酸酶的阳离子性质，导致我们调查的抗菌活性的碱性磷酸酶。ALP显示出对大肠杆菌和金黄色葡萄球菌的显着体外抗菌活性。在摩尔基础上，ALP的活性低于其他两种阳离子抗菌多肽，溶菌酶和防御素。ALP包含两个同源结构域：已知其蛋白酶抑制活性位于第二个COOH-末端结构域，而其第一个NH 2-末端结构域的功能在很大程度上未知。将完整的ALP或其分离的第一结构域与E. coli或S.金黄色葡萄球菌导致这些细菌被杀死，而其第二结构域显示出非常少的抗菌活性。总之，这些数据表明ALP的第一结构域的推定的抗菌作用，并表明其抗菌活性可能装备ALP，以有助于宿主防御感染。
Antileukoprotease (ALP), or secretory leukocyte proteinase inhibitor, is an endogenous inhibitor of serine proteinases that is present in various external secretions. ALP, one of the major inhibitors of serine proteinases present in the human lung, is a potent reversible inhibitor of elastase and, to a lesser extent, of cathespin G. In equine neutrophils, an antimicrobial polypeptide that has some of the characteristics of ALP has been identified (M. A. Couto, S. S. L. Harwig, J. S. Cullor, J. P. Hughes, and R. I. Lehrer, Infect. Immun. 60:5042-5047, 1992). This report, together with the cationic nature of ALP, led us to investigate the antimicrobial activity of ALP. ALP was shown to display marked in vitro antibacterial activity against Escherichia coli and Staphylococcus aureus. On a molar basis, the activity of ALP was lower than that of two other cationic antimicrobial polypeptides, lysozyme and defensin. ALP comprises two homologous domains: its proteinase-inhibitory activities are known to be located in the second COOH-terminal domain, and the function of its first NH2-terminal domain is largely unknown. Incubation of intact ALP or its isolated first domain with E. coli or S. aureus resulted in killing of these bacteria, whereas its second domain displayed very little antibacterial activity. Together these data suggest a putative antimicrobial role for the first domain of ALP and indicate that its antimicrobial activity may equip ALP to contribute to host defense against infection.