scholarly journals Genome-Wide Profiling of Liver X Receptor, Retinoid X Receptor, and Peroxisome Proliferator-Activated Receptor   in Mouse Liver Reveals Extensive Sharing of Binding Sites

2011 ◽  
Vol 32 (4) ◽  
pp. 852-867 ◽  
Author(s):  
M. Boergesen ◽  
T. A. Pedersen ◽  
B. Gross ◽  
S. J. van Heeringen ◽  
D. Hagenbeek ◽  
...  
Keyword(s):  
Binding Sites ◽  
Mouse Liver ◽  
Liver X Receptor ◽  
Retinoid X Receptor ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Genome Wide

scholarly journals Peroxisome proliferator-activated receptor α-retinoid X receptor agonists induce beta-cell protection against palmitate toxicity

FEBS Journal ◽  
2007 ◽  
Vol 274 (23) ◽  
pp. 6094-6105 ◽  
Author(s):  
Karine Hellemans ◽  
Karen Kerckhofs ◽  
Jean-Claude Hannaert ◽  
Geert Martens ◽  
Paul Van Veldhoven ◽  
...  
Keyword(s):  
Beta Cell ◽  
Retinoid X Receptor ◽  
Peroxisome Proliferator ◽  
Cell Protection ◽  
Peroxisome Proliferator Activated Receptor ◽  
Receptor Agonists ◽  
Beta Cell Protection

scholarly journals Peroxisome proliferator-activated receptor γ and retinoid X receptor transcription factors are released from activated human platelets and shed in microparticles

2008 ◽  
Vol 99 (01) ◽  
pp. 86-95 ◽  
Author(s):  
Sherry L Spinelli ◽  
Stephen J Pollock ◽  
Thomas I Murant ◽  
Jamie J O’Brien ◽  
Neil Blumberg ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Platelet Activation ◽  
Human Platelets ◽  
Retinoid X Receptor ◽  
Complex Spectrum ◽  
Peroxisome Proliferator ◽  
Monocytic Cell ◽  
Peroxisome Proliferator Activated Receptor ◽  
Pparγ Agonist ◽  
New Findings

SummaryPeroxisome proliferator-activated receptor γ (PPARγ) and its ligands are important regulators of lipid metabolism, inflammation, and diabetes. We previously demonstrated that anucleate human platelets express the transcription factor PPARγ and that PPARγ ligands blunt platelet activation. To further understand the nature of PPARγ in platelets, we determined the platelet PPARγ isoform(s) and investigated the fate of PPARγ following platelet activation. Our studies demonstrated that human platelets contain only the PPARγ1 isoform and after activation with thrombin, TRAP, ADP or collagen PPARγ is released from internal stores. PPARγ release was blocked by a cytoskeleton inhibitor, Latrunculin A. Platelet-released PPARγ was complexed with the retinoid X receptor (RXR) and retained its ability to bind DNA. Interestingly, the released PPARγ and RXR were microparticle associated and the released PPARγ/RXR complex retained DNA-binding ability. Additionally, a monocytic cell line, THP-1, is capable of internalizing PMPs. Further investigation following treatment of these cells with the PPARγ agonist, rosiglitazone and PMPs revealed a possible transcellular mechanism to attenuate THP-1 activation. These new findings are the first to demonstrate transcription factor release from platelets, revealing the complex spectrum of proteins expressed and expelled from platelets, and suggests that platelet PPARγ has an undiscovered role in human biology.

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