Linked Life Data

8978332

Source:http://linkedlifedata.com/resource/pubmed/id/8978332

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-1-27
pubmed:abstractText
Many lines of evidence have suggested that angiotensin II (Ang II)plays an important role in cardiac hypertrophy. Ang II not only increases protein synthesis but also induces the reprogramming of gene expression in cultured cardiac myocytes. In the present study, to elucidate the mechanism by which Ang II regulates gene expression in cardiac myocytes, we examined whether Ang II activates c-Jun NH2-terminal kinase (JNK), which is a member of the mitogen-activated protein kinase family and activates the transcription factor, activator protein-1 (AP-1). The activity of JNK increased 5 minutes after the addition of Ang II, peaked at 20 minutes, and gradually decreased thereafter. Examination of the Ang II dose-response relation revealed detectable JNK activation at 10(-9) mol/L and maximal activation at 10(-6) mol/L. Ang II activated JNK through the AT1 receptor, and the activation was attenuated by the downregulation of protein kinase C or the chelation of intracellular Ca2+. Although the addition of either Ca2+ ionophore or phorbol ester resulted in little or no activation of JNK, simultaneous addition of both Ca2+ ionophore and phorbol ester markedly activated JNK. Slight expressions of the c-jun gene were observed in unstimulated cardiac myocytes, and Ang II increased expressions of the c-jun gene as well as the c-fos gene. Ang II increased transcription of the endothelin-1 gene through the AP-1 binding site. In conclusion, Ang II may activate JNK in cultured cardiac myocytes through an increase in intracellular Ca2+ and activation of protein kinase C, and the activated JNK may regulate gene expression by activating AP-1 during Ang II-induced cardiac hypertrophy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0009-7330
pubmed:author
pubmed:issnType
Print
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-46
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8978332-Angiotensin II, pubmed-meshheading:8978332-Animals, pubmed-meshheading:8978332-Animals, Newborn, pubmed-meshheading:8978332-Calcium, pubmed-meshheading:8978332-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:8978332-Cells, Cultured, pubmed-meshheading:8978332-Dose-Response Relationship, Drug, pubmed-meshheading:8978332-Gene Expression, pubmed-meshheading:8978332-Genes, fos, pubmed-meshheading:8978332-Genes, jun, pubmed-meshheading:8978332-JNK Mitogen-Activated Protein Kinases, pubmed-meshheading:8978332-Mitogen-Activated Protein Kinases, pubmed-meshheading:8978332-Myocardium, pubmed-meshheading:8978332-Promoter Regions, Genetic, pubmed-meshheading:8978332-Protein Kinase C, pubmed-meshheading:8978332-Rats, pubmed-meshheading:8978332-Rats, Wistar, pubmed-meshheading:8978332-Receptors, Angiotensin, pubmed-meshheading:8978332-Tetradecanoylphorbol Acetate, pubmed-meshheading:8978332-Time Factors
pubmed:year
1997
pubmed:articleTitle
Angiotensin II stimulates c-Jun NH2-terminal kinase in cultured cardiac myocytes of neonatal rats.
pubmed:affiliation
Department of Medicine III, University of Tokyo, School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't