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Arch Biochem Biophys. 1998 Jan 1;349(1):89-94.

Indication of a protein kinase C-independent pathway for NADPH oxidase activation in human neutrophils.

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1
Department of Environmental Biochemistry, Kyoto Pharmaceutical University, Japan.

Abstract

A potent tyrosine phosphatase inhibitor, pervanadate, induced (i) translocation of the cytosolic NADPH oxidase factors, p47-phox and p67-phox, to the plasma membrane; and (ii) O2- production in human neutrophils. However, the translocation of p47-phox and p67-phox was inhibited by H-7, a protein kinase C (PKC) inhibitor without markedly affecting O2- production in whole neutrophils. Results from the plasma membrane fraction showed that NADPH oxidase activity in neutrophils treated with pervanadate did not vary in the presence or absence of H-7, despite a lower content of p47-phox and p67-phox in H-7-treated neutrophils. These findings suggest that in addition to the well-known PKC-dependent pathway, there may exist another PKC-independent pathway to activate NADPH oxidase in human neutrophils. This pathway involves protein tyrosine phosphorylation but does not seem to necessitate translocation of p47-phox and p67-phox to the plasma membrane.

PMID:
9439586
DOI:
10.1006/abbi.1997.0446
[Indexed for MEDLINE]
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