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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-3-20
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pubmed:abstractText |
Tin(Sn)-protoporphyrin is a potent competitive inhibitor of heme oxygenase and can also suppress naturally occurring or experimentally induced hyperbilirubinemia in animals. In this study we examined the plasma clearance of Sn-protoporphyrin, its persistence in tissues and the time course of heme oxygenase inhibition up to 7 days after administration of doses up to 50 mumol/kg b.w. to adult male rats. After s.c. doses the metalloporphyrin was rapidly and almost completely absorbed. Initial plasma clearance was log-linear with a T 1/2 of approximately 3 h after either i.v. or s.c. administration. Levels of Sn-protoporphyrin in most tissues rose during the first 2 h and persisted for up to 7 days. Concentrations were highest in kidney and liver, were considerably lower in spleen, lung, intestine, adrenal and testes, and as Sn-protoporphyrin concentrations in plasma declined, concentrations in these tissues eventually exceeded simultaneous plasma concentrations. This suggests a varying degree of uptake and binding of the metalloporphyrin in these tissues. There was little or no uptake of Sn-protoporphyrin in heart, brain and red cells. Markedly decreased heme oxygenase activity in liver, kidney and spleen persisted as did Sn-protoporphyrin up to 7 days. The total amount of Sn-protoporphyrin present in tissues and excreta was a fairly constant fraction of the dose (approximately 50%) at time intervals up to 7 days after injection. These results indicate that single doses of Sn-protoporphyrin are rapidly cleared from plasma and persist in tissues and potently inhibit heme oxygenase activity for prolonged periods.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Metalloporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Porphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/tin protoporphyrin IX
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-3565
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
228
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
327-33
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:6546399-Animals,
pubmed-meshheading:6546399-Heme Oxygenase (Decyclizing),
pubmed-meshheading:6546399-Kidney,
pubmed-meshheading:6546399-Kinetics,
pubmed-meshheading:6546399-Liver,
pubmed-meshheading:6546399-Male,
pubmed-meshheading:6546399-Metalloporphyrins,
pubmed-meshheading:6546399-Mixed Function Oxygenases,
pubmed-meshheading:6546399-Porphyrins,
pubmed-meshheading:6546399-Protoporphyrins,
pubmed-meshheading:6546399-Rats,
pubmed-meshheading:6546399-Rats, Inbred Strains,
pubmed-meshheading:6546399-Spectrometry, Fluorescence,
pubmed-meshheading:6546399-Spleen,
pubmed-meshheading:6546399-Time Factors,
pubmed-meshheading:6546399-Tissue Distribution
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pubmed:year |
1984
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pubmed:articleTitle |
Tissue distribution and disposition of tin-protoporphyrin, a potent competitive inhibitor of heme oxygenase.
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pubmed:publicationType |
Journal Article
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