Information de reference pour ce titreAccession Number: | 00003949-200501010-00011.
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Author: | Kim, Yun-Sook; Zhuang, Hean; Koehler, Raymond C.; Dore, Sylvain *
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Institution: | Department of Anesthesiology/Critical Care Medicine, Johns Hopkins University, School of Medicine, Baltimore, MD, USA
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Title: | |
Source: | Free Radical Biology & Medicine. 38(1):85-92, January 2005.
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Abstract: | : Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P450 reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin. Under basal conditions, HO-1 is often undetected and can be induced by numerous stress conditions. Although HO-2 is constitutively expressed, its activity appears to be regulated by post-translational modifications. HO activity has been associated with cellular protection, by which it degrades heme, a prooxidant, into bioactive metabolites. Under given circumstances, overexpression of HO-1 can render cells more sensitive to free radicals. Here, we investigated the properties of human HO isoforms that protect against oxidative stress. Considering that CPR can be a limiting factor for optimal HO activity, we tested stable HO-1 and HO-2 cell lines that derived from the CPR cells. Results indicate that the HO-1 and HO-2 cells are more resistant than controls to hemin and to the organic tert-butyl hydroperoxide, t-BuOOH. However, HO-1 cells are less resistant than HO-2 cells to hydrogen peroxide (H2O2). The levels of oxidatively modified proteins of HO-1 and HO-2 cells in response to t-BuOOH toxicity are identical, but the level of oxidatively modified proteins of HO-2 cells is less than that of HO-1 cells in response to H2O2 toxicity. Performing subcellular fractionations revealed that HO-2 and CPR are found together in the microsomal fractions, whereas HO-1 is partially present in the microsome and also found in other fractions, such as the cytosol. These same findings were observed in non-transfected primary neurons where HO-1 proteins were chemically induced with 15-deoxy-[DELTA]12,14-prostaglandin J2 (15dPGJ2). The differences in subcellular localization of HO-1 and HO-2 could explain some of the discrepancies in their cellular activity and enzymatic protective mechanisms.
(C) 2005Elsevier, Inc.
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Author Keywords: | Cytochrome P450 reductase; Endoplasmic reticulum; Heme oxygenase; Microsome; Prostaglandins; Subcellular localization; Free radicals.
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Language: | English.
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Document Type: | Original Contribution.
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Journal Subset: | Clinical Medicine. Life & Biomedical Sciences.
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ISSN: | 0891-5849
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NLM Journal Code: | 8709159, fre
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DOI Number: | https://dx.doi.org/10.1016/j.fre...- ouverture dans une nouvelle fenêtre
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