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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1982-6-24
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pubmed:abstractText |
The induction of heme oxygenase (EC 1.14.99.3) in response to various metal treatments was investigated in monolayer cultures of chick embryo liver cells maintained in a chemically defined serum-free medium. The most potent heme oxygenase-inducing action was exhibited by CO2+, Cd2+, Sb3+, As3+, and Au1+ followed by lesser induction observed with Cu2+, Fe2+, and Fe3+. Mn2+, Ni2+, Se4+, Sn2+, and Zn2+ were without effect. In contrast to the marked inducing effect of Co2+ on heme oxygenase, Co-protoporphyrin IX decreased the enzyme activity in a dose-dependent manner. Addition of Zn2+ (20 microM) to Co2+-treated liver cell cultures revealed a striking ability of Zn2+ to block completely Co2+-induced heme oxygenase. Simultaneous addition of Mn2+ (50 microM) to Co2+-treated cells also blocked Co2+-induced heme oxygenase (approximately 50%). These findings in tissue culture confirm those made earlier in whole animals (Drummond, G. S., and Kappas, A. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 5331-5335) and indicate that these effects of Zn2+ and Mn2+ are exerted directly in liver cells. Addition of cysteine (400 microM) to the cultures also inhibited heme oxygenase induction by Co2+ substantially. Cycloheximide and actinomycin D blocked the induction of heme oxygenase, indicating that increased heme oxygenase activity by metal treatment is dependent on fresh RNA and protein synthesis. The half-life of the enzyme was calculated to be approximately 15 h after treatment with cycloheximide. These findings provide further evidence that metal ions can regulate heme oxygenase synthesis directly in isolated liver cells and that the metal-metal interactions which lead to blockade of the enzyme induction do not involve extrahepatic tissues.
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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/Antimony,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenic,
http://linkedlifedata.com/resource/pubmed/chemical/Cadmium,
http://linkedlifedata.com/resource/pubmed/chemical/Cobalt,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Gold,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4806-11
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6896052-Animals,
pubmed-meshheading:6896052-Antimony,
pubmed-meshheading:6896052-Arsenic,
pubmed-meshheading:6896052-Cadmium,
pubmed-meshheading:6896052-Cells, Cultured,
pubmed-meshheading:6896052-Chick Embryo,
pubmed-meshheading:6896052-Cobalt,
pubmed-meshheading:6896052-Copper,
pubmed-meshheading:6896052-Enzyme Induction,
pubmed-meshheading:6896052-Gold,
pubmed-meshheading:6896052-Heme Oxygenase (Decyclizing),
pubmed-meshheading:6896052-Iron,
pubmed-meshheading:6896052-Kinetics,
pubmed-meshheading:6896052-Liver,
pubmed-meshheading:6896052-Manganese,
pubmed-meshheading:6896052-Metals,
pubmed-meshheading:6896052-Mixed Function Oxygenases,
pubmed-meshheading:6896052-Zinc
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pubmed:year |
1982
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pubmed:articleTitle |
Metal ion-mediated regulation of heme oxygenase induction in cultured avian liver cells.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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