دورية أكاديمية
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Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: evidence against a stress-mediated response.

التفاصيل البيبلوغرافية
العنوان: Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: evidence against a stress-mediated response.
المؤلفون: Cable EE; Department of Medicine, University of Massachusetts Medical Center, Worcester 01655, USA., Gildemeister OS, Pepe JA, Lambrecht RW, Bonkovsky HL
المصدر: Molecular and cellular biochemistry [Mol Cell Biochem] 1997 Apr; Vol. 169 (1-2), pp. 13-20.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Netherlands NLM ID: 0364456 Publication Model: Print Cited Medium: Print ISSN: 0300-8177 (Print) Linking ISSN: 03008177 NLM ISO Abbreviation: Mol Cell Biochem Subsets: MEDLINE
أسماء مطبوعة: Publication: New York : Springer
Original Publication: The Hague, Dr. W. Junk B. V. Publishers.
مواضيع طبية MeSH: Heme Oxygenase (Decyclizing)/*biosynthesis , Liver/*metabolism , Metalloporphyrins/*pharmacology, Animals ; Antioxidants/pharmacology ; Chick Embryo ; Gene Expression Regulation ; Heme/pharmacology ; Lipid Peroxidation/drug effects ; Liver/drug effects ; RNA, Messenger/metabolism
مستخلص: Heme oxygenase catalyzes the first and rate-controlling step in heme catabolism. One of the two forms of heme oxygenase (heme oxygenase-1) has been shown to be increased by heme, metals, and in some systems, by certain environmental stresses. However, it remains uncertain whether heme induces hepatic heme oxygenase-1 by a general stress response, or a specific heme-dependent cellular response. The work communicated here explores this issue by examining possible mechanisms whereby heme and other metalloporphyrins induce heme oxygenase-1 in normal liver cells. Primary cultures of chick embryo liver cells were tested for their ability to increase heme oxygenase mRNA after exposure to selected metalloporphyrins (heme, chromium mesoporphyrin, cobalt protoporphyrin and manganese protoporphyrin). The ability of antioxidants to decrease metalloporphyrin-mediated induction of heme oxygenase-1 mRNA was also tested. Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1. We conclude that heme and other non-heme metalloporphyrins induce heme oxygenase-1 through a mechanism requiring protein synthesis, not because metalloporphyrins increase cellular oxidative or other stress.
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معلومات مُعتمدة: DK38825 United States DK NIDDK NIH HHS; RR06009 United States RR NCRR NIH HHS
المشرفين على المادة: 0 (Antioxidants)
0 (Metalloporphyrins)
0 (RNA, Messenger)
42VZT0U6YR (Heme)
EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
تواريخ الأحداث: Date Created: 19970401 Date Completed: 19970611 Latest Revision: 20210107
رمز التحديث: 20231215
DOI: 10.1023/a:1006817207166
PMID: 9089626
قاعدة البيانات: MEDLINE
الوصف
تدمد:0300-8177
DOI:10.1023/a:1006817207166