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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-11-16
pubmed:abstractText
In this study, we investigated the mechanisms through which norepinephrine (NE) regulates MAPK phosphatase-1 (MKP-1) expression in rat pinealocytes. Stimulation with NE (a mixed alpha- and beta-adrenergic agonist) caused a rapid increase in MKP-1 mRNA and protein that peaked around 1 h post stimulation, and the response was sustained for at least 4 h. Selective activation of beta-adrenergic receptors with isoproterenol for 1 h caused a similar increase in MKP-1 mRNA and protein as observed with NE, but at 3 h, the isoproterenol response was much lower relative to NE. In contrast, selective activation of alpha-adrenergic receptors caused only small increases in MKP-1 mRNA and protein and appeared to function primarily in prolonging the beta-adrenergic-stimulated responses. In NE-stimulated pinealocytes, blockade of beta-adrenergic receptors caused a rapid reduction in MKP-1 mRNA, but it had a minimal effect on MKP-1 protein. In contrast, blockade of alpha-adrenergic receptors specifically reduced NE-induced MKP-1 protein but not mRNA. At the postreceptor level, treatment with dibutyryl cAMP caused parallel increases in MKP-1 mRNA and protein. However, treatment with a protein kinase C activator caused a significant increase in MKP-1 protein but had little effect on MKP-1 mRNA. Together, these results suggest that, in rat pinealocytes, NE activates the beta-adrenergic receptor --> protein kinase A pathway to induce transcription and translation of MKP-1 expression and the alpha-adrenergic receptor --> protein kinase C pathway to prolong the stimulated responses through increased stability of the MKP-1 protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dual Specificity Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Dusp1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta, http://linkedlifedata.com/resource/pubmed/chemical/Sympathomimetics
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
145
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5723-33
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15358679-Animals, pubmed-meshheading:15358679-Cell Cycle Proteins, pubmed-meshheading:15358679-Cells, Cultured, pubmed-meshheading:15358679-Dual Specificity Phosphatase 1, pubmed-meshheading:15358679-Gene Expression Regulation, Enzymologic, pubmed-meshheading:15358679-Immediate-Early Proteins, pubmed-meshheading:15358679-MAP Kinase Signaling System, pubmed-meshheading:15358679-Male, pubmed-meshheading:15358679-Norepinephrine, pubmed-meshheading:15358679-Phosphoprotein Phosphatases, pubmed-meshheading:15358679-Pineal Gland, pubmed-meshheading:15358679-Protein Phosphatase 1, pubmed-meshheading:15358679-Protein Tyrosine Phosphatases, pubmed-meshheading:15358679-RNA, Messenger, pubmed-meshheading:15358679-Rats, pubmed-meshheading:15358679-Rats, Sprague-Dawley, pubmed-meshheading:15358679-Receptors, Adrenergic, alpha, pubmed-meshheading:15358679-Receptors, Adrenergic, beta, pubmed-meshheading:15358679-Sympathomimetics
pubmed:year
2004
pubmed:articleTitle
Norepinephrine induction of mitogen-activated protein kinase phosphatase-1 expression in rat pinealocytes: distinct roles of alpha- and beta-adrenergic receptors.
pubmed:affiliation
Department of Physiology, Faculty of Medicine, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't