The Peroxisome Proliferator Response Element (PPRE) Present at Positions −681/−669 in the Rat Liver 3-Ketoacyl-CoA Thiolase B Gene Functionally Interacts Differently with PPARα and HNF-4

2000 ◽  
Vol 269 (2) ◽  
pp. 347-351 ◽  
Author(s):  
Valérie Nicolas-Frances ◽  
Vijay Kumar Dasari ◽  
Elric Abruzzi ◽  
Takashi Osumi ◽  
Norbert Latruffe
Keyword(s):  
Rat Liver ◽  
Peroxisome Proliferator ◽  
Response Element ◽  
Peroxisome Proliferator Response Element

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 Induction of the Acyl-Coenzyme A Synthetase Gene by Fibrates and Fatty Acids Is Mediated by a Peroxisome Proliferator Response Element in the C Promoter

1995 ◽  
Vol 270 (33) ◽  
pp. 19269-19276 ◽  
Author(s):  
Kristina Schoonjans ◽  
Mitsuhiro Watanabe ◽  
Hiroyuki Suzuki ◽  
Abderrahim Mahfoudi ◽  
Grigorios Krey ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Coenzyme A ◽  
Peroxisome Proliferator ◽  
Response Element ◽  
Peroxisome Proliferator Response Element ◽  
Acyl Coenzyme A

scholarly journals Identification and characterization of peroxisome proliferator response element in the mouse GLUT2 promoter

2005 ◽  
Vol 37 (2) ◽  
pp. 101-110 ◽  
Author(s):  
Seung-Soon Im ◽  
Jae-Woo Kim ◽  
Tae-Hyun Kim ◽  
Xian-Li Song ◽  
So-Youn Kim ◽  
...  
Keyword(s):  
Peroxisome Proliferator ◽  
Response Element ◽  
Peroxisome Proliferator Response Element ◽  
Identification And Characterization

scholarly journals Peroxisome Proliferator-Activated Receptor-γ Increases Adiponectin Secretion via Transcriptional Repression of Endoplasmic Reticulum Chaperone Protein ERp44

Endocrinology ◽  
2010 ◽  
Vol 151 (7) ◽  
pp. 3195-3203 ◽  
Author(s):  
Qinqiang Long ◽  
Ting Lei ◽  
Bin Feng ◽  
Changjun Yin ◽  
Dan Jin ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Transcriptional Repression ◽  
Energy Homeostasis ◽  
Luciferase Reporter ◽  
Peroxisome Proliferator ◽  
Response Element ◽  
Peroxisome Proliferator Activated Receptor ◽  
Ppar Γ ◽  
Pparγ Agonist ◽  
Peroxisome Proliferator Response Element

Adiponectin, an adipocyte-derived hormone, is a versatile player involved in the regulation of energy homeostasis, cardiovascular disease, and diabetes. Within adipocytes, adiponectin is retained in the lumen of the endoplasmic reticulum (ER) by binding to the thiol protein ER resident protein 44 kDa (ERp44), which is apparently regulated by the activation of nuclear receptor peroxisome proliferator-activated receptor (PPAR)-γ. However, the precise role of ERp44 in adiponectin secretion remains elusive. In the present study, we investigated the functional correlation between ERp44 and adiponectin in a pig model. The transcription of porcine ERp44 was regulated by PPARγ, which was consistent with the finding of putative peroxisome proliferator response element sites within ERp44 promoter. Using chromatin immunoprecipitation and luciferase reporter assays, we demonstrated that the transcription of porcine ERp44 is repressed through binding of PPARγ to a peroxisome proliferator response element site located between positions −981 and −1004 in its 5′-flanking region. In human embryonic kidney 293 cells stably transfected with cDNA encoding porcine adiponectin, the secretion of adiponectin was significantly up-regulated and the ERp44 mRNA was down-regulated observably, by either the treatment of PPARγ agonist rosiglitazone or the overexpression of PPARγ in these cells. Taken together, our results indicated that PPARγ is an essential regulatory factor for the transcriptional activity of ERp44, which in turn controls the secretion of adiponectin.

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