Wortmannin and 1-butanol block activation of a novel family of protein kinases in neutrophils.

Abstract:

:Neutrophils contain four uncharacterized protein kinases with molecular masses of ca. 69, 63, 49 and 40 kDa that are rapidly activated upon stimulation of these cells with the chemoattractant fMet-Leu-Phe [Ding, J. and Badwey, J.A. (1993) J. Biol. Chem. 268, 17326-17333]. We now report that wortmannin and 1-butanol block activation of all four of these kinases. These reagents are known to inhibit superoxide generation in neutrophils stimulated with this agonist. Wortmannin inhibits phosphatidylinositol 3-kinase and blocks activation of phospholipase D, whereas 1-butanol can reduce the generation of phosphatidate in cells by serving as a substrate for phospholipase D. These data suggest that phosphatidylinositol 3-kinase and phospholipase D may be involved in the activation of several novel protein kinases in neutrophils and that one or more of these kinases is/are involved in superoxide release.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ding J,Badwey JA

doi

10.1016/0014-5793(94)00593-1

subject

Has Abstract

pub_date

1994-07-11 00:00:00

pages

149-52

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00593-1

journal_volume

348

pub_type

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