4.5 Article

Lipid rafts determine efficiency of NADPH oxidase activation in neutrophils

Journal

FEBS LETTERS
Volume 550, Issue 1-3, Pages 101-106

Publisher

WILEY
DOI: 10.1016/S0014-5793(03)00845-7

Keywords

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

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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.

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