PPARγ3 mRNA: a distinct PPARγ mRNA subtype transcribed from an independent promoter
- 30 October 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 438 (1-2), 55-60
- https://doi.org/10.1016/s0014-5793(98)01273-3
Abstract
PPARγ is a member of the peroxisome proliferator activated receptors (PPAR) subfamily of nuclear receptors. So far two PPARγ isoforms, PPARγ1 and PPARγ2, were known in mammals. We describe the structure of a novel human PPARγ subtype, PPARγ3. The PPARγ3 mRNA is transcribed from a novel promoter localized 5′ of exon A2. PPARγ3 mRNA expression was restricted to adipose tissue and large intestine. Similar to human PPARγ1 and -2, PPARγ3 is activated by thiazolidinediones and prostaglandin J derivatives and binds with high affinity to a PPRE.Keywords
This publication has 19 references indexed in Scilit:
- Ligand-independent Activation Domain in the N Terminus of Peroxisome Proliferator-activated Receptor γ (PPARγ)Journal of Biological Chemistry, 1997
- The Organization, Promoter Analysis, and Expression of the Human PPARγ GeneJournal of Biological Chemistry, 1997
- Thiazolidinediones produce a conformational change in peroxisomal proliferator-activated receptor-gamma: binding and activation correlate with antidiabetic actions in db/db miceEndocrinology, 1996
- A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiationCell, 1995
- 15-Deoxy-Δ12,14-Prostaglandin J2 is a ligand for the adipocyte determination factor PPARγCell, 1995
- Transient increase in obese gene expression after food intake or insulin administrationNature, 1995
- Fibrates increase human apolipoprotein A-II expression through activation of the peroxisome proliferator-activated receptor.Journal of Clinical Investigation, 1995
- Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factorCell, 1994
- mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer.Genes & Development, 1994
- Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficientlyCell, 1992