Source:http://linkedlifedata.com/resource/pubmed/id/14624451
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2003-11-18
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pubmed:abstractText |
The function of bcl-2 in preventing cell death is well known, but the mechanisms whereby bcl-2 functions are not well characterized. One mechanism whereby bcl-2 is thought to function is by alleviating the effects of oxidative stress upon the cell. To examine whether Bcl-2 can protect cells against oxidative injury resulting from post-hypoxic reoxygenation (H/R), we subjected rat fibroblasts Rat-1 and their bcl-2 transfectants b5 to hypoxia (5% CO2, 95% N2) followed by reoxygenation (5% CO2, 95% air). The bcl-2 transfectants exhibited the cell viability superior to that of their parent non-transfectants upon treatment with reoxygenation after 24-, 48-, or 72-h hypoxia, but not upon normoxic serum-deprivation or upon serum-supplied hypoxic treatment alone. Thus bcl-2 transfection can prevent cell death of some types, which occurred during H/R but yet not appreciably until termination of hypoxia. The time-sequential events of H/R-induced cell death were shown to be executed via (1) reactive oxygen species (ROS) production at 1-12 h after H/R, (2) activation of caspases-1 and -3, at 1-3 h and 3-6 h after H/R, respectively, and (3) loss of mitochondrial membrane potential (DeltaPsi) at 3-12 h after H/R. These cell death-associated events were prevented entirely except caspase-1 activation by bcl-2 transfection, and were preceded by Bcl-2 upregulation which was executed as early as at 0-1 h after H/R for the bcl-2 transfectants but not their non-transfected counterpart cells. Thus upregulation of Bcl-2 proteins may play a role in prevention of H/R-induced diminishment of cell viability, but may be executed not yet during hypoxia itself and be actually operated as promptly as ready to go immediately after beginning of H/R, resulting in cytoprotection through blockage of either ROS generation, caspase-3 activation, or DeltaPsi decline.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0730-2312
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2003 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
914-24
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pubmed:meshHeading |
pubmed-meshheading:14624451-Animals,
pubmed-meshheading:14624451-Apoptosis,
pubmed-meshheading:14624451-Caspases,
pubmed-meshheading:14624451-Cell Hypoxia,
pubmed-meshheading:14624451-Cell Survival,
pubmed-meshheading:14624451-Cells, Cultured,
pubmed-meshheading:14624451-Enzyme Activation,
pubmed-meshheading:14624451-Fibroblasts,
pubmed-meshheading:14624451-Oxidative Stress,
pubmed-meshheading:14624451-Oxygen,
pubmed-meshheading:14624451-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:14624451-Rats,
pubmed-meshheading:14624451-Reactive Oxygen Species,
pubmed-meshheading:14624451-Transfection,
pubmed-meshheading:14624451-Up-Regulation
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pubmed:year |
2003
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pubmed:articleTitle |
Bcl-2 prevents hypoxia/reoxygenation-induced cell death through suppressed generation of reactive oxygen species and upregulation of Bcl-2 proteins.
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pubmed:affiliation |
Division of Cell Biochemistry, Hiroshima Prefectural University School of BioSciences, Shobara, Hiroshima 727-0023, Japan.
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pubmed:publicationType |
Journal Article
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