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

TY - JOUR

T1 - Prostaglandin D2 synthase enzymes and PPARγ are co-expressed in mouse 3T3-L1 adipocytes and human tissues

AU - Jowsey, Ian R.

AU - Murdock, Paul R.

AU - Moore, Gary B. T.

AU - Murphy, Gregory J.

AU - Smith, Stephen A.

AU - Hayes, John D.

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

U2 - 10.1016/S0090-6980(02)00134-X

DO - 10.1016/S0090-6980(02)00134-X

M3 - Article

C2 - 12611492

SN - 1098-8823

VL - 70

SP - 267

EP - 284

JO - Prostaglandins & Other Lipid Mediators

JF - Prostaglandins & Other Lipid Mediators

IS - 3-4

ER -