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J. Biol. Chem., Vol. 277, Issue 36, 33153-33163, September 6, 2002
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From the ¶ Department of Pathology, University of Pittsburgh
School of Medicine, Pittsburgh, Pennsylvania 15213, The 85-kDa cytosolic phospholipase
A2 (cPLA2) plays an important role in the
control of arachidonic acid metabolism. This study was designed to
investigate the possible contributions of cPLA2 and group
IIA secretory phospholipase A2 (sPLA2) in the regulation of peroxisome proliferator-activated receptor
(PPAR)-mediated gene transcription in human airway epithelial cells.
Primary normal human bronchial epithelial cells and human lung
epithelial cell lines BEAS 2B, A549, and NCI-H292 all express PPAR
85-kDa Cytosolic Phospholipase A2 Mediates Peroxisome
Proliferator-activated Receptor
Activation in Human Lung
Epithelial Cells*
§,,, and
Critical Care Medicine Department, Clinical Center,
National Institutes of Health, Bethesda, Maryland 20892, and the
§ Department of Allergy and Clinical Immunology, Medical
University of Lodz, Lodz 92213, Poland
and -
. Overexpression of cPLA2 in BEAS 2B cells and
primary bronchial epithelial cells resulted in a significant increase
of PPAR-mediated reporter activity. In contrast, overexpression of
group IIA sPLA2 had no effect on PPAR activation. The
PPAR activity in A549 cells was significantly inhibited by the
cPLA2 inhibitor arachidonyltrifluoromethyl ketone but not
by the sPLA2 inhibitor LY311727 and the iPLA2
inhibitor HELSS. Activation of cPLA2 by the calcium
ionophore, A23187, induced a dose-dependent increase of
PPAR activity in normal human bronchial epithelial cells and in the
A549 cells. Electrophoretic mobility shift assays show that the binding
between PPAR isolated from A549 cells and peroxisome proliferator
response element (PPRE) is enhanced by A23187 but partially blocked by
the cPLA2 inhibitors arachidonyltrifluoromethyl ketone and
methyl arachidonyl fluorophosphate. Finally, NS 398, a COX-2 inhibitor,
partially blocked the A23187 effect on PPAR activity and binding
to the PPRE suggesting involvement of COX-2 metabolites in PPRE
activation. The above results demonstrate a novel function of
cPLA2 in the control of PPAR activation in human lung
epithelial cells.
*
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: Dept. of
Pathology, University of Pittsburgh, Pittsburgh, PA 15213. E-mail:
wut@msx.upmc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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