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Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury

Skin heme oxygenase is locally elevated by stimuli such as tissue injury and injections of whole blood, myoglobin, and hematin. The enzyme activity is also increased at the proximity of the injection site of chemicals such as cobalt and cobalt-protoporphyrin-IX (cobalt- heme). Protoporphyrin-IX, the...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1977
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2180622/
https://www.ncbi.nlm.nih.gov/pubmed/870606
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description Skin heme oxygenase is locally elevated by stimuli such as tissue injury and injections of whole blood, myoglobin, and hematin. The enzyme activity is also increased at the proximity of the injection site of chemicals such as cobalt and cobalt-protoporphyrin-IX (cobalt- heme). Protoporphyrin-IX, the tetrapyrrole nucleus of type-b heme compounds, was ineffective in altering the enzyme activity in vivo. The developmental pattern of heme oxygenase in skin was compared to that of the enzyme in liver. The enzyme activity in both organs was greatest during the 1st postpartum wk and declined to adult levels after 2 wk. The physiological implications of the increased activity of skin heme oxygenase are discussed, and it is concluded that the activity of the hepatic heme oxygenase system and that of the skin are regulated by the same mechanism.
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spelling pubmed-21806222008-04-17 Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury J Exp Med Articles Skin heme oxygenase is locally elevated by stimuli such as tissue injury and injections of whole blood, myoglobin, and hematin. The enzyme activity is also increased at the proximity of the injection site of chemicals such as cobalt and cobalt-protoporphyrin-IX (cobalt- heme). Protoporphyrin-IX, the tetrapyrrole nucleus of type-b heme compounds, was ineffective in altering the enzyme activity in vivo. The developmental pattern of heme oxygenase in skin was compared to that of the enzyme in liver. The enzyme activity in both organs was greatest during the 1st postpartum wk and declined to adult levels after 2 wk. The physiological implications of the increased activity of skin heme oxygenase are discussed, and it is concluded that the activity of the hepatic heme oxygenase system and that of the skin are regulated by the same mechanism. The Rockefeller University Press 1977-04-01 /pmc/articles/PMC2180622/ /pubmed/870606 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title_full Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title_fullStr Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title_full_unstemmed Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title_short Bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
title_sort bile pigment formation by skin heme oxygenase: studies on the response of the enzyme to heme compounds and tissue injury
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2180622/
https://www.ncbi.nlm.nih.gov/pubmed/870606