Structural Insight into Peroxisome Proliferator-Activated Receptor γ Binding of Two Ureidofibrate-Like Enantiomers by Molecular Dynamics, Cofactor Interaction Analysis, and Site-Directed Mutagenesis

2010 ◽  
Vol 53 (11) ◽  
pp. 4354-4366 ◽  
Author(s):  
Giorgio Pochetti ◽  
Nico Mitro ◽  
Antonio Lavecchia ◽  
Federica Gilardi ◽  
Neva Besker ◽  
...  
Metallomics ◽  
2015 ◽  
Vol 7 (7) ◽  
pp. 1180-1188 ◽  
Author(s):  
Youhei Hiromori ◽  
Akira Aoki ◽  
Jun-ichi Nishikawa ◽  
Hisamitsu Nagase ◽  
Tsuyoshi Nakanishi

Organotins, such as tributyltin (TBT) and triphenyltin (TPT), may disrupt endocrine activity in mammals arising from their ability to act as ligands for the retinoid X receptor (RXR) and the peroxisome proliferator-activated receptor γ (PPARγ).


2012 ◽  
Vol 2012 (31) ◽  
pp. n/a-n/a
Author(s):  
Christian R. Wick ◽  
Harald Lanig ◽  
Christof M. Jäger ◽  
Nicolai Burzlaff ◽  
Timothy Clark

PPAR Research ◽  
2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Yazi Huang ◽  
Beilei Zhao ◽  
Yahan Liu ◽  
Nanping Wang

Lipid phosphate phosphohydrolase 1 (LPP1), a membrane ectophosphohydrolase regulating the availability of bioactive lipid phosphates, plays important roles in cellular signaling and physiological processes such as angiogenesis and endothelial migration. However, the regulated expression of LPP1 remains largely unknown. Here, we aimed to examine a role of peroxisome proliferator-activated receptorγ(PPARγ) in the transcriptional control ofLPP1gene expression. In human umbilical vein endothelial cells (HUVECs), quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) demonstrated that activation of PPARγincreased the mRNA level of LPP1. Chromatin immunoprecipitation assay showed that PPARγbinds to the putative PPAR-responsive elements (PPREs) within the 5′-flanking region of the humanLPP1gene. Genomic fragment containing 1.7-kilobase of the promoter region was cloned by using PCR. The luciferase reporter assays demonstrated that overexpression of PPARγand rosiglitazone, a specific ligand for PPARγ, could significantly upregulate the reporter activity. However, site-directed mutagenesis of the PPRE motif abolished the induction. In conclusion, our results demonstrated that PPARγtranscriptionally activated the expression ofLPP1gene in ECs, suggesting a potential role of PPARγin the metabolism of phospholipids.


PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0116589 ◽  
Author(s):  
Joanna Lee ◽  
Veronique Daniels ◽  
Zara A. Sands ◽  
Florence Lebon ◽  
Jiye Shi ◽  
...  

2012 ◽  
Vol 2012 (31) ◽  
pp. 4973-4985 ◽  
Author(s):  
Christian R. Wick ◽  
Harald Lanig ◽  
Christof M. Jäger ◽  
Nicolai Burzlaff ◽  
Timothy Clark

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