pubmed-article:7507104 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0079281 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0225828 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0016026 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0020564 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C1158478 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C2611812 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C1522538 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C1705422 | lld:lifeskim |
pubmed-article:7507104 | lifeskim:mentions | umls-concept:C1707310 | lld:lifeskim |
pubmed-article:7507104 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7507104 | pubmed:dateCreated | 1994-2-22 | lld:pubmed |
pubmed-article:7507104 | pubmed:abstractText | Maximally effective concentrations of endothelin-1 (ET-1), acidic FGF (aFGF), or 12-O-tetradecanoylphorbol-13-acetate (TPA) activated mitogen-activated protein kinase (MAPK) by 3-4-fold in crude extracts of myocytes cultured from neonatal rat heart ventricles. Maximal activation was achieved after 5 min. Thereafter, MAPK activity stimulated by ET-1 or aFGF declined to control values within 1-2 h, whereas activation by TPA was more sustained. Two peaks of MAPK activity (a 42- and a 44-kDa MAPK) were resolved in cells exposed to ET-1 or aFGF by fast protein liquid chromatography on a Mono Q column. One major and one minor peak of MAPK kinase (MAPKK) was stimulated by ET-1 or aFGF. Cardiac myocytes expressed protein kinase C (PKC)-alpha, -delta, -epsilon and -zeta as shown immunoblotting. Exposure to 1 microM TPA for 24 h down-regulated PKC-alpha, -delta, and -epsilon, but not PKC-zeta. This maneuver wholly abolished the activation of MAPK on re-exposure to TPA but did not affect the response to aFGF. The effect of ET-1 was partially down-regulated. ET-1 stimulated phospho[3H]inositide hydrolysis 18-fold, whereas aFGF stimulated by only 30%. Agonists which initially utilize dissimilar signaling pathways may therefore converge at the level of MAPKK/MAPK and this may be relevant to the hypertrophic response of the heart. | lld:pubmed |
pubmed-article:7507104 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507104 | pubmed:language | eng | lld:pubmed |
pubmed-article:7507104 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507104 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7507104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507104 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7507104 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7507104 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:SugdenP HPH | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:MarshallC JCJ | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:ParkerP JPJ | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:ClerkAA | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:LazouAA | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:BogoyevitchM... | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:GlennonP EPE | lld:pubmed |
pubmed-article:7507104 | pubmed:author | pubmed-author:AnderssonM... | lld:pubmed |
pubmed-article:7507104 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7507104 | pubmed:day | 14 | lld:pubmed |
pubmed-article:7507104 | pubmed:volume | 269 | lld:pubmed |
pubmed-article:7507104 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7507104 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7507104 | pubmed:pagination | 1110-9 | lld:pubmed |
pubmed-article:7507104 | pubmed:dateRevised | 2010-8-25 | lld:pubmed |
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pubmed-article:7507104 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7507104 | pubmed:articleTitle | Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy. | lld:pubmed |
pubmed-article:7507104 | pubmed:affiliation | Department of Cardiac Medicine, National Heart and Lung Institute, University of London, United Kingdom. | lld:pubmed |
pubmed-article:7507104 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7507104 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:7507104 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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