Vol. 272, No. 30, Issue of July 25, pp. 18779–18789, 1997 | Lluis Fajas‡, Didier Auboeuf‡, Eric Raspé‡, Kristina Schoonjans‡, Anne-Marie Lefebvre‡, Regis Saladin†, Jamilla Najib‡, Martine Laville‡, Jean-Charles Fruchart‡, Samir Deeb‡, Antonio Vidal-Puig**, Jeffrey Flier**, Michael R. Briggs‡, Bart Staels‡ ‡‡, Hubert Vidal‡, and Johan Auwerx‡ §§
This study characterized the human PPARγ gene and its promoters, and analyzed the tissue-specific expression of PPARγ mRNA. The human PPARγ gene spans over 100 kb and contains nine exons, encoding two isoforms, PPARγ1 and PPARγ2. PPARγ1 is the predominant isoform in all tissues analyzed, with PPARγ2 being less abundant. High levels of PPARγ mRNA were found in adipose tissue and the large intestine, while intermediate levels were detected in kidney, liver, and small intestine. PPARγ2 was barely detectable in skeletal muscle. The human PPARγ gene structure is highly conserved with the mouse gene, and the 3' and 1' kb upstream regions of the transcription start sites of PPARγ1 and PPARγ2 are sufficient to control basal and tissue-specific gene expression. The study also demonstrated that PPARγ2 binds to a PPRE and transactivates reporter genes driven by PPREs. These findings provide insights into the regulation and function of PPARγ in human physiology, particularly in adipocyte differentiation and colonic function.This study characterized the human PPARγ gene and its promoters, and analyzed the tissue-specific expression of PPARγ mRNA. The human PPARγ gene spans over 100 kb and contains nine exons, encoding two isoforms, PPARγ1 and PPARγ2. PPARγ1 is the predominant isoform in all tissues analyzed, with PPARγ2 being less abundant. High levels of PPARγ mRNA were found in adipose tissue and the large intestine, while intermediate levels were detected in kidney, liver, and small intestine. PPARγ2 was barely detectable in skeletal muscle. The human PPARγ gene structure is highly conserved with the mouse gene, and the 3' and 1' kb upstream regions of the transcription start sites of PPARγ1 and PPARγ2 are sufficient to control basal and tissue-specific gene expression. The study also demonstrated that PPARγ2 binds to a PPRE and transactivates reporter genes driven by PPREs. These findings provide insights into the regulation and function of PPARγ in human physiology, particularly in adipocyte differentiation and colonic function.