XENOPUS PEROXISOME PROLIFERATOR ACTIVATED RECEPTORS - GENOMIC ORGANIZATION, RESPONSE ELEMENT RECOGNITION, HETERODIMER FORMATION WITH RETINOID-X RECEPTOR AND ACTIVATION BY FATTY-ACIDS

Citation
G. Krey et al., XENOPUS PEROXISOME PROLIFERATOR ACTIVATED RECEPTORS - GENOMIC ORGANIZATION, RESPONSE ELEMENT RECOGNITION, HETERODIMER FORMATION WITH RETINOID-X RECEPTOR AND ACTIVATION BY FATTY-ACIDS, Journal of steroid biochemistry and molecular biology, 47(1-6), 1993, pp. 65-73
Citations number
31
Categorie Soggetti
Biology,"Endocrynology & Metabolism
ISSN journal
09600760
Volume
47
Issue
1-6
Year of publication
1993
Pages
65 - 73
Database
ISI
SICI code
0960-0760(1993)47:1-6<65:XPPAR->2.0.ZU;2-8
Abstract
Peroxisome proliferator activated receptors are ligand activated trans cription factors belonging to the nuclear hormone receptor superfamily . Three cDNAs encoding such receptors have been isolated from Xenopus laevis (xPPAR alpha, beta, and gamma). Furthermore, the gene coding fo r xPPAR beta has been cloned, thus being the first member of this subf amily whose genomic organization has been solved. Functionally, xPPAR alpha as well as its mouse and rat homologs are thought to play an imp ortant role in lipid metabolism due to their ability to activate trans cription of a reporter gene through the promoter of the acyl-CoA oxida se (ACO) gene. ACO catalyzes the rate limiting step in the peroxisomal beta-oxidation of fatty acids. Activation is achieved by the binding of xPPAR alpha on a regulatory element (DR1) found in the promoter reg ion of this gene, xPPAR beta and gamma are also able to recognize the same type of element and are, as PPAR alpha, able to form heterodimers with retinoid X receptor. All three xPPARs appear to be activated by synthetic peroxisome proliferators as well as by naturally occurring f atty acids, suggesting that a common mode of action exists for all the members of this subfamily of nuclear hormone receptors.