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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1996-3-12
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pubmed:abstractText |
The ability of 3,5,3'-triiodothyronine (T3) and cobalt-protoporphyrin LX (CoPP) to alter the levels of the cytochrome P-450 isoforms, CYP3A2, CYP2E1, CYP2B1 and CYP2B2, was examined in vitro in thyroidectomized adult male rats. With the exception of CYP2B2, CoPP administration resulted in a decline in each of the cytochrome P450 isoforms examined. The effects of T3 administration on immunoreactive levels of cytochrome P-450 were also examined in the liver of thyroidectomized rats. T3 treatment produced a marked depletion in all four cytochrome P-450 isoforms examined. Moreover, this T3-mediated depletion of hepatic cytochrome P-450 occurred in the absence of elevated heme oxygenase levels but in the presence of increased delta-aminolevulinate synthase activity. Thus, CoPP and T3 appear capable of producing isoform-specific downregulation of cytochrome P-450 in the liver of thyroidectomized rats. Based on relative levels of immunoreactive protein, the phenobarbital-inducible isoforms, CYP2B1 and CYP2B2, are most susceptible to T3-mediated suppression. Evidence is presented to suggest that these agents elicit these effects by entirely different mechanisms.
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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/5-Aminolevulinate Synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phenobarbital,
http://linkedlifedata.com/resource/pubmed/chemical/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Triiodothyronine,
http://linkedlifedata.com/resource/pubmed/chemical/cobaltiprotoporphyrin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0031-7012
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
254-62
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8577819-5-Aminolevulinate Synthetase,
pubmed-meshheading:8577819-Animals,
pubmed-meshheading:8577819-Blotting, Western,
pubmed-meshheading:8577819-Cytochrome P-450 Enzyme System,
pubmed-meshheading:8577819-Down-Regulation,
pubmed-meshheading:8577819-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8577819-Enzyme Induction,
pubmed-meshheading:8577819-Heme Oxygenase (Decyclizing),
pubmed-meshheading:8577819-Isoenzymes,
pubmed-meshheading:8577819-Liver,
pubmed-meshheading:8577819-Male,
pubmed-meshheading:8577819-Phenobarbital,
pubmed-meshheading:8577819-Protoporphyrins,
pubmed-meshheading:8577819-Rats,
pubmed-meshheading:8577819-Rats, Sprague-Dawley,
pubmed-meshheading:8577819-Thyroidectomy,
pubmed-meshheading:8577819-Triiodothyronine
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pubmed:year |
1995
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pubmed:articleTitle |
Depletion of cytochrome P-450 by thyroid hormone and cobalt-protoporphyrin IX in rat liver: evidence that susceptibility varies among forms of the heme protein.
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pubmed:affiliation |
Department of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut, Storrs 06268, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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