Source:http://linkedlifedata.com/resource/pubmed/id/16259607
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9-10
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pubmed:dateCreated |
2005-11-1
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pubmed:abstractText |
We investigated the effect of heat shock on cytochrome P-450 activity in rat hepatocytes and report a significant, selective, and time-dependent enhancement of cytochrome P-450 activity in heatshocked hepatocytes. Stable long-term cultures of rat hepatocytes were heat shocked (42.5 degrees C) for 1 to 3 h and allowed to recover at 37 degrees C. Cytochrome P-450-dependent ethoxyresorufin O-dealkylase (EROD) and benzyloxyresorufin O-dealkylase (BROD) activities were measured up to 48 h after heat shock treatment. In general, the optimal heat shock exposure time was between 2 and 3 h. BROD activity (induced by sodium phenobarbital) increased approximately 6-fold in hepatocytes heat shocked for 3 h in comparison with hepatocytes maintained at 37 degrees C. EROD activity (induced by 3-methylcholanthrene) increased 2-fold on exposure to heat shock for 2 h. The expression of inducible heat shock proteins Hsp70 and Hsp32 was verified by Western immunoblot analyses. In the absence of the appropriate inducer, heat shock treatment did not enhance cytochrome P-450 activity. Furthermore, enhanced P-450 enzyme activity was delayed for heat-shocked hepatocytes. It is hypothesized that heat shock treatment attenuates the negative effects triggered by the addition of the toxic inducers and possibly stabilizes the levels of cytochrome P-450 proteins. These results suggest that heat shock treatment may be used to enhance the functionality of hepatocytes, specifically, in bioartificial liver assist devices.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Albumins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Urea
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pubmed:status |
MEDLINE
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pubmed:issn |
1076-3279
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1527-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16259607-Albumins,
pubmed-meshheading:16259607-Animals,
pubmed-meshheading:16259607-Blotting, Western,
pubmed-meshheading:16259607-Cell Culture Techniques,
pubmed-meshheading:16259607-Cells, Cultured,
pubmed-meshheading:16259607-Cytochrome P-450 Enzyme System,
pubmed-meshheading:16259607-DNA,
pubmed-meshheading:16259607-Enzyme Induction,
pubmed-meshheading:16259607-Female,
pubmed-meshheading:16259607-HSP70 Heat-Shock Proteins,
pubmed-meshheading:16259607-Heat-Shock Response,
pubmed-meshheading:16259607-Heme Oxygenase (Decyclizing),
pubmed-meshheading:16259607-Hepatocytes,
pubmed-meshheading:16259607-Nitric Oxide,
pubmed-meshheading:16259607-Rats,
pubmed-meshheading:16259607-Rats, Inbred Lew,
pubmed-meshheading:16259607-Time Factors,
pubmed-meshheading:16259607-Urea
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pubmed:articleTitle |
Selective enhancement of cytochrome p-450 activity in rat hepatocytes by in vitro heat shock.
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pubmed:affiliation |
Center for Engineering in Medicine, Massachusetts General Hospital, Harvard Medical School, and Shriners Hospital for Children, Boston, Massachusetts 02114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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