2. Academic Validation
  3. Identification of a novel prostaglandin reductase reveals the involvement of prostaglandin E2 catabolism in regulation of peroxisome proliferator-activated receptor gamma activation

Identification of a novel prostaglandin reductase reveals the involvement of prostaglandin E2 catabolism in regulation of peroxisome proliferator-activated receptor gamma activation

  • J Biol Chem. 2007 Jun 22;282(25):18162-18172. doi: 10.1074/jbc.M702289200.
Wen-Ling Chou 1,  Lee-Ming Chuang 2,  Chi-Chi Chou 3,  Andrew H-J Wang 3,  John A Lawson 4,  Garret A FitzGerald 4,  Zee-Fen Chang 5
Affiliations

Affiliations

  • 1 Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei 100, Taiwan.
  • 2 Department of Internal Medicine, National Taiwan University Hospital, Taipei 100, Taiwan.
  • 3 Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan; National Core Facilities for Proteomics Research, Taipei 115, Taiwan.
  • 4 Institute for Translational Medicine and Therapeutics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104.
  • 5 Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei 100, Taiwan. Electronic address: ZFCHANG@ha.mc.ntu.edu.tw.
PMID: 17449869 DOI: 10.1074/jbc.M702289200
Abstract

This report identifies a novel gene encoding 15-oxoprostaglandin-Delta13-reductase (PGR-2), which catalyzes the reaction converting 15-keto-PGE2 to 13,14-dihydro-15-keto-PGE2. The expression of PGR-2 is up-regulated in the late phase of 3T3-L1 adipocyte differentiation and predominantly distributed in adipose tissue. Overexpression of PGR-2 in cells decreases Peroxisome Proliferator-activated Receptor gamma (PPARgamma)-dependent transcription and prohibits 3T3-L1 adipocyte differentiation without affecting expression of PPARgamma. Interestingly, we found that 15-keto-PGE2 can act as a ligand of PPARgamma to increase co-activator recruitment, thus activating PPARgamma-mediated transcription and enhancing adipogenesis of 3T3-L1 cells. Overexpression of 15-hydroxyprostaglandin dehydrogenase, which catalyzes the oxidation reaction of PGE2 to form 15-keto-PGE2, significantly increased PPARgamma-mediated transcription in a PGE2-dependent manner. Reciprocally, overexpression of wild-type PGR-2, but not the catalytically defective mutant, abolished the effect of 15-keto-PGE2 on PPARgamma activation. These results demonstrate a novel link between catabolism of PGE2 and regulation of ligand-induced PPARgamma activation.

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