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rdf:type |
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lifeskim:mentions |
umls-concept:C0010453,
umls-concept:C0021289,
umls-concept:C0031469,
umls-concept:C0033634,
umls-concept:C0079281,
umls-concept:C0332282,
umls-concept:C0443199,
umls-concept:C0597298,
umls-concept:C0752312,
umls-concept:C1424650,
umls-concept:C1539079,
umls-concept:C1879547,
umls-concept:C1882687,
umls-concept:C1948023,
umls-concept:C2339371
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pubmed:issue |
52
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pubmed:dateCreated |
1995-1-30
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pubmed:abstractText |
The translocation of protein kinase C (PKC) isoforms PKC-alpha, PKC-delta, PKC-epsilon, and PKC-zeta from soluble to particulate fractions was studied in ventricular cardiomyocytes cultured from neonatal rats. Endothelin-1 (ET-1) caused a rapid ETA receptor-mediated translocation of PKC-delta and PKC-epsilon (complete in 0.5-1 min). By 3-5 min, both isoforms were returning to the soluble fraction, but a greater proportion of PKC-epsilon remained associated with the particulate fraction. The EC50 of translocation for PKC-delta was 11-15 nM ET-1 whereas that for PKC-epsilon was 1.4-1.7 nM. Phenylephrine caused a rapid translocation of PKC-epsilon (EC50 = 0.9 microM) but the proportion lost from the soluble fraction was less than with ET-1. Translocation of PKC-delta was barely detectable with phenylephrine. Neither agonist caused any consistent translocation of PKC-alpha or PKC-zeta. Activation of p42 and p44 mitogen-activated protein kinase (MAPK) by ET-1 or phenylephrine followed more slowly (complete in 3-5 min). Phosphorylation of p42-MAPK occurred simultaneously with its activation. The proportion of the total p42-MAPK pool phosphorylated in response to ET-1 (50%) was greater than with phenylephrine (20%). In addition to activation of MAPK, an unidentified p85 protein kinase was activated by ET-1 in the soluble fraction whereas an unidentified p58 protein kinase was activated in the particulate fraction.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylephrine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Endothelin,
http://linkedlifedata.com/resource/pubmed/chemical/cyclo(Trp-Asp-Pro-Val-Leu)
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32848-57
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7806510-Amino Acid Sequence,
pubmed-meshheading:7806510-Animals,
pubmed-meshheading:7806510-Animals, Newborn,
pubmed-meshheading:7806510-Biological Transport,
pubmed-meshheading:7806510-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:7806510-Cells, Cultured,
pubmed-meshheading:7806510-Endothelins,
pubmed-meshheading:7806510-Enzyme Activation,
pubmed-meshheading:7806510-Heart Ventricles,
pubmed-meshheading:7806510-Isoenzymes,
pubmed-meshheading:7806510-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:7806510-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:7806510-Mitogen-Activated Protein Kinases,
pubmed-meshheading:7806510-Molecular Sequence Data,
pubmed-meshheading:7806510-Peptides, Cyclic,
pubmed-meshheading:7806510-Phenylephrine,
pubmed-meshheading:7806510-Phosphatidylinositols,
pubmed-meshheading:7806510-Phosphorylation,
pubmed-meshheading:7806510-Protein Kinase C,
pubmed-meshheading:7806510-Protein-Tyrosine Kinases,
pubmed-meshheading:7806510-Rats,
pubmed-meshheading:7806510-Rats, Sprague-Dawley,
pubmed-meshheading:7806510-Receptors, Endothelin
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pubmed:year |
1994
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pubmed:articleTitle |
Differential activation of protein kinase C isoforms by endothelin-1 and phenylephrine and subsequent stimulation of p42 and p44 mitogen-activated protein kinases in ventricular myocytes cultured from neonatal rat hearts.
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pubmed:affiliation |
Department of Cardiac Medicine, University of London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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