Source:http://linkedlifedata.com/resource/pubmed/id/15474356
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2004-10-11
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| pubmed:abstractText |
Heme oxygenase-1 (HO-1) is induced in the CNS after hemorrhage, and may have an effect on injury to surrounding tissue. Hemin, the preferred substrate of HO, is a neurotoxin that is present in intracranial hematomas. In a prior study, we observed that HO inhibitors increased the vulnerability of cultured cortical astrocytes to heme-mediated oxidative injury. To investigate the effect of HO more specifically, we used an adenoviral vector encoding the human HO-1 gene to specifically increase HO-1 expression. Incubation with 100 MOI of the HO-1 adenovirus (Adv-HHO-1) for 24 h increased both HO-1 protein and HO activity; a control adenovirus lacking the HO-1 gene had no effect. Using a DNA probe that was specific for human HO-1, 80.5 +/- 7.2% of astrocytes were observed to be infected by in situ hybridization. The cell death produced by 30-60 microM hemin was significantly reduced by pretreatment with 100 MOI Adv-HHO-1, as assessed by LDH release, propidium iodide exclusion, and MTT reduction assay. The threefold increase in cell protein oxidation produced by hemin was also attenuated in cultures pretreated with Adv-HHO-1. These results support the hypothesis that HO-1 protects astrocytes from heme-mediated oxidative injury. Specifically increasing astrocytic HO-1 by gene transfer may have a beneficial effect on hemorrhagic CNS injury.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ferritins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/HMOX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hemin,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins
|
| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
|
| pubmed:issn |
0969-9961
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
17
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
179-87
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15474356-Adenoviridae,
pubmed-meshheading:15474356-Animals,
pubmed-meshheading:15474356-Astrocytes,
pubmed-meshheading:15474356-Cells, Cultured,
pubmed-meshheading:15474356-Corpus Striatum,
pubmed-meshheading:15474356-Drug Resistance,
pubmed-meshheading:15474356-Ferritins,
pubmed-meshheading:15474356-Gene Transfer Techniques,
pubmed-meshheading:15474356-Glutathione,
pubmed-meshheading:15474356-Heme Oxygenase (Decyclizing),
pubmed-meshheading:15474356-Heme Oxygenase-1,
pubmed-meshheading:15474356-Hemin,
pubmed-meshheading:15474356-Humans,
pubmed-meshheading:15474356-Membrane Proteins,
pubmed-meshheading:15474356-Mice,
pubmed-meshheading:15474356-Mice, Inbred Strains,
pubmed-meshheading:15474356-Oxidation-Reduction,
pubmed-meshheading:15474356-Oxidative Stress,
pubmed-meshheading:15474356-Polymerase Chain Reaction
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| pubmed:year |
2004
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| pubmed:articleTitle |
Adenoviral transfer of the heme oxygenase-1 gene protects striatal astrocytes from heme-mediated oxidative injury.
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| pubmed:affiliation |
Department of Emergency Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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