| pubmed-article:11158304 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11158304 | lifeskim:mentions | umls-concept:C0225828 | lld:lifeskim |
| pubmed-article:11158304 | lifeskim:mentions | umls-concept:C0751984 | lld:lifeskim |
| pubmed-article:11158304 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:11158304 | lifeskim:mentions | umls-concept:C1419227 | lld:lifeskim |
| pubmed-article:11158304 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11158304 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11158304 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11158304 | pubmed:abstractText | Small guanine nucleotide-binding proteins of the Ras and Rho (Rac, Cdc42, and Rho) families have been implicated in cardiac myocyte hypertrophy, and this may involve the extracellular signal-related kinase (ERK), c-Jun N-terminal kinase (JNK), and/or p38 mitogen-activated protein kinase (MAPK) cascades. In other systems, Rac and Cdc42 have been particularly implicated in the activation of JNKs and p38-MAPKs. We examined the activation of Rho family small G proteins and the regulation of MAPKs through Rac1 in cardiac myocytes. Endothelin 1 and phenylephrine (both hypertrophic agonists) induced rapid activation of endogenous Rac1, and endothelin 1 also promoted significant activation of RhoA. Toxin B (which inactivates Rho family proteins) attenuated the activation of JNKs by hyperosmotic shock or endothelin 1 but had no effect on p38-MAPK activation. Toxin B also inhibited the activation of the ERK cascade by these stimuli. In transfection experiments, dominant-negative N17Rac1 inhibited activation of ERK by endothelin 1, whereas activated V12Rac1 cooperated with c-Raf to activate ERK. Rac1 may stimulate the ERK cascade either by promoting the phosphorylation of c-Raf or by increasing MEK1 and/or -2 association with c-Raf to facilitate MEK1 and/or -2 activation. In cardiac myocytes, toxin B attenuated c-Raf(Ser-338) phosphorylation (50 to 70% inhibition), but this had no effect on c-Raf activity. However, toxin B decreased both the association of MEK1 and/or -2 with c-Raf and c-Raf-associated ERK-activating activity. V12Rac1 cooperated with c-Raf to increase expression of atrial natriuretic factor (ANF), whereas N17Rac1 inhibited endothelin 1-stimulated ANF expression, indicating that the synergy between Rac1 and c-Raf is potentially physiologically important. We conclude that activation of Rac1 by hypertrophic stimuli contributes to the hypertrophic response by modulating the ERK and/or possibly the JNK (but not the p38-MAPK) cascades. | lld:pubmed |
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| pubmed-article:11158304 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11158304 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11158304 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11158304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11158304 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11158304 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11158304 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:SugdenP HPH | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:MarshallCC | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:AktoriesKK | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:ClerkAA | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:MaraisRR | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:FullerS JSJ | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:SahayUU | lld:pubmed |
| pubmed-article:11158304 | pubmed:author | pubmed-author:PhamF HFH | lld:pubmed |
| pubmed-article:11158304 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11158304 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11158304 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11158304 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11158304 | pubmed:pagination | 1173-84 | lld:pubmed |
