Peroxisome proliferator-activated receptor g (PPARg) has been shown to stimulate progesterone production by bovine luteal cells. We previously reported higher expression of PPARg in old compared with new luteal tissue in the rat. The following studies were conducted to determine the role of PPARg in rat corpora lutea (CL) and test the hypothesis that PPARg plays a role in the metabolism of progesterone and/or luteal lifespan. Ovaries were removed from naturally cycling rats throughout the estrous cycle, and pseudopregnant rats. mRNA for PPARg and P450 side-chain cleavage (SCC) was localized in luteal tissue by in situ hybridization, and protein corresponding to PPARg and macrophages identified by immunohistochemistry. Luteal tissue was cultured with agonists (ciglitazone, prostaglandin J 2 ) or an antagonist (GW-9662) of PPARg. Progesterone was measured in media by RIA and levels of mRNA for 20a-hydroxysteriod dehydrogenase (HSD) and bcl-2 were measured in luteal tissue after culture by RT-PCR. An inverse relationship existed between the expression of mRNA for SCC and PPARg. There was no effect of PPARg agonists or the antagonist on luteal progesterone production in vitro, or levels of mRNA for 20a-HSD. PPARg protein was localized to the nuclei of luteal cells and did not correspond with the presence of macrophages. In new CL, ciglitazone decreased mRNA for bcl-2 on proestrus, estrus, and metestrus. Interestingly, GW-9662 also decreased mRNA for bcl-2 on proestrus and diestrus in old and new CL, and on metestrus in new CL. These data indicate that PPARg is not a major player in luteal progesterone production or metabolism but may be involved in regulating luteal lifespan.