Source:http://linkedlifedata.com/resource/pubmed/id/10671549
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2000-3-21
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| pubmed:abstractText |
Nitric oxide (NO) challenge to human neuroblastoma cells (SH-SY5Y) ultimately results in apoptosis. Tumor suppressor protein p53 and cell cycle inhibitor p21 accumulate as an early sign of S-nitrosoglutathione-mediated toxicity. Cytochrome c release from mitochondria and caspase 3 activation also occurred. Cells transfected with either wild type (WT) or mutant (G93A) Cu, Zn-superoxide dismutase (Cu,Zn-SOD) produced comparable amounts of nitrite/nitrate but showed different degree of apoptosis. G93A cells were the most affected and WT cells the most protected; however, Cu, Zn-SOD content of these two cell lines was 2-fold the SH-SY5Y cells under both resting and treated conditions. We linked decreased susceptibility of the WT cells to higher and more stable Bcl-2 and decreased reactive oxygen species. Conversely, we linked G93A susceptibility to increased reactive oxygen species production since simultaneous administration of S-nitrosoglutathione and copper chelators protects from apoptosis. Furthermore, G93A cells showed a significant decrease of Bcl-2 expression and, as target of NO-derived radicals, showed lower cytochrome c oxidase activity. These results demonstrate that resistance to NO-mediated apoptosis is strictly related to the level and integrity of Cu,Zn-SOD and that the balance between reactive nitrogen and reactive oxygen species regulates neuroblastoma apoptosis.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Protein p21(ras),
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/S-Nitrosoglutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
18
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| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5065-72
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10671549-Amyotrophic Lateral Sclerosis,
pubmed-meshheading:10671549-Apoptosis,
pubmed-meshheading:10671549-Caspases,
pubmed-meshheading:10671549-Cytochrome c Group,
pubmed-meshheading:10671549-Down-Regulation,
pubmed-meshheading:10671549-Enzyme Activation,
pubmed-meshheading:10671549-Glutathione,
pubmed-meshheading:10671549-Humans,
pubmed-meshheading:10671549-Neurons,
pubmed-meshheading:10671549-Nitric Oxide,
pubmed-meshheading:10671549-Nitroso Compounds,
pubmed-meshheading:10671549-Oncogene Protein p21(ras),
pubmed-meshheading:10671549-Oxidative Stress,
pubmed-meshheading:10671549-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10671549-S-Nitrosoglutathione,
pubmed-meshheading:10671549-Superoxide Dismutase,
pubmed-meshheading:10671549-Tumor Cells, Cultured,
pubmed-meshheading:10671549-Tumor Suppressor Protein p53
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| pubmed:year |
2000
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| pubmed:articleTitle |
Cu,Zn-superoxide dismutase-dependent apoptosis induced by nitric oxide in neuronal cells.
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| pubmed:affiliation |
Department of Biomedical Sciences, University of Chieti "G. D'Annunzio," via dei Vestini, 66100 Chieti, Italy. Ciriolo@bio.uniroma2.it
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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