Cyclooxygenase‐2 is acutely induced by CCAAT/enhancer‐binding protein β to produce prostaglandin E 2 and F 2α following gonadotropin stimulation in Leydig cells

2019 ◽  
Vol 86 (7) ◽  
pp. 786-797 ◽  
Author(s):  
Takashi Yazawa ◽  
Yoshitaka Imamichi ◽  
Koh‐ichi Yuhki ◽  
Junsuke Uwada ◽  
Daisuke Mikami ◽  
...  
Keyword(s):  
Leydig Cells ◽  
Binding Protein ◽  
Cyclooxygenase 2 ◽  
Prostaglandin E ◽  
Gonadotropin Stimulation ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein

CCAAT/Enhancer binding protein β regulates prostaglandin E synthase expression and prostaglandin E2production in activated microglial cells

Glia ◽  
2013 ◽  
Vol 61 (10) ◽  
pp. 1607-1619 ◽  
Author(s):  
Marco Straccia ◽  
Guido Dentesano ◽  
Tony Valente ◽  
Marta Pulido-Salgado ◽  
Carme Solà ◽  
...  
Keyword(s):  
Binding Protein ◽  
Microglial Cells ◽  
Prostaglandin E ◽  
Prostaglandin E Synthase ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein

scholarly journals Transcriptional cooperation between NF-κB p50 and CCAAT/enhancer binding protein β regulates Nur77 transcription in Leydig cells

2008 ◽  
Vol 42 (2) ◽  
pp. 131-138 ◽  
Author(s):  
Bassam El-Asmar ◽  
Xavier C Giner ◽  
Jacques J Tremblay
Keyword(s):  
Transcription Factors ◽  
Leydig Cells ◽  
Binding Protein ◽  
Site Directed Mutagenesis ◽  
Orphan Nuclear Receptor ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein ◽  
Cell Gene Expression ◽  
Factor C ◽  
And Function

Expression of steroidogenic enzyme-encoding genes in testicular Leydig cells is complex and involves several transcription factors including the orphan nuclear receptor NUR77 (NR4A1) and the bZIP factor CCAAT/enhancer binding protein β (EBPβ). How these transcription factors are integrated into a functional network, however, remains to be fully understood. Here, we report that the transcription factor C/EBPβ can activate the Nur77 promoter as revealed by transient transfections in MA-10 Leydig cells. Through 5′ progressive deletions and site-directed mutagenesis, the C/EBPβ-mediated activation of the Nur77 promoter was found to be dependent on a novel species-conserved C/EBP element located at −110 bp. We also demonstrate using electromobility shift assay that C/EBPβ specifically binds to this element. Furthermore, we report a functional cooperation between C/EBPβ and the p50 subunit of NF-κB that involves a previously uncharacterized κB element located at −18 bp. Promoter analysis revealed that either the C/EBP or the κB element was sufficient to sustain the C/EBPβ-p50 cooperation thus suggesting that both factors physically interact. Altogether, our results provide new data regarding Nur77 transcription in testicular Leydig cells in addition to providing new insights into the interplay between transcription factors involved in Leydig cell gene expression and function.

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