Isolation and Cloning of Human Peroxisome Proliferator Activated Receptor Gamma CDNA

Abstract

The nuclear hormone receptor superfamily proteins are ligand modulated transcription factors that directly connect cellular transcriptional responses to extracellular lipophilic signalling compounds, such as retinoids, steroids, and perhaps fatty acid and arachidonic acid metabolites as well (1). These receptors regulate major cellular processes including reproduction, development, homeostasis, differentiation, and oncogenesis (2). Retinoic acid receptors (RARs), v-erb A, and other nuclear receptors have important transcription regulating interactions with proteins from other transcription factor families, for example fos and jun (3–5). Nuclear receptors also have significant interactions with other members of their nuclear hormone receptor superfamily, for example retinoid X receptors, (RXRs) form functionally important heterodimers with the RARs (6). RXRs, however, can also heterodimerize with a number of different nuclear hormone receptors in vitro, including the Peroxisome Proliferatior Activated Receptors, (PPARs) (7).