scholarly journals Progesterone Receptor Rapid Signaling Mediates Serine 345 Phosphorylation and Tethering to Specificity Protein 1 Transcription Factors

2008 ◽  
Vol 22 (4) ◽  
pp. 823-837 ◽  
Author(s):  
Emily J. Faivre ◽  
Andrea R. Daniel ◽  
Christopher J. Hillard ◽  
Carol A. Lange
Keyword(s):  
Transcription Factors ◽  
Progesterone Receptor ◽  
Specificity Protein 1 ◽  
Specificity Protein ◽  
Rapid Signaling

Transcription factors YY1, Sp1 and Sp3 modulate dystrophin Dp71 gene expression in hepatic cells

2016 ◽  
Vol 473 (13) ◽  
pp. 1967-1976 ◽  
Author(s):  
Katia Peñuelas-Urquides ◽  
Carolina Becerril-Esquivel ◽  
Laura C. Mendoza-de-León ◽  
Beatriz Silva-Ramírez ◽  
José Dávila-Velderrain ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Promoter Region ◽  
Site Directed Mutagenesis ◽  
Cellular Processes ◽  
Specificity Protein 1 ◽  
Hepatic Cells ◽  
Dna Elements ◽  
Yin And Yang ◽  
Specificity Protein ◽  
Flanking Regions

Dystrophin Dp71, the smallest product encoded by the Duchenne muscular dystrophy gene, is ubiquitously expressed in all non-muscle cells. Although Dp71 is involved in various cellular processes, the mechanisms underlying its expression have been little studied. In hepatic cells, Dp71 expression is down-regulated by the xenobiotic β-naphthoflavone. However, the effectors of this regulation remain unknown. In the present study we aimed at identifying DNA elements and transcription factors involved in Dp71 expression in hepatic cells. Relevant DNA elements on the Dp71 promoter were identified by comparing Dp71 5′-end flanking regions between species. The functionality of these elements was demonstrated by site-directed mutagenesis. Using EMSAs and ChIP, we showed that the Sp1 (specificity protein 1), Sp3 (specificity protein 3) and YY1 (Yin and Yang 1) transcription factors bind to the Dp71 promoter region. Knockdown of Sp1, Sp3 and YY1 in hepatic cells increased endogenous Dp71 expression, but reduced Dp71 promoter activity. In summary, Dp71 expression in hepatic cells is carried out, in part, by YY1-, Sp1- and Sp3-mediated transcription from the Dp71 promoter.

scholarly journals Progesterone promotes endothelial nitric oxide synthase expression through enhancing nuclear progesterone receptor-SP-1 formation

2020 ◽  
Vol 319 (2) ◽  
pp. H341-H348
Author(s):  
Yuehua You ◽  
Wanying Tan ◽  
Yongzheng Guo ◽  
Minghao Luo ◽  
Fei-fei Shang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Progesterone Receptor ◽  
Endothelial Nitric Oxide Synthase ◽  
Dependent Manner ◽  
Enos Expression ◽  
Specificity Protein 1 ◽  
Specificity Protein ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Progesterone directly upregulated endothelial nitric oxide synthase (eNOS) expression in human endothelial cells. Progesterone augmented eNOS promoter activity through a progesterone receptor A- and specificity protein-1-dependent manner. Antagonism of the progesterone receptor reduced eNOS expression and impaired vasodilation in rats.

Sumoylation of Specificity Protein 1 Augments Its Degradation by Changing the Localization and Increasing the Specificity Protein 1 Proteolytic Process

2008 ◽  
Vol 380 (5) ◽  
pp. 869-885 ◽  
Author(s):  
Yi-Ting Wang ◽  
Jian-Ying Chuang ◽  
Meng-Ru Shen ◽  
Wen-Bin Yang ◽  
Wen-Chang Chang ◽  
...  
Keyword(s):  
Specificity Protein 1 ◽  
Specificity Protein

Specificity protein 1 and Smad-dependent regulation of human heme oxygenase-1 gene by transforming growth factor-β1 in renal epithelial cells

2007 ◽  
Vol 293 (3) ◽  
pp. F885-F894 ◽  
Author(s):  
Amie Traylor ◽  
Thomas Hock ◽  
Nathalie Hill-Kapturczak
Keyword(s):  
Growth Factor ◽  
Heme Oxygenase ◽  
Transforming Growth Factor ◽  
Tissue Injury ◽  
Transforming Growth Factor Β1 ◽  
Molecular Regulation ◽  
Heme Oxygenase 1 ◽  
Specificity Protein 1 ◽  
Specificity Protein ◽  
Tgf Β1

Excess transforming growth factor-β1 (TGF-β1) in the kidney leads to increased cell proliferation and deposition of extracellular matrix, resulting in progressive kidney fibrosis. TGF-β1, however, stabilizes and attenuates tissue injury through the activation of cytoprotective proteins, including heme oxygenase-1 (HO-1). HO-1 catabolizes pro-oxidant heme into substances with anti-oxidant, anti-apoptotic, anti-fibrogenic, vasodilatory and immune modulatory properties. Little is known regarding the molecular regulation of human HO-1 induction by TGF-β1 except that it is dependent on de novo RNA synthesis and requires a group of structurally related proteins called Smads. It is not known whether other DNA binding proteins are required to initiate transcription of HO-1 and, furthermore, the promoter region(s) involved in TGF-β1-mediated induction of HO-1 has not been identified. The purpose of this study was to further delineate the molecular regulation of HO-1 by TGF-β1 in human renal proximal tubular cells. Actinomycin D and nuclear run-on studies demonstrate that TGF-β1 augments HO-1 expression by increased gene transcription and does not involve increased mRNA stability. Using transient transfection, mithramycin A, small interfering RNA, electrophoretic mobility shift assays, and decoy oligonucleotide experiments, a TGF-β1-responsive region is identified between 9.1 and 9.4 kb of the human HO-1 promoter. This ∼280-bp TGF-β1-responsive region contains a putative Smad binding element and specificity protein 1 binding sites, both of which are required for human HO-1 induction by TGF-β1.

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