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Journal of Lipid Research, Vol. 42, 716-724, May 2001
Copyright © 2001 by Lipid Research, Inc.

Original Article

Modulation of cytosolic phospholipase A₂ by PPAR activators in human preadipocytes

Correspondence to: Patrick C. Choy, To whom correspondence should be addressed.

Cytosolic phospholipase A₂ (cPLA₂) is responsible for the release of arachidonic acid, a precursor for eicosanoid biosynthesis, from cellular phospholipids. The objective of this study is to examine the regulation of cPLA₂ by peroxisome proliferator-activated receptor (PPAR) activators in preadipocyte SW872 (SW) cells. PPAR belong to the superfamily of nuclear hormone receptors that heterodimerize with the retinoid X receptor. In this study, the presence of both PPAR and PPAR was confirmed in SW cells by positive identification of their mRNA in the cellular homogenate. Clofibrate, a PPAR activator, caused an enhancement of ionophore A-23187-induced arachidonate release in SW cells. This increase resulted from an enhancement of cPLA₂ activity, which was caused by an increase in enzyme protein. Clofibrate at lower concentrations (10;–200 µM) produced increases in the mRNA levels of cPLA₂ in a dose-response manner. At higher concentrations (>400 µM), clofibrate treatment resulted in the attenuation of the cPLA₂ mRNA level and protein expression.

We postulate that clofibrate, acting through the PPAR, caused an induction in the transcription of cPLA₂ gene, which led to an increase in the cPLA₂ protein. The observed increase in arachidonate release in SW cells appeared to be a direct result of the enhanced cPLA₂ activity.—Jiang, Y. J., G. M. Hatch, D. Mymin, T. Dembinski, E. A. Kroeger, and P. C. Choy. Modulation of cytosolic phospholipase A₂ by PPAR activators in human preadipocytes. J. Lipid Res. 2001. 42: 716–724.

Supplementary key words: cPLA₂, PPAR, clofibrate, preadipocytes, arachidonic acid, SW cells, COX-2, peroxisome proliferator-activated receptor

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