Regulation of transcription of the steroidogenic acute regulatory protein (StAR) gene: temporal and spatial changes in transcription factor binding and histone modification

2004 ◽  
Vol 215 (1-2) ◽  
pp. 119-126 ◽  
Author(s):  
Hisahiko Hiroi ◽  
Lane K Christenson ◽  
Jerome F Strauss
Keyword(s):  
Transcription Factor ◽  
Histone Modification ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Regulation Of Transcription ◽  
Factor Binding ◽  
Spatial Changes ◽  
Temporal And Spatial ◽  
Steroidogenic Acute Regulatory ◽  
Star Gene

scholarly journals Porcine and Bovine Steroidogenic Acute Regulatory Protein (StAR) Gene Expression during Gestation1

Endocrinology ◽  
1997 ◽  
Vol 138 (3) ◽  
pp. 1085-1091 ◽  
Author(s):  
Nicolas Pilon ◽  
Isabelle Daneau ◽  
Chantal Brisson ◽  
Jean-François Ethier ◽  
Jacques G. Lussier ◽  
...  
Keyword(s):  
Gene Expression ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Steroidogenic Acute Regulatory ◽  
Star Gene

scholarly journals Synergistic Activation of Steroidogenic Acute Regulatory Protein Expression and Steroid Biosynthesis by Retinoids: Involvement of cAMP/PKA Signaling

Endocrinology ◽  
2014 ◽  
Vol 155 (2) ◽  
pp. 576-591 ◽  
Author(s):  
Pulak R. Manna ◽  
Andrzej T. Slominski ◽  
Steven R. King ◽  
Cloyce L. Stetson ◽  
Douglas M. Stocco
Keyword(s):  
Retinoic Acid ◽  
Leydig Cells ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Liver X Receptor ◽  
Steroidogenic Acute Regulatory Protein ◽  
Type I ◽  
Steroid Biosynthesis ◽  
Steroidogenic Acute Regulatory ◽  
Star Gene

Both retinoic acid receptors (RARs) and retinoid X receptors (RXRs) mediate the action of retinoids that play important roles in reproductive development and function, as well as steroidogenesis. Regulation of steroid biosynthesis is principally mediated by the steroidogenic acute regulatory protein (StAR); however, the modes of action of retinoids in the regulation of steroidogenesis remain obscure. In this study we demonstrate that all-trans retinoic acid (atRA) enhances StAR expression, but not its phosphorylation (P-StAR), and progesterone production in MA-10 mouse Leydig cells. Activation of the protein kinase A (PKA) cascade, by dibutyrl-cAMP or type I/II PKA analogs, markedly increased retinoid-responsive StAR, P-StAR, and steroid levels. Targeted silencing of endogenous RARα and RXRα, with small interfering RNAs, resulted in decreases in 9-cis RA-stimulated StAR and progesterone levels. Truncation of and mutational alterations in the 5′-flanking region of the StAR gene demonstrated the importance of the −254/−1-bp region in retinoid responsiveness. An oligonucleotide probe encompassing an RXR/liver X receptor recognition motif, located within the −254/−1-bp region, specifically bound MA-10 nuclear proteins and in vitro transcribed/translated RXRα and RARα in EMSAs. Transcription of the StAR gene in response to atRA and dibutyrl-cAMP was influenced by several factors, its up-regulation being dependent on phosphorylation of cAMP response-element binding protein (CREB). Chromatin immunoprecipitation studies revealed the association of phosphorylation of CREB, CREB binding protein, RXRα, and RARα to the StAR promoter. Further studies elucidated that hormone-sensitive lipase plays an important role in atRA-mediated regulation of the steroidogenic response that involves liver X receptor signaling. These findings delineate the molecular events by which retinoids influence cAMP/PKA signaling and provide additional and novel insight into the regulation of StAR expression and steroidogenesis in mouse Leydig cells.

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