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产生超氧化物的NADPH氧化酶激活的分子机制。

Molecular mechanism for activation of superoxide-producing NADPH oxidases.

作者信息

Takeya Ryu, Sumimoto Hideki

机构信息

Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.

出版信息

Mol Cells. 2003 Dec 31;16(3):271-7.

PMID:14744014
Abstract

The membrane-integrated protein gp91phox, existing as a heterodimer with p22phox, functions as the catalytic core of the phagocyte NADPH oxidase, which plays a crucial role in host defence. The oxidase, dormant in resting cells, becomes activated to produce superoxide, a precursor of microbicidal oxidants, by interacting with the adaptor proteins p47phox and p67phox as well as the small GTPase Rac. In the past few years, several proteins homologous to gp91phox were discovered as superoxide-producing NAD(P)H oxidases (Nox's) in non-phagocytic cells; however, regulatory mechanisms for the novel oxidases have been largely unknown. Current identification of proteins highly related to p47phox and p67phox, designated Noxol (Nox organizer 1) and Noxal (Nox activator 1), respectively, has shed lights on common and distinct mechanisms underlying activations of Nox family oxidases.

摘要

膜整合蛋白gp91phox与p22phox形成异源二聚体,作为吞噬细胞NADPH氧化酶的催化核心,在宿主防御中起关键作用。该氧化酶在静息细胞中处于休眠状态,通过与衔接蛋白p47phox和p67phox以及小GTP酶Rac相互作用而被激活,产生超氧化物,这是一种杀菌性氧化剂的前体。在过去几年中,几种与gp91phox同源的蛋白被发现是非吞噬细胞中产生超氧化物的NAD(P)H氧化酶(Nox);然而,新型氧化酶的调节机制在很大程度上仍不清楚。目前分别鉴定出与p47phox和p67phox高度相关的蛋白,即Noxol(Nox组织者1)和Noxal(Nox激活剂1),这为Nox家族氧化酶激活的共同和不同机制提供了线索。

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