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J. Biol. Chem., Vol. 277, Issue 12, 9920-9928, March 22, 2002
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From the Evidence suggests that the arachidonic acid
metabolite of 12-lipoxygenase,
12(S)-hydroxyeicosatetraenoic acid
(12(S)-HETE), not only mediates the effects of angiotensin
II (AngII), but also has direct effects on hypertrophy and matrix
protein production in vascular smooth muscle cells (VSMCs). This study
is aimed at identifying the signaling pathways involved in these
events. Treatment of porcine VSMCs with 12(S)-HETE led to
the activation of Ras and p38 MAPK. It also stimulated phosphorylation,
DNA-binding activity, and transactivation of the transcription factor
cAMP response element (CRE)-binding protein. In addition,
12(S)-HETE induced transcription from a fibronectin
promoter containing multiple CREs. AngII also induced transactivation
of CRE-binding protein and transcription from the fibronectin promoter.
A specific p38 MAPK inhibitor (SB202190) as well as a dominant-negative
Ras mutant (Ras-N17) blocked both 12(S)-HETE and AngII
effects. In addition, inhibitors of lipoxygenase also blocked AngII
effects. Both 12(S)-HETE and AngII increased cellular
hypertrophy with similar potency, and this was significantly blocked by
SB202190. Stable overexpression of murine leukocyte-type
12/15-lipoxygenase in VSMCs increased the levels of cell-associated
12(S)-HETE as well as basal activity of both ERK and p38
MAPKs. Furthermore, these 12-lipoxygenase-overexpressing cells
displayed significantly greater cellular hypertrophy relative to
mock-transfected cells. These results show for the first time that
oxidized lipids such as 12(S)-HETE can induce VSMC growth and matrix gene expression and mediate growth factor effects via activation of the Ras-MAPK pathway and key target transcription factors.
The Oxidized Lipid and Lipoxygenase Product
12(S)-Hydroxyeicosatetraenoic Acid Induces Hypertrophy and
Fibronectin Transcription in Vascular Smooth Muscle Cells via p38 MAPK
and cAMP Response Element-binding Protein Activation
MEDIATION OF ANGIOTENSIN II EFFECTS*
,,
Gonda Diabetes Center, Beckman Research
Institute of the City of Hope, Duarte, California 91010, the
§ Department of Endocrinology, University of Virginia
Medical School, Charlottesville, Virginia 22908, and the
¶ Department of Pharmacology, University of Tennessee,
Memphis, Tennessee 38163
*
This work was supported by National Institutes of Health
Grants PO1 HL55798 (to R. N. and J. L. N.) and RO1 DK58191 (to
R. N.) and by a grant from the Juvenile Diabetes Foundation (to
R. N.).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.
To whom correspondence should be addressed: Gonda Diabetes
Center, Beckman Research Institute of the City of Hope, 1500 East Duarte Rd., Duarte, CA 91010. Tel.: 626-359-8111 (ext. 62289); Fax:
626-301-8136; E-mail: rnatarajan@coh.org.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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