J. Lipid Res.
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A more recent version of this article appeared on April 1, 2008

Papers In Press, published online ahead of print January 9, 2008
J. Lipid Res., doi:10.1194/jlr.M700419-JLR200
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Submitted on September 21, 2007
Revised on November 30, 2007
Accepted on January 8, 2008

cPLA2 phosphorylation at S515 and S505 is required for arachidonic acid release in vascular smooth muscle cell

Zoran Pavicevic, Christina C. Leslie, and Kafait U. Malik

Pharmacology, University of Tennessee Health Science Center, Memphis, TN 38163

Corresponding Author: kmalik{at}utmem.edu

Cytosolic phospholipase A2 (cPLA2) is activated by phosphorylation at S505 by ERK1/2. However, rat brain calcium/calmodulin-dependent kinase II (CaMKII) phosphorylates recombinant cPLA2 at S515 and increases its activity in vitro. We studied the sites of cPLA2 phosphorylation and their significance in arachidonic acid (AA) release in response to norepinephrine (NE) in vivo in rabbit vascular smooth muscle cells (VSMC) by using specific anti-phospho-S515- and -S505 cPLA2 antibodies and by mutagenesis of S515 and S505 to alanine. NE increased phosphorylation of cPLA2 at S515 followed by phosphorylation of ERK1/2 and consequently phosphorylation of cPLA2 at S505. CaMKII inhibitor KN-93, attenuated phosphorylation of cPLA2 at S515 and S505, whereas ERK1/2 inhibitor U0126 reduced phosphorylation at S505 but not at S515. NE in cells transduced with adenovirus carrying ECFPcPLA2 wild type caused phosphorylation at S515 and S505 and increased AA release. Expression of S515A mutant in VSMC reduced phosphorylation of S505, ERK1/2, and AA release in response to NE. Transduction with double mutant (S515A/S505A) blocked phosphorylation of cPLA2, and AA release. This suggests that NE stimulated phosphorylation of cPLA2 at S515 is required for phosphorylation of S505 by ERK1/2 and that both sites of phosphorylation are important for AA release in VSMC.


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