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M101516200v1
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Papers In Press, published online ahead of print September 24, 2001
J. Biol. Chem, 10.1074/jbc.M101516200
Submitted on February 19, 2001
Revised on September 20, 2001
Accepted on September 24, 2001

p38 MAP kinase regulates Group IIa phospholipase A2 expression in interleukin-1beta stimulated rat neonatal cardiomyocytes

Norbert Degousee, Eva Stefanski, Thomas F. Lindsay, David Ford, Rohan Shahani, Catherine A. Andrews, Donna J. Thuerauf, Christhopher C. Glembotski, Timo J. Nevalainen, Jay Tischfield, and Barry B. Rubin

Vascular Surgery, Toronto General Hospital, Toronto, Ontario M5G-2C4

Corresponding Author: barry.rubin{at}uhn.on.ca

Group IIa PLA2 (GIIa PLA2) is released by some cells in response to interleukin-1beta . The purpose of this study was to determine if 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. While 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.


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