scholarly journals Estrogen Induces Estrogen Receptor  -Dependent cAMP Response Element-Binding Protein Phosphorylation via Mitogen Activated Protein Kinase Pathway in Basal Forebrain Cholinergic Neurons In Vivo

2006 ◽  
Vol 26 (15) ◽  
pp. 4104-4110 ◽  
Author(s):  
E. M. Szego
Keyword(s):  
Basal Forebrain ◽  
Cholinergic Neurons ◽  
Camp Response Element Binding ◽  
Mitogen Activated Protein Kinase ◽  
Camp Response Element ◽  
Basal Forebrain Cholinergic Neurons ◽  
Mitogen Activated Protein ◽  
Element Binding Protein ◽  
Kinase Pathway

scholarly journals Estrogen Activation of Cyclic Adenosine 5′-Monophosphate Response Element-Mediated Transcription Requires the Extracellularly Regulated Kinase/Mitogen-Activated Protein Kinase Pathway

Endocrinology ◽  
2003 ◽  
Vol 144 (3) ◽  
pp. 832-838 ◽  
Author(s):  
Christian B. Wade ◽  
Daniel M. Dorsa
Keyword(s):  
Protein Kinase ◽  
Mapk Pathway ◽  
Camp Response Element Binding ◽  
Mitogen Activated Protein Kinase ◽  
Camp Response Element ◽  
Response Element ◽  
Creb Phosphorylation ◽  
Mitogen Activated Protein ◽  
Element Binding Protein

The ability of estrogen to rapidly initiate a variety of signal transduction cascades is increasingly recognized as playing an important role in a number of tissue-specific transcriptional actions of the hormone. In vivo, estrogen rapidly elicits phosphorylation of cAMP response element-binding protein (CREB). We have previously shown that both ERα and ERβ are capable of activating the MAPK pathway in response to a low dose of 17β-estradiol. In the present study, the ability of estrogen to act through both ERα and ERβ to increase CREB phosphorylation was evaluated in an immortalized hippocampal cell line stably expressing either receptor. Estrogen treatment promoted rapid CREB phosphorylation, reaching a maximum by 15 min. This activation is completely blocked by the antiestrogen ICI 182,780, suggesting an estrogen receptor-dependent mechanism. The addition of the mitogen/ERK kinase-1 inhibitor, PD98059, also blocked the ability of estrogen to signal to CREB phosphorylation. Estrogen also caused an increase in p90Rsk activity, a critical mediator of MAPK effects. Surprisingly, blockade of the protein kinase A pathway in cells treated with estrogen did not affect estrogen-mediated CREB phosphorylation. Thus, MAPK and p90Rsk appear to be the primary mediators of estrogen-induced gene transcription through ERα and ERβ.

scholarly journals CNS neuroplasticity and salt-sensitive hypertension induced by prior treatment with subpressor doses of ANG II or aldosterone

2014 ◽  
Vol 306 (12) ◽  
pp. R908-R917 ◽  
Author(s):  
Sarah C. Clayton ◽  
Zhongming Zhang ◽  
Terry Beltz ◽  
Baojian Xue ◽  
Alan Kim Johnson
Keyword(s):  
Camp Response Element Binding ◽  
Salt Sensitivity ◽  
Mitogen Activated Protein Kinase ◽  
Male Rats ◽  
Ang Ii ◽  
Camp Response Element ◽  
Mitogen Activated Protein ◽  
Element Binding Protein ◽  
Salt Sensitive Hypertension ◽  
Prior Administration

Although sensitivity to high dietary NaCl is regarded to be a risk factor for cardiovascular disease, the causes of salt-sensitive hypertension remain elusive. Previously, we have shown that rats pretreated with subpressor doses of either ANG II or aldosterone (Aldo) show sensitized hypertensive responses to a mild pressor dose of ANG II when tested after an intervening delay. The current studies investigated whether such treatments will induce salt sensitivity. In studies employing an induction-delay-expression experimental design, male rats were instrumented for chronic mean arterial pressure (MAP) recording. In separate experiments, ANG II, Aldo, or vehicle was delivered either subcutaneously or intracerebroventricularly during the induction. There were no sustained differences in BP during the delay prior to being given 2% saline. While consuming 2% saline during the expression, both ANG II- and Aldo-pretreated rats showed significantly greater hypertension. When hexamethonium was used to assess autonomic control of MAP, no differences in the decrease of MAP in response to ganglionic blockade were detected during the induction. However, during the expression, the fall was greater in sensitized rats. In separate experiments, brain tissue that was collected at the end of delay showed increases in message or activation of putative markers of neuroplasticity (i.e., brain-derived neurotrophic factor, p38 mitogen-activated protein kinase, and cAMP response element-binding protein). These experiments demonstrate that prior administration of nonpressor doses of either ANG II or Aldo will induce salt sensitivity. Collectively, our findings indicate that treatment with subpressor doses of ANG II and Aldo initiate central neuroplastic changes that are involved in hypertension of different etiologies.

scholarly journals A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element-binding protein

2000 ◽  
Vol 350 (3) ◽  
pp. 717-722 ◽  
Author(s):  
Henri H. VERSTEEG ◽  
Evert NIJHUIS ◽  
Gijs R. VAN DEN BRINK ◽  
Maaike EVERTZEN ◽  
Gwenda N. PYNAERT ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
P38 Mapk ◽  
Protein Kinase B ◽  
Camp Response Element Binding ◽  
Mitogen Activated Protein Kinase ◽  
Camp Response Element ◽  
Response Element ◽  
Mitogen Activated Protein ◽  
Element Binding Protein

Assaying activation of signal transduction is laborious and does not allow the study of large numbers of samples, essential for high-throughput drug screens or for large groups of patients. Using phosphospecific antibodies, we have developed ELISA techniques enabling non-radioactive semi-quantitative assessment of the activation state of p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and the transcription factor cAMP-response-element-binding protein (CREB) in 96-well plates. This assay has been termed PACE (phosphospecific antibody cell-based ELISA) and was used successfully for both adherent and suspension cells. Various stimuli induced dose-dependent enzymic activity of which the kinetics closely correlated with those measured via classical methodology. Using PACE we have now characterized for the first time the concentration-dependent effects of various inflammatory prostaglandins on CREB phosphorylation in macrophages. PACE is a straightforward and novel technique enabling the large-scale analysis of signal transduction.

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