Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
23
|
| pubmed:dateCreated |
1997-6-26
|
| pubmed:abstractText |
The role of heme oxygenase (HO)-1 was evaluated in the oxygen-resistant hamster fibroblast cell line, O2R95, which moderately overexpress HO when compared with the parental cell line, HA-1. To suppress HO-1 expression, O2R95 were transfected with HO-1 antisense oligonucleotide or treated with tin-mesoporphyrin (SnMP). To increase HO-1 expression, cells were transfected with HO-1 cDNA in a pRC/cytomegalovirus (CMV) vector. All cells were challenged with a 48-h exposure to 95% O2 (hyperoxia). When HO activity was suppressed, O2R95 cells had significantly decreased cell viability, increased susceptibility to lipid peroxidation, and increased protein oxidation in hyperoxia. In contrast, further overexpression of HO-1 did not improve resistance to oxygen toxicity. Antisense-transfected cells and SnMP-treated cells with lowered HO activity showed increased levels of cellular heme compared with controls. In the HO-1 cDNA-transfected O2R95 cells, cellular heme was lowered compared with controls; however, cellular redox active iron levels were increased. We conclude that HO mediates cytoprotection to oxygen toxicity within a narrow range of expression. We speculate that this protective effect may be mediated in part through increased metabolism of the pro-oxidant heme but that higher levels of HO activity obviate protection by increased redox active iron release.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tin mesoporphyrin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
6
|
| pubmed:volume |
272
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14937-42
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9169465-Animals,
pubmed-meshheading:9169465-Antioxidants,
pubmed-meshheading:9169465-Cell Line,
pubmed-meshheading:9169465-Cell Survival,
pubmed-meshheading:9169465-Cricetinae,
pubmed-meshheading:9169465-Cytomegalovirus,
pubmed-meshheading:9169465-Drug Resistance,
pubmed-meshheading:9169465-Enzyme Inhibitors,
pubmed-meshheading:9169465-Fibroblasts,
pubmed-meshheading:9169465-Genetic Vectors,
pubmed-meshheading:9169465-Heme Oxygenase (Decyclizing),
pubmed-meshheading:9169465-Heme Oxygenase-1,
pubmed-meshheading:9169465-Kinetics,
pubmed-meshheading:9169465-Lipid Peroxidation,
pubmed-meshheading:9169465-Metalloporphyrins,
pubmed-meshheading:9169465-Oligonucleotides, Antisense,
pubmed-meshheading:9169465-Oxidative Stress,
pubmed-meshheading:9169465-Oxygen,
pubmed-meshheading:9169465-Recombinant Proteins,
pubmed-meshheading:9169465-Transfection
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Heme oxygenase-mediated resistance to oxygen toxicity in hamster fibroblasts.
|
| pubmed:affiliation |
Department of Pediatrics, Stanford University School of Medicine, Stanford, California 94305, USA. mn.phd@forsythe.stanford.edu
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|