scholarly journals Functional characterization of peroxisome proliferator-activated receptor-β/δ expression in colon cancer

2011 ◽  
Vol 50 (11) ◽  
pp. 884-900 ◽  
Author(s):  
Jennifer E. Foreman ◽  
Wen-Chi L. Chang ◽  
Prajakta S. Palkar ◽  
Bokai Zhu ◽  
Michael G. Borland ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Functional Characterization ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

Functional characterization of a peroxisome proliferator response-element located in the intron 3 of rat peroxisomal thiolase B gene

2003 ◽  
Vol 311 (1) ◽  
pp. 149-155 ◽  
Author(s):  
Franck Hansmannel ◽  
Marie-Claude Clémencet ◽  
Catherine Le Jossic-Corcos ◽  
Takashi Osumi ◽  
Norbert Latruffe ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Peroxisome Proliferator ◽  
Response Element ◽  
Peroxisome Proliferator Response Element

scholarly journals PRIC295, a Nuclear Receptor Coactivator, Identified from PPAR-Interacting Cofactor Complex

PPAR Research ◽  
2010 ◽  
Vol 2010 ◽  
pp. 1-16 ◽  
Author(s):  
Sean R. Pyper ◽  
Navin Viswakarma ◽  
Yuzhi Jia ◽  
Yi-Jun Zhu ◽  
Joseph D. Fondell ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Target Genes ◽  
Peroxisome Proliferator ◽  
Dependent Manner ◽  
Peroxisome Proliferator Activated Receptor ◽  
Nuclear Receptor Coactivator ◽  
Evolutionarily Conserved

The peroxisome proliferator-activated receptor- (PPAR) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPAR in rodents leads to the development of hepatocellular carcinomas. The ability of PPAR to induce expression of its target genes depends on Mediator, an evolutionarily conserved complex of cofactors and, in particular, the subunit 1 (Med1) of this complex. Here, we report the identification and characterization of PPAR-interacting cofactor (PRIC)-295 (PRIC295), a novel coactivator protein, and show that it interacts with the Med1 and Med24 subunits of the Mediator complex. PRIC295 contains 10 LXXLL signature motifs that facilitate nuclear receptor binding and interacts with PPAR and five other members of the nuclear receptor superfamily in a ligand-dependent manner. PRIC295 enhances the transactivation function of PPAR, PPAR, and ER. These data demonstrate that PRIC295 interacts with nuclear receptors such as PPAR and functions as a transcription coactivator underin vitroconditions and may play an important role in mediating the effectsin vivoas a member of the PRIC complex with Med1 and Med24.

Sign in / Sign up

Export Citation Format

Share Document