Prostaglandin D2 synthase enzymes and PPARγ are co-expressed in mouse 3T3-L1 adipocytes and human tissues

Ian R. Jowsey, Paul R. Murdock, Gary B. T. Moore, Gregory J. Murphy, Stephen A. Smith, John D. Hayes

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    44 Citations (Scopus)


    Peroxisome proliferator-activated receptor gamma (PPAR?) is a critical regulator of adipocyte differentiation. Whilst 15-deoxy-delta(12,14)-prostaglandin J2 (15-d-PGJ2) has been identified as a putative endogenous ligand for this transcription factor, it is unclear whether the enzymes necessary for 15-d-PGJ2 biosynthesis are co-expressed with PPARgamma. Prostaglandin D2 synthase (PGDS) enzymes represent the terminal enzymatic components responsible for 15-d-PGJ2 production. Both glutathione (GSH)-dependent and GSH-independent PGDS isoenzymes exist. We have, therefore, examined the expression of PGDS isoenzymes in mouse 3T3-L1 adipocytes, and various human tissues. The GSH-independent PGDS was found to be expressed in 3T3-L1 cells both before and after their differentiation into adipocytes. By contrast, we were unable to detect expression of the GSH-dependent PGDS at any stage during the adipose conversion of 3T3-L1 cells. Quantitative analysis of mRNA levels for PPARgamma and each PGDS isoenzyme revealed their co-expression in a number of human tissues and cell types, including adipose tissue, placenta, prostate, and macrophages. These data reveal the potential for de novo 15-d-PGJ2 synthesis in the context of PPARgamma expression, suggesting that this prostaglandin may contribute to PPARgamma signalling in vivo.
    Original languageEnglish
    Pages (from-to)267-84
    Number of pages18
    JournalProstaglandins & Other Lipid Mediators
    Issue number3-4
    Publication statusPublished - 2003


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