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J Biol Chem, Vol. 273, Issue 44, 28766-28772, October 30, 1998
From the Department of Pharmacology, University of Oxford,
Mansfield Road, Oxford OX1 3QT, United Kingdom
The kinase inhibitors SB 203580 and PD 98059 have
been reported to be specific inhibitors of the 38- and 42/44-kDa
mitogen-activated protein kinase (MAPK) pathways, respectively. In this
study, the two inhibitors were found to decrease platelet aggregation
induced by low concentrations of arachidonic acid, suggesting that they also interfere with the metabolism of arachidonic acid to thromboxane A2. In support of this, SB 203580 and PD 98059 inhibited the conversion of exogenous [3H]arachidonic
acid to [3H]thromboxane in intact platelets. Measurement
of platelet cyclooxygenase-1 activity following immunoprecipitation
revealed that SB 203580 and PD 98059 are direct inhibitors of this
enzyme. Both compounds were shown to inhibit purified cyclooxygenase-1
and -2 by a reversible mechanism. In addition, SB 203580 (but not PD
98059) inhibited platelet aggregation induced by prostaglandin
H2 and the conversion of prostaglandin H2 to
thromboxane A2 in intact platelets. SB 203580 also
inhibited this pathway in platelet microsome preparations, suggesting a
direct inhibitory effect on thromboxane synthase. These results
demonstrate that direct effects of the two kinase inhibitors on active
arachidonic acid metabolites have to be excluded before using these
compounds for the investigation of MAPKs in signal transduction
pathways. This is of particular relevance to studies on the regulation
of cytosolic phospholipase A2 as these two MAPKs are
capable of phosphorylating cytosolic phospholipase A2,
thereby increasing its intrinsic activity.
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