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

2003; Elsevier BV; Volume: 70; Issue: 3-4 Linguagem: Inglês

10.1016/s0090-6980(02)00134-x

2212-196X

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

Metabolism, Diabetes, and Cancer

Peroxisome proliferator-activated receptor γ (PPARγ) is a critical regulator of adipocyte differentiation. Whilst 15-deoxy-Δ12,14-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 PPARγ. 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 PPARγ 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 PPARγ expression, suggesting that this prostaglandin may contribute to PPARγ signalling in vivo.