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Originally published In Press as doi:10.1074/jbc.M101516200 on September 24, 2001

J. Biol. Chem., Vol. 276, Issue 47, 43842-43849, November 23, 2001
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p38 MAPK Regulates Group IIa Phospholipase A2 Expression in Interleukin-1beta -stimulated Rat Neonatal Cardiomyocytes*

Norbert DegouseeDagger , Eva StefanskiDagger , Thomas F. LindsayDagger , David A. Ford§, Rohan ShahaniDagger , Catherine A. Andrews, Donna J. Thuerauf, Christopher C. Glembotski, Timo J. Nevalainen||, Jay Tischfield**, and Barry B. RubinDagger Dagger Dagger

From the Dagger  Division of Vascular Surgery, Max Bell Research Center 1-917, Toronto General Hospital, Toronto, Ontario M5G-2C4, Canada, the § Department of Biochemistry and Molecular Biology, St. Louis University Health Sciences Center, St. Louis, Missouri 63104,  San Diego State University Heart Institute and the Department of Biology, San Diego State University, San Diego, California 92182, the || Department of Pathology, University of Turku, Turku 20520, Finland, and the ** Department of Genetics, Rutgers, State University of New Jersey, Piscataway, New Jersey 08854-8082

Group IIa phospholipase A2 (GIIa PLA2) is released by some cells in response to interleukin-1beta . The purpose of this study was to determine whether interleukin-1beta would stimulate the synthesis and release of GIIa PLA2 from cardiomyocytes, and to define the role of p38 MAPK and cytosolic PLA2 in the regulation of this process. Whereas GIIa PLA2 mRNA was not identified in untreated cells, exposure to interleukin-1beta resulted in the sustained expression of GIIa PLA2 mRNA. Interleukin-1beta also stimulated a progressive increase in cellular and extracellular GIIa PLA2 protein levels and increased extracellular PLA2 activity 70-fold. In addition, interleukin-1beta stimulated the p38 MAPK-dependent activation of the downstream MAPK-activated protein kinase, MAPKAP-K2. Treatment with the p38 MAPK inhibitor, SB202190, decreased interleukin-1beta stimulated MAPKAP-K2 activity, GIIa PLA2 mRNA expression, GIIa PLA2 protein synthesis, and the release of extracellular PLA2 activity. Infection with an adenovirus encoding a constitutively active form of MKK6, MKK6(Glu), which selectively phosphorylates p38 MAPK, induced cellular GIIa PLA2 protein synthesis and the release of GIIa PLA2 and increased extracellular PLA2 activity 3-fold. In contrast, infection with an adenovirus encoding a phosphorylation-resistant MKK6, MKK6(A), did not result in GIIa PLA2 protein synthesis or release by unstimulated cardiomyocytes. In addition, infection with an adenovirus encoding MKK6(A) abrogated GIIa PLA2 protein synthesis and release by interleukin-1beta -stimulated cells. These results provide direct evidence that p38 MAPK activation was necessary for interleukin-1beta -induced synthesis and release of GIIa PLA2 by cardiomyocytes.

* This work was supported in part by Heart and Stroke Foundation of Canada Grant NA-4151 (to B. B. R.), the Research Fund of Turku University Hospital (to T. J. N.), and National Institutes of Health Grants HL 42665 (to D. A. F.), HL-25037, HL-63975 (to C. C. G.), and DK38185 (to J. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger Recipient of the Wylie Scholar Award in Academic Vascular Surgery from the Pacific Vascular Research Foundation, San Francisco, CA and a Fellowship from the Bickel Foundation, Toronto, Ontario, Canada. To whom correspondence should be addressed: Division of Vascular Surgery, 200 Elizabeth St., EC5-302a, Toronto General Hospital, Toronto, Ontario M5G-2C4, Canada. Tel.: 416-340-3645; Fax: 416-340-5029; E-mail: barry.rubin@uhn.on.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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