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(Received for publication, June 20, 1996, and in revised form, August 13, 1996)
From Lilly Research Laboratories, Indianapolis, Indiana 46285 and
§ University of Oxford,
Oxford OX1 3QT, United Kingdom
The Ca2+-sensitive 85-kDa cytosolic
phospholipase A2 (cPLA2) is responsible for
thrombin-stimulated mobilization of arachidonic acid for the synthesis
of thromboxane A2 in human platelets. We have previously
shown that thrombin activates p38 kinase, a recently discovered new
member of the mitogen-activated protein kinase family (Kramer, R. M.,
Roberts, E. F., Strifler, B. A., and Johnstone, E. M. (1995)
J. Biol. Chem. 270, 27395-27398) and also induces
phosphorylation of cPLA2, thereby increasing its intrinsic
catalytic activity. In the present study we have examined the role of
p38 kinase in the phosphorylation and activation of cPLA2
in stimulated platelets. We have observed that activation of p38 kinase
accompanies receptor-mediated events in platelets and coincides with
cPLA2 phosphorylation. Furthermore, in the presence of
inhibitors of p38 kinase, the proline-directed phosphorylation of
cPLA2 was completely blocked in platelets stimulated with
the thrombin receptor agonist peptide SFLLRN and was suppressed during
the early (up to 2 min) phase of platelet stimulation caused by
thrombin. Unexpectedly, we found that prevention of proline-directed
phosphorylation of cPLA2 in stimulated platelets did not
attenuate its ability to release arachidonic acid from platelet
phospholipids. We conclude that: 1) cPLA2 is a
physiological target of p38 kinase; 2) p38 kinase is involved in the
early phosphorylation of cPLA2 in stimulated platelets; and
3) proline-directed phosphorylation of cPLA2 is not
required for its receptor-mediated activation.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27723-27729
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
EVIDENCE THAT PROLINE-DIRECTED PHOSPHORYLATION IS NOT REQUIRED
FOR MOBILIZATION OF ARACHIDONIC ACID BY cPLA2
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