Osmomechanical stress selectively regulates translocation of protein kinase C isoforms |
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| Authors: | Liu X Zhang M I N Peterson L B O'Neil R G |
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| Affiliation: | Department of Integrative Biology and Pharmacology, The University of Texas Health Science Center, 6431 Fannin Street, Houston, TX 77030, USA. |
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| Abstract: | 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 Fcγ 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 Fcγ receptor, resulting in efficient coupling. |
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| Keywords: | Raft NADPH oxidase Neutrophil Protein kinase C Fcγ receptor Methyl-β-cyclodextrin |
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