Linked Life Data

11810220

Source:http://linkedlifedata.com/resource/pubmed/id/11810220

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-1-25
pubmed:abstractText
The study addressed the question of why in adult ventricular rat cardiomyocytes ERK activation is required for the hypertrophic stimulation caused by angiotensin II but not in the case of alpha-adrenoceptor stimulation. We therefore compared in the same culture system the intracellular signaling steps that are involved in inducing the hypertrophic growth evoked by stimulating either of these two receptors. alpha-Adrenoceptor stimulation strongly increased protein synthesis ([14C]phenylalanine incorporation) up to 53% in a PKC- and p70s6k-dependent, but ERK-independent way. In contrast, angiotensin II increased protein synthesis less efficiently (by 23%), in a PKC-, p70s6k-, but ERK-dependent way. The kinetics of activation for ERK were different for the two hypertrophic stimuli: alpha-adrenoceptor stimulation caused a rapid and transient activation, but angiotensin II caused a rapid and sustained activation. In contrast to alpha-adrenoceptor stimulation, angiotensin II activated calcium-independent PKC isoforms but not calcium-dependent PKC isoforms. In conclusion, ERK activation by angiotensin II is sustained and leads to an increase in protein synthesis on adult ventricular cardiomyocytes, but ERK activation by alpha-adrenoceptor stimulation is transient and not involved in hypertrophic growth responsiveness. The ERK-dependent pathway seems to be less efficient than ERK-independent pathways. The difference in the hypertrophic responsiveness of cardiomyocytes exposed to either of the two stimuli may be explained by the activation of different PKC isoform types.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0031-6768
pubmed:author
pubmed:issnType
Print
pubmed:volume
443
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
483-90
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11810220-Angiotensin II, pubmed-meshheading:11810220-Animals, pubmed-meshheading:11810220-Carbon Radioisotopes, pubmed-meshheading:11810220-Cardiomegaly, pubmed-meshheading:11810220-Cells, Cultured, pubmed-meshheading:11810220-Heart Ventricles, pubmed-meshheading:11810220-MAP Kinase Signaling System, pubmed-meshheading:11810220-Male, pubmed-meshheading:11810220-Mitogen-Activated Protein Kinases, pubmed-meshheading:11810220-Muscle Fibers, Skeletal, pubmed-meshheading:11810220-Myocardium, pubmed-meshheading:11810220-Phenylalanine, pubmed-meshheading:11810220-Phenylephrine, pubmed-meshheading:11810220-Protein Kinase C, pubmed-meshheading:11810220-Rats, pubmed-meshheading:11810220-Rats, Wistar, pubmed-meshheading:11810220-Ribosomal Protein S6 Kinases, pubmed-meshheading:11810220-Vasoconstrictor Agents
pubmed:year
2002
pubmed:articleTitle
Specific role for the extracellular signal-regulated kinase pathway in angiotensin II- but not phenylephrine-induced cardiac hypertrophy in vitro.
pubmed:affiliation
Physiologisches Institut, Justus-Liebig-Universität Giessen, Aulweg 129, 35392 Giessen, Germany.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't