scholarly journals The Role of c-Jun N-Terminal Kinase, p38, and Extracellular Signal-Regulated Kinase in Insulin-Induced Thr69 and Thr71 Phosphorylation of Activating Transcription Factor 2

2006 ◽  
Vol 20 (8) ◽  
pp. 1786-1795 ◽  
Author(s):  
Bart Baan ◽  
Hans van Dam ◽  
Gerard C. M. van der Zon ◽  
J. Antonie Maassen ◽  
D. Margriet Ouwens
Keyword(s):  
Transcription Factor ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Activating Transcription Factor

Temporal regulation of extracellular signal-regulated kinase 1/2 phosphorylation, heat shock protein 70 and activating transcription factor 3 during prostaglandin F-induced luteal regression in pseudopregnant rats following heat stress

2017 ◽  
Vol 29 (6) ◽  
pp. 1184 ◽  
Author(s):  
Wu-jiao Bai ◽  
Peng-jing Jin ◽  
Mei-qian Kuang ◽  
Quan-wei Wei ◽  
Fang-xiong Shi ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Luteal Regression ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Prostaglandin F ◽  
Activating Transcription Factor

The aim of the present study was to investigate the effects of heat stress on heat shock protein (HSP) 70 expression and mitogen-activated protein kinase (MAPK) and protein kinase (PK) B signalling during prostaglandin F (PGF)-induced luteal regression. During pseudopregnancy, rats were exposed to heat stress (HS, 40°C, 2 h) for 7 days and treated with PGF or physiological saline on Day 7; serum and ovaries were collected 0, 1, 2, 8 or 24 h after PGF treatment. The early inhibitory effect of PGF on progesterone was reduced in HS rats. HSP70 expression in response to PGF was significantly enhanced in HS rats. PGF-induced phosphorylation of extracellular signal-regulated kinase (ERK) 1/2 was significantly greater in the HS group; however, HS rats exhibited elevated basal levels of phosphorylation of p38 MAPK, but not ERK1/2. PGF treatment increased expression of activating transcription factor (ATF) 3 at 2 h, which was inhibited by heat stress. Evaluating PKB signalling revealed that phosphorylation of p-Akt (Thr308 and Ser473) was reduced at 8 and 24 h after PGF treatment in both non-heat stress (NHS) and HS groups, but there were no significant differences between the HS and NHS groups at any of the time points. In conclusion, the present study provides further evidence that heat stress may enhance HSP70 and affect ERK1/2 and ATF3 expression, but not Akt activation, during PGF-induced luteal regression in pseudopregnant rats.

ERK5 and its role in tumour development

2012 ◽  
Vol 40 (1) ◽  
pp. 251-256 ◽  
Author(s):  
Pamela A. Lochhead ◽  
Rebecca Gilley ◽  
Simon J. Cook
Keyword(s):  
Mitogen Activated Protein Kinase ◽  
Invasion And Migration ◽  
Extracellular Signal Regulated Kinase ◽  
Protein Levels ◽  
Extracellular Signal ◽  
Mapk Signalling ◽  
Mitogen Activated Protein ◽  
Tumour Cell Invasion ◽  
And Migration

The MEK5 [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase 5]/ERK5 pathway is the least well studied MAPK signalling module. It has been proposed to play a role in the pathology of cancer. In the present paper, we review the role of the MEK5/ERK5 pathway using the ‘hallmarks of cancer’ as a framework and consider how this pathway is deregulated. As well as playing a key role in endothelial cell survival and tubular morphogenesis during tumour neovascularization, ERK5 is also emerging as a regulator of tumour cell invasion and migration. Several oncogenes can stimulate ERK5 activity, and protein levels are increased by a novel amplification at chromosome locus 17p11 and by down-regulation of the microRNAs miR-143 and miR-145. Together, these finding underscore the case for further investigation into understanding the role of ERK5 in cancer.

cAMP and Extracellular Signal-Regulated Kinase Signaling in Response to d-Amphetamine and Methylphenidate in the Prefrontal Cortex in Vivo: Role of β1-Adrenoceptors

2005 ◽  
Vol 68 (2) ◽  
pp. 421-429 ◽  
Author(s):  
Vincent Pascoli ◽  
Emmanuel Valjent ◽  
Anne-Gaëlle Corbillé ◽  
Jean-Christophe Corvol ◽  
Jean-Pol Tassin ◽  
...  
Keyword(s):  
Prefrontal Cortex ◽  
Kinase Signaling ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal

scholarly journals Glycogen Synthase Kinase 3β and Extracellular Signal-Regulated Kinase Inactivate Heat Shock Transcription Factor 1 by Facilitating the Disappearance of Transcriptionally Active Granules after Heat Shock

1998 ◽  
Vol 18 (11) ◽  
pp. 6624-6633 ◽  
Author(s):  
Bin He ◽  
Yong-Hong Meng ◽  
Nahid F. Mivechi
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Transcriptional Activity ◽  
Glycogen Synthase ◽  
Heat Shock Transcription Factor ◽  
Glycogen Synthase Kinase 3Β ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Gsk 3Β ◽  
Transcription Factor 1

ABSTRACT Heat shock transcription factor 1 (HSF-1) activates the transcription of heat shock genes in eukaryotes. Under normal physiological growth conditions, HSF-1 is a monomer. Its transcriptional activity is repressed by constitutive phosphorylation. Upon activation, HSF-1 forms trimers, acquires DNA binding activity, increases transcriptional activity, and appears as punctate granules in the nucleus. In this study, using bromouridine incorporation and confocal laser microscopy, we demonstrated that newly synthesized pre-mRNAs colocalize to the HSF-1 punctate granules after heat shock, suggesting that these granules are sites of transcription. We further present evidence that glycogen synthase kinase 3β (GSK-3β) and extracellular signal-regulated kinase mitogen-activated protein kinase (ERK MAPK) participate in the down regulation of HSF-1 transcriptional activity. Transient increases in the expression of GSK-3β facilitate the disappearance of HSF-1 punctate granules and reduce hsp-70 transcription after heat shock. We have also shown that ERK is the priming kinase for GSK-3β. Taken together, these results indicate that GSK-3β and ERK MAPK facilitate the inactivation of activated HSF-1 after heat shock by dispersing HSF-1 from the sites of transcription.

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