scholarly journals Green Tea Polyphenol and Curcumin Inversely Regulate Human Involucrin Promoter Activity via Opposing Effects on CCAAT/Enhancer-binding Protein Function

2004 ◽  
Vol 279 (23) ◽  
pp. 24007-24014 ◽  
Author(s):  
Sivaprakasam Balasubramanian ◽  
Richard L. Eckert
Keyword(s):  
Green Tea ◽  
Protein Function ◽  
Promoter Activity ◽  
Binding Protein ◽  
Tea Polyphenol ◽  
Enhancer Binding Protein ◽  
Green Tea Polyphenol ◽  
Ccaat Enhancer Binding Protein ◽  
Opposing Effects ◽  
Involucrin Promoter

scholarly journals Thapsigargin suppresses phorbol ester-dependent human involucrin promoter activity by suppressing CCAAT-enhancer-binding protein α (C/EBPα) DNA binding

2000 ◽  
Vol 350 (3) ◽  
pp. 791 ◽  
Author(s):  
Sivaprakasam BALASUBRAMANIAN ◽  
Chapla AGARWAL ◽  
Tatiana EFIMOVA ◽  
George R. DUBYAK ◽  
Eric BANKS ◽  
...  
Keyword(s):  
Dna Binding ◽  
Phorbol Ester ◽  
Promoter Activity ◽  
Binding Protein ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein ◽  
Involucrin Promoter

Exchange protein directly activated by cAMP (EPAC) promotes transcriptional activation of the decidual prolactin gene via CCAAT/enhancer-binding protein in human endometrial stromal cells

2018 ◽  
Vol 30 (11) ◽  
pp. 1454
Author(s):  
Kazuya Kusama ◽  
Kazuhiro Tamura ◽  
Hanako Bai ◽  
Toshihiro Sakurai ◽  
Hirotaka Nishi ◽  
...  
Keyword(s):  
Promoter Activity ◽  
Binding Protein ◽  
Luciferase Assay ◽  
Mrna Levels ◽  
Reporter Activity ◽  
Camp Analogue ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein ◽  
Decidual Prolactin ◽  
Exchange Protein

Protein kinase A (PKA) signalling accompanies elevated intracellular cAMP levels during endometrial stromal cell (ESC) decidualisation. Exchange protein directly activated by cAMP (EPAC), an alternate mediator of cAMP signalling, promotes PKA analogue-induced decidualisation; however, the precise mechanism by which EPAC and PKA co-operatively stimulate decidualisation has not been characterised. To examine the role of CCAAT/enhancer-binding protein (C/EBP) in EPAC- and PKA-mediated decidualisation of primary human ESCs, a reporter plasmid containing the 332 bp region upstream from the transcription initiation site of the decidual prolactin (dPRL) gene was generated and the promoter activity was evaluated using a luciferase assay. The dPRL promoter activity was increased by treatment of transfected ESCs with the PKA-selective cAMP analogue N6-phenyl-cAMP (Phe) and enhanced further by co-treatment with the EPAC-selective cAMP analogue 8-(4-chlorophenyltio)-2′-O-methyl cAMP (CPT). Treatment with forskolin, an adenylyl cyclase activator, had a similar effect on reporter activity. Site-directed mutagenesis of the C/EBPβ- and/or C/EBPδ-binding site in the dPRL promoter abolished Phe/CPT-mediated elevation of the reporter activity. EPAC2 knockdown markedly reduced Phe-stimulated C/EBPβ and C/EBPδ mRNA levels, as well as forkhead box O1 (FOXO1) protein levels. These results suggest that EPAC signalling enhances PKA-mediated dPRL expression in ESCs by acting on C/EBP response elements in the promoter region of the gene.

scholarly journals Prostaglandin E2 Increases Transforming Growth Factor-β Type III Receptor Expression through CCAAT Enhancer-Binding Protein δ in Osteoblasts

2007 ◽  
Vol 21 (11) ◽  
pp. 2713-2724 ◽  
Author(s):  
Thomas L. McCarthy ◽  
Tony H. Pham ◽  
Bianca I. Knoll ◽  
Michael Centrella
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Promoter Activity ◽  
Binding Protein ◽  
Gene Promoter ◽  
Dominant Negative ◽  
Type Iii ◽  
Kinase C ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein

Abstract Variations in individual TGF-β receptors (TβRs) may modify TGF-β activity and significantly alter its effects on connective tissue growth or repair. Differences in the amount of TβR type III (TβRIII) relative to signal transducing TβRI occur on bone cells during differentiation or in response to other growth regulators. Here we investigated prostaglandin (PG) E2, a potent effector during trauma, inflammation, or mechanical load, on TβR expression in primary osteoblast-enriched cultures. PGE2 rapidly increased TβRIII mRNA and protein expression and enhanced TβRIII gene promoter activity through a discrete region within 0.4 kb of the transcription start site. PGE2 alters osteoblast function through multiple signal-inducing pathways. In this regard, protein kinase A (PKA) activators, PGE1 and forskolin, also enhanced gene expression through the TβRIII gene promoter, whereas protein kinase C activators, PGF2α and phorbol myristate acetate, did not. The stimulatory effect of PGE2 on TβRIII promoter activity was suppressed by a dominant negative PKA-regulatory subunit, but not by dominant negative protein kinase C. PGE2 specifically increased nuclear factor CCAAT enhancer-binding protein δ (C/EBPδ) binding to a half-binding site upstream of the basal TβRIII promoter region, and promoter activity was sensitive to C/EBPδ overexpression and to dominant-negative C/EBPδ competition. In parallel with their effect on TβRIII expression, activators of PKA decreased TGF-β-induced activity. In summary, high levels of PGE2 that occur with inflammation or trauma may, through PKA-activated C/EBPδ, preferentially increase TβRIII expression and in this way delay TGF-β-dependent activation of osteoblasts during the early stabilization phase of bone repair.

Sign in / Sign up

Export Citation Format

Share Document