| pubmed-article:11007772 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0291573 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0225828 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:11007772 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:11007772 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:11007772 | pubmed:dateCreated | 2001-1-8 | lld:pubmed |
| pubmed-article:11007772 | pubmed:abstractText | Apoptosis of cardiac muscle cells contributes to the development of cardiomyopathy. Recent studies showed that insulin-like growth factor I (IGF-I) inhibits apoptosis of cardiac muscle cells and improves myocardial function in experimental heart failure. This study was carried out to elucidate the role of phosphatidylinositol 3-kinase (PI 3-kinase) in the anti-apoptotic actions of IGF-I in cardiomyocytes and to explore whether expression of constitutively active PI 3-kinase can inhibit apoptosis in cardiomyocytes. Apoptosis of primary cardiomyocytes was induced by doxorubicin treatment and serum withdrawal. Transduction of cardiomyocytes with constitutively active PI 3-kinase specifically lead to serine phosphorylation of Akt, whereas phosphorylation of IGF-I receptor, IRS1/2 and p44/42 mitogen-activated protein kinase were not increased. In the cardiomyocytes transduced with constitutively active PI 3-kinase, activation of the pro-apoptotic caspase 3 was attenuated and fragmentation of DNA was reduced. Preincubating cells with PI 3-kinase inhibitor LY294002 was associated with loss of anti-apoptotic actions of IGF-I and PI 3-kinase. Neither IGF-I nor constitutively active PI 3-kinase lead to serine phosphorylation of Bad, suggesting that the anti-apoptotic effects of PI 3-kinase are not mediated through Bad phosphorylation in cardiac muscle cells. To determine whether activation of caspase 3 is sufficient to induce apoptosis in cardiomyocytes, an engineered TAT-caspase 3 protein was introduced to cardiomyocytes. Significant reduction of cell viability occurred in the cardiomyocytes transduced with active caspase 3, indicating that activation of caspase 3 is sufficient to cause cardiomyocyte death. These findings indicate the existence of an IGF-I receptor-PI 3-kinase-caspase 3 pathway in cardiomyocytes that plays an important role in the anti-apoptotic actions of IGF-I in heart. Moreover, these data suggest that modulation of PI 3-kinase activities may represent a potential therapeutic strategy to counteract the occurrence of apoptosis in cardiomyopathy. | lld:pubmed |
| pubmed-article:11007772 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11007772 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11007772 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11007772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11007772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11007772 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11007772 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11007772 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:LeeW LWL | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:ChenDD | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:WuWW | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:DAWH THT | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:JannFF | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:WuY YYY | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:SharmaP MPM | lld:pubmed |
| pubmed-article:11007772 | pubmed:author | pubmed-author:WangP HPH | lld:pubmed |
| pubmed-article:11007772 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11007772 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:11007772 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:11007772 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11007772 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11007772 | pubmed:pagination | 40113-9 | lld:pubmed |
| pubmed-article:11007772 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:11007772 | pubmed:meshHeading | pubmed-meshheading:11007772... | lld:pubmed |
| pubmed-article:11007772 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11007772 | pubmed:articleTitle | Expression of constitutively active phosphatidylinositol 3-kinase inhibits activation of caspase 3 and apoptosis of cardiac muscle cells. | lld:pubmed |
| pubmed-article:11007772 | pubmed:affiliation | Department of Medicine and Biological Chemistry, Division of Endocrinology, Diabetes, and Metabolism, University of California, Irvine, California 92697, USA. | lld:pubmed |
| pubmed-article:11007772 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11007772 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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