| pubmed-article:12876275 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12876275 | lifeskim:mentions | umls-concept:C0011065 | lld:lifeskim |
| pubmed-article:12876275 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:12876275 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:12876275 | lifeskim:mentions | umls-concept:C1291081 | lld:lifeskim |
| pubmed-article:12876275 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12876275 | pubmed:dateCreated | 2003-7-23 | lld:pubmed |
| pubmed-article:12876275 | pubmed:abstractText | Mitochondrial release of cytochrome c in apoptotic cells activates caspases, which execute apoptotic cell death. However, the events themselves that culminate in caspase activation can have deleterious effects because caspase inhibitor-saved cells ultimately die in a caspase-independent manner. To determine what events may underlie this form of cell death, we examined bioenergetic changes in sympathetic neurons deprived of NGF in the presence of a broad-spectrum caspase inhibitor, boc-aspartyl-(OMe)-fluoromethylketone. Here, we report that NGF-deprived, boc-aspartyl-(OMe)-fluoromethylketone-saved neurons rely heavily on glycolysis for ATP generation and for survival. Second, the activity of F0F1 contributes to caspase-independent death, but has only a minor role in the maintenance of mitochondrial membrane potential, which is maintained primarily by electron transport. Third, permeability transition pore inhibition by cyclosporin A attenuates NGF deprivation-induced loss of mitochondrial proteins, suggesting that permeability transition pore opening may have a function in regulating the degradation of mitochondria after cytochrome c release. Identification of changes in caspase inhibitor-saved cells may provide the basis for rational strategies to augment the effectiveness of the therapeutic use of postmitochondrial interventions. | lld:pubmed |
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| pubmed-article:12876275 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12876275 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12876275 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12876275 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12876275 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12876275 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:12876275 | pubmed:author | pubmed-author:JohnsonEugene... | lld:pubmed |
| pubmed-article:12876275 | pubmed:author | pubmed-author:SchmidtRobert... | lld:pubmed |
| pubmed-article:12876275 | pubmed:author | pubmed-author:ChangLouis... | lld:pubmed |
| pubmed-article:12876275 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12876275 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:12876275 | pubmed:volume | 162 | lld:pubmed |
| pubmed-article:12876275 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12876275 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12876275 | pubmed:pagination | 245-56 | lld:pubmed |
| pubmed-article:12876275 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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