| pubmed-article:14962831 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C0109317 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1705767 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C0225828 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C0031686 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1120843 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1370600 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1366882 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1150579 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1333340 | lld:lifeskim |
| pubmed-article:14962831 | lifeskim:mentions | umls-concept:C1705791 | lld:lifeskim |
| pubmed-article:14962831 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14962831 | pubmed:dateCreated | 2004-5-18 | lld:pubmed |
| pubmed-article:14962831 | pubmed:abstractText | Mitogen-activated protein kinases (MAPKs) play different regulatory roles in signaling oxidative stress-induced apoptosis in cardiac ventricular myocytes. The regulation and functional role of cross-talk between p38 MAPK and extracellular signal-regulated kinase (ERK) pathways were investigated in cardiac ventricular myocytes in the present study. We demonstrated that inhibition of p38 MAPK with SB-203580 and SB-239063 enhanced H(2)O(2)-stimulated ERK phosphorylation, whereas preactivation of p38 MAPK with sodium arsenite reduced H(2)O(2)-stimulated ERK phosphorylation. In addition, pretreatment of cells with the protein phosphatase 2A (PP2A) inhibitors okadaic acid and fostriecin increased basal and H(2)O(2)-stimulated ERK phosphorylation. We also found that PP2A coimmunoprecipitated with ERK and MAPK/ERK (MEK) in cardiac ventricular myocytes, and H(2)O(2) increased the ERK-associated PP2A activity that was blocked by inhibition of p38 MAPK. Finally, H(2)O(2)-induced apoptosis was attenuated by p38 MAPK or PP2A inhibition, whereas it was enhanced by MEK inhibition. Thus the present study demonstrated that p38 MAPK activation decreases H(2)O(2)-induced ERK activation through a PP2A-dependent mechanism in cardiac ventricular myocytes. This represents a novel cellular mechanism that allows for interaction of two opposing MAPK pathways and fine modulation of apoptosis during oxidative stress. | lld:pubmed |
| pubmed-article:14962831 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14962831 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14962831 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14962831 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14962831 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14962831 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:14962831 | pubmed:issn | 0363-6135 | lld:pubmed |
| pubmed-article:14962831 | pubmed:author | pubmed-author:LiuQinghangQ | lld:pubmed |
| pubmed-article:14962831 | pubmed:author | pubmed-author:HofmannPolly... | lld:pubmed |
| pubmed-article:14962831 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14962831 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:14962831 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14962831 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14962831 | pubmed:pagination | H2204-12 | lld:pubmed |
| pubmed-article:14962831 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:14962831 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14962831 | pubmed:articleTitle | Protein phosphatase 2A-mediated cross-talk between p38 MAPK and ERK in apoptosis of cardiac myocytes. | lld:pubmed |
| pubmed-article:14962831 | pubmed:affiliation | Dept. of Physiology, University of Tennessee Health Science Center, 894 Union Avenue, Memphis, TN 38163, USA. | lld:pubmed |
| pubmed-article:14962831 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14962831 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:14962831 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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