Lipid rafts determine efficiency of NADPH oxidase activation in neutrophils

被引：116

作者：

Shao, DM ^{[1
]}

Segal, AW ^{[1
]}

Dekker, LV ^{[1
]}

机构：

[1] UCL, Rayne Inst, Dept Med, London WC1E 6JJ, England

来源：

FEBS LETTERS | 2003年 / 550卷 / 1-3期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

raft; NADPH oxidase; neutrophil; protein kinase C; Fc gamma receptor; methyl-beta-cyclodextrin;

D O I：

10.1016/S0014-5793(03)00845-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have investigated the contribution of lipid rafts to activation of the NADPH oxidase enzyme system in neutrophils. Membrane-bound NADPH oxidase subunits are present in the lipid raft compartment of neutrophils. Cytosolic NADPH oxidase components are mainly absent from but are recruited to rafts upon Fcgamma receptor activation. In parallel, protein kinase C isotypes are recruited to the rafts. Kinetic analysis of NADPH oxidase activation revealed that rafts determine the onset but not the maximal rate of enzyme activity. Thus lipid rafts serve to physically juxtapose the NADPH oxidase effector, protein kinase C and Fcgamma receptor, resulting in efficient coupling. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：101 / 106

页数：6

共 16 条

[1] Structure and function of sphingolipid- and cholesterol-rich membrane rafts [J].