1972
DOI: 10.1016/0014-5793(72)80434-4
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Oxidation in the NADP system and release of GSSG from hemoglobin‐free perfused rat liver during peroxidatic oxidation of glutathione by hydroperoxides

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Cited by 248 publications
(77 citation statements)
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“…BHP, in addition, is lipid soluble. Sies et al (17) re ported that BHP is readily extracted by the isolated liver up to certain amounts: e.g., only 3% of the BHP appears in the effluent per fusate under infusion of 0.6 mM BHP and the maximum extraction rate by the liver is calcu lated to be 1.5 umol/g liver/min, although the intralobular distribution of BHP still remains to be determined. Therefore, in the perfusion system, hepatocytes in the inlet zones are ex pected to be exposed to higher concentration of BHP as well as higher oxygen tension and eventually to be more peroxidized than the outlet hepatocytes.…”
Section: Discussionmentioning
confidence: 99%
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“…BHP, in addition, is lipid soluble. Sies et al (17) re ported that BHP is readily extracted by the isolated liver up to certain amounts: e.g., only 3% of the BHP appears in the effluent per fusate under infusion of 0.6 mM BHP and the maximum extraction rate by the liver is calcu lated to be 1.5 umol/g liver/min, although the intralobular distribution of BHP still remains to be determined. Therefore, in the perfusion system, hepatocytes in the inlet zones are ex pected to be exposed to higher concentration of BHP as well as higher oxygen tension and eventually to be more peroxidized than the outlet hepatocytes.…”
Section: Discussionmentioning
confidence: 99%
“…Sies et al (17) and Sies and Summer (25) reported that an infusion of 0.3-0.6 mM BHP for 5 min into hemoglobin-free perfused livers leads to only reversible changes, accompanied by cellular oxidation of GSH through GSH per oxidase and the resultant release of GSSG into the perfusate. In the present study, we in fused 0.8 mM BHP for much longer periods.…”
Section: Discussionmentioning
confidence: 99%
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“…By reduction of hydroperoxides to the corresponding alcohols, these enzymes can prevent the production of reactive oxygen radicals and thus may contribute to the protection of the Selenium in Biology 851 Ursini et al, 1982;Brigelius-Flohé et al, 1994 Plasma GPx (pGPx, GPx-3) Takahashi et al, 1987 Gastrointestinal GPx (GI-GPx, GPx-GI, GPx-2) Chu et al, 1993 Iodothyronine deiodinases 5Ј-deiodinase, type I (5ЈDI) Behne et al, 1990;Arthur et al, 1990 5Ј-deiodinase Lee et al, 1999;Watabe et al, 1999;Miranda-Vizuete et al, 1999;Gasdaska et al, 1999 Thioredoxin reductase homologs (SelZf1; SelZf2) Lescure et al, 1999 Selenophosphate synthetase-2 Guimaraes et al, 1996 Functionally undefined 15 kDa selenoprotein of T cells Gladyshev et al, 1998 Selenoprotein P 10 (SelP) Motsenbocker and Tappel organism's macromolecules and biomembranes against oxidation (Sies et al, 1972;Flohé, 1989;Ursini et al, 1995). The role of the cytoplasmic GPx as an 'emergency enzyme' to fight oxidative stress was verified by reverse genetics (Ho et al, 1997;Cheng et al, 1998;de Haan et al, 1998;Fu et al, 1999;Jaeschke et al, 1999) and, in this role, cGPx cannot be substituted by any of the other selenoproteins.…”
Section: Metabolic Function Of Mammalian Selenoproteinsmentioning
confidence: 99%
“…The link between nutritional science and enzymology was, however, established appreciably later when Flohé et al (1973), intrigued by a preliminary report from Hoekstra's group (Rotruck et al, 1972), identified selenium as a stoichiometric, covalently bound component of glutathione peroxidase (GPx), an enzyme previously demonstrated to dominate mammalian hydroperoxide metabolism (Sies et al, 1972). Selenium proved to be present in this enzyme as a selenocysteine residue (Forstrom et al, 1978, Wendel et al, 1978 that is integrated into the amino acid chain (Günzler et al, 1984).…”
Section: Introduction: Some Historical Landmarksmentioning
confidence: 99%