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J. Biol. Chem., Vol. 276, Issue 19, 15704-15711, May 11, 2001
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From the Department of Pharmacology, College of Medicine,
University of Tennessee Health Science Center,
Memphis, Tennessee 38163
Norepinephrine (NE) stimulates
phospholipase D (PLD) through a Ras/MAPK pathway in rabbit vascular
smooth muscle cells (VSMC). NE also activates calcium influx and
calmodulin (CaM)-dependent protein kinase
II-dependent cytosolic phospholipase A2
(cPLA2). Arachidonic acid (AA) released by
cPLA2-catalyzed phospholipid hydrolysis is then metabolized
into hydroxyeicosatetraenoic acids (HETEs) through lipoxygenase
and cytochrome P450 4A (CYP4A) pathways. HETEs, in turn, have been
shown to stimulate Ras translocation and to increase MAPK activity in
VSMC. This study was conducted to determine the contribution of
cPLA2-derived AA and its metabolites (HETEs) to the
activation of PLD. NE-induced PLD activation was reduced by two
structurally distinct CaM antagonists, W-7 and calmidazolium, and by
CaM-dependent protein kinase II inhibition. Blockade of
cPLA2 activity or protein depletion with selective cPLA2 antisense oligonucleotides abolished NE-induced PLD
activation. The increase in PLD activity elicited by NE was also
blocked by inhibitors of lipoxygenases (baicalein) and CYP4A
(17-octadecynoic acid), but not of cyclooxygenase
(indomethacin). AA and its metabolites (12(S)-,
15(S)-, and 20-HETEs) increased PLD activity. PLD
activation by AA and HETEs was reduced by inhibitors of Ras
farnesyltransferase (farnesyl protein transferase III and
BMS-191563) and MEK (U0126 and PD98059). These data suggest that HETEs
are the mediators of cPLA2-dependent PLD
activation by NE in VSMC. In addition to cPLA2, PLD was
also found to contribute to AA release for prostacyclin production via
the phosphatidate phosphohydrolase/diacylglycerol lipase pathway.
Finally, a catalytically inactive PLD2 (but not PLD1) mutant inhibited NE-induced PLD activity, and
PLD2 was tyrosine-phosphorylated in response to NE by a
MAPK-dependent pathway. We conclude that NE stimulates
cPLA2-dependent PLD2 through
lipoxygenase- and CYP4A-derived HETEs via the Ras/ERK pathway by a
mechanism involving tyrosine phosphorylation of PLD2 in
rabbit VSMC.
Phospholipase D Activation by Norepinephrine Is Mediated by
12(S)-, 15(S)-, and 20-Hydroxyeicosatetraenoic
Acids Generated by Stimulation of Cytosolic Phospholipase
A2
TYROSINE PHOSPHORYLATION OF PHOSPHOLIPASE D2 IN
RESPONSE TO NOREPINEPHRINE*
,
*
This work was supported in part by NHLBI Grant 19134-26 from
the National Institutes of Health.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.
Recipient of a postdoctoral fellowship from the American Heart
Association, Southeast Affiliate.
§
Supported by a National Institutes of Health minority postdoctoral fellowship.
¶
To whom correspondence should be addressed: Dept. of
Pharmacology, College of Medicine, University of Tennessee Health
Science Center, 874 Union Ave., Memphis, TN 38163. Tel.: 901-448-6075; Fax: 901-448-7206; E-mail: kmalik@utmem.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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