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人类多形核白细胞流感蛋白激活的NADPH氧化酶中超氧阴离子的产生。

Superoxide anion production in influenza protein-activated NADPH oxidase of human polymorphonuclear leukocytes.

作者信息

Arora D J, Henrichon M

机构信息

Virology Research Center, Institut Armand Frappier, Université du Québec, Laval, Canada.

出版信息

J Infect Dis. 1994 May;169(5):1129-33. doi: 10.1093/infdis/169.5.1129.

DOI:10.1093/infdis/169.5.1129
PMID:8169407
Abstract

There are conflicting reports regarding superoxide anion (O2-) production by human polymorphonuclear leukocytes (PMNL) that have been activated by influenza virus. In the present study, the output of O2- was determined by measuring superoxide dismutase-inhibitable cytochrome c reduction. Incubation of PMNL with purified influenza matrix (M) protein, neuraminidase (NA), or hemagglutinin (HA) enhanced the production of O2-: 4.93 nmol of O2-/4 x 10(5) cells/15 min was produced with M protein, 5.20 with NA, and 6.89 with HA. These values were significantly higher (P < .05) than that for untreated PMNL (1.51). Both nonglycosylated and glycosylated proteins had the potential to generate O2- in human PMNL. Neither the hemagglutinating activity of HA nor the enzymatic activity of NA were necessary for viral protein activation of PMNL.

摘要

关于流感病毒激活的人多形核白细胞(PMNL)产生超氧阴离子(O2-),有相互矛盾的报道。在本研究中,通过测量超氧化物歧化酶抑制的细胞色素c还原作用来确定O2-的产量。用纯化的流感病毒基质(M)蛋白、神经氨酸酶(NA)或血凝素(HA)孵育PMNL可增强O2-的产生:M蛋白产生4.93 nmol O2-/4×10(5)个细胞/15分钟,NA产生5.20,HA产生6.89。这些值显著高于未处理的PMNL(1.51)(P<0.05)。非糖基化和糖基化蛋白都有在人PMNL中产生O2-的潜力。HA的血凝活性和NA的酶活性对于PMNL的病毒蛋白激活都不是必需的。

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