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Journal of Lipid Research, Vol. 45, 667-673, April 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology

Induction of lysosomal phospholipase A₂ through the retinoid X receptor in THP-1 cells

Akira Abe, Heather K. Poucher, Miki Hiraoka and James A. Shayman¹

Nephrology Division, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109

¹ To whom correspondence should be addressed. e-mail: jshayman{at}umich.edu

An acidic phospholipase A₂ (LPLA₂) was recently purified and cloned. THP-1 cells were used to characterize the gene induction of LPLA₂. THP-1 cells were stimulated with several differentiation agents. The LPLA₂ mRNA and activity increased in cells treated with phorbol ester but not with vitamin D3, interferon-, or granulocyte macrophage colony-stimulating factor. All-trans-retinoic acid enhanced mRNA expression and enzyme activity in a dose- and time-dependent manner. The natural 9-cis and 13-cis isomers of retinoic acid enhanced transcription and activity. Two classes of nuclear receptors, the retinoic acid receptor (RAR) and the retinoid X receptor (RXR), mediate retinoic acid signaling. Specific RAR and RXR agonists were used to identify the nuclear receptor responsible for LPLA₂ induction by retinoic acid. Treatment with the RAR agonist 4-[E-2-tetrahydro-5,5,8,8-tetra-methyl-2-naphthalenyl]1-propenyl benzoic acid (TTNPB) resulted in a small and statistically significant increase of the mRNA expression and activity of LPLA₂. The RXR agonist methoprene acid worked as well as all-trans-retinoic acid at increasing both mRNA and enzyme activity. The methoprene acid and TTNPB effects were not synergistic. The peroxisome proliferator-activated receptor agonists 15-deoxy-^12,14-prostaglandin J₂ and troglitazone failed to induce LPLA₂ activity and mRNA.

Thus, an RXR-dependent pathway controls LPLA₂ gene activation by retinoic acid in THP-1 cells.

Supplementary key words retinoic acid • lysosome • phospholipase • phorbol ester

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