Effect of Vitamin E on Glutathione-Dependent Enzymes

References

• Aarts L., Hee van der R., Dekker I., Jong de J., Langemeijer H., Bast A. The widely used anesthetic agent propofol can replace alpha-tocopherol as an antioxidant. Fed. Eur. Biochem. Soc. 1995; 357: 83–85
   Google Scholar
• Acker van F. A. A., Schouten O., Haenen G. R. M. M., Vijgh van der W. J. F., Bast A. Flavonoids can replace alpha-tocopherol as an antioxant. Fed. Eur. Biochem. Soc. Lett. 2000; 473: 145–148
   Google Scholar
• Adler V., Yin Z., Fuchs S. Y., Benezra M., Rosario L., Tew K. D., Pincus M. R., Sardana M., Henderson C. J., Wolf C. R., Davis R. J., Ronai Z. Regulation of JNK signaling by GSTp. EMBO J. 1999; 18: 1321–1334
   Google Scholar
• Aniya Y., Naito A. Oxidative stress-induced activation of microsomal glutathione S-transferase in isolated rat liver. Biochem. Pharmacol. 1993; 45: 37–42
   Google Scholar
• Aratri E., Spycher S., Breyer I., Azzi A. Modulation of alpha-tropomyosin expression by alpha-tocopherol in rat vascular smooth muscle cells. Fed. Eur. Biochem. Soc. Lett. 1999; 447: 91–94
   Google Scholar
• Arita M., Sato Y., Arai H., Inoue K. Binding of alpha-tocopherylquinone, an oxidized form of alpha-tocopherol, to glutathione-S-transferase in the liver cytosol. Fed. Eur. Biochem. Soc. Lett. 1998; 436: 424–426
   Google Scholar
• Arrigo A. P. Gene expression and the thiol redox state. Free Radic. Biol. Med. 1999; 27: 936–944
   Google Scholar
• Awasthi Y. C., Sharma R., Singhal S. S. Human glutathione S-transferases. Int. J. Biochem. 1994; 26: 295–308
   Google Scholar
• Azzi A., Stocker A. Vitamin E: non-antioxidant roles. Prog. Lipid Res. 2000; 39: 231–255
   Google Scholar
• Azzi A., Boscoboinik D., Chatelain E., Ozer N. K., Stauble B. d-alpha-tocopherol control of cell proliferation. Mol. Asp. Med. 1993; 14: 265–271
   Google Scholar
• Azzi A., Boscoboinik D., Clement S., Ozer N. K., Ricciarelli R., Stocker A., Tasinato A., Sirikci O. Signalling functions of alpha-tocopherol in smooth muscle cells. Int. J. Vitam. Nutr. Res. 1997; 67: 343–349
   Google Scholar
• Azzi A., Boscoboinik D., Clement S., Ozer N., Ricciarelli R., Stocker A. Vitamin E mediated response of smooth muscle cell to oxidant stress. Diabetes Res. Clin. Pract. 1999; 45: 191–198
   Google Scholar
• Azzi A., Breyer I., Feher M., Ricciarelli R., Stocker A., Zimmer S., Zingg J. Nonantioxidant functions of alpha-tocopherol in smooth muscle cells. J. Nutr. 2001; 131: 378S–381S
   Google Scholar
• Azzi A., Gysin R., Ricciarelli R., Villacorta L., Visarius T., Zingg J.-M. Regulation of gene and protein expression by vitamin E. Free Radic. Res. 2002a; 36: 30–35
   Google Scholar
• Azzi A., Ricciarelli R., Zingg J. M. Non-antioxidant molecular functions of alpha-tocopherol (vitamin E). Fed. Eur. Biochem. Soc. Lett. 2002b; 519: 8–10
   Google Scholar
• Bast A., Haenen G. R. M. M. Zin en onzin van antioxidantia. Pharm. Weekbl. 1991; 126: 600–605
   Google Scholar
• Bast A., Haenen G. R., Doelman C. J. Oxidants and antioxidants: state of the art. Am. J. Med. 1991; 91: 2S–13S
   Google Scholar
• Bauernfeind J. C. The tocopherol content of food and influencing factors. Crit. Rev. Food Sci. Nutr. 1977; 8: 337–382
   Google Scholar
• Bindoli A., Valente M., Cavallini L. Inhibition of lipid peroxidation by alpha-tocopherolquinone and alpha-tocopherolhydroquinone. Biochem. Int. 1985; 10: 753–761
   Google Scholar
• Birringer M., Drogan D., Bregelius-Flohe R. Tocopherols are metabolized in HepG2 cells by side chain ω-oxidation and consecutive β-oxidation. Free Radic. Biol. Med. 2001; 31: 226–232
   Google Scholar
• Birringer M., Pfluger P., Kluth D., Landes N., Brigelius Flohe R. Identities and differences in the metabolism of tocotrienols and tocopherols in HepG2 cells. J. Nutr. 2002; 132: 3113–3118
   Google Scholar
• Bjorneboe A., Bjorneboe G. E. A., Drevon C. A. Absorption, transport and distribution of vitamin E. J. Nutr. 1990; 120: 233–242
   Google Scholar
• Black S. M., Wolf C. R. The role of glutathione-dependent enzymes in drug resistance. Pharmacol. Ther. 1991; 51: 139–154
   Google Scholar
• Blatt D. H., Leonard S., Traber M. Vitamin E kinetics and the function of tocopherol regulatory proteins. Nutrition 2001; 17
   Google Scholar
• Board P. G., Baker R. T., Chelvanayagam G., Jermiin L. S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 1997; 328: 929–935
   Google Scholar
• Board P. G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L. S., Schulte G. K., Danley D. E., Hoth L. R., Griffor M. C., Kamath A. V., Rosner M. H., Chrunyk B. A., Perregaux D. E., Gabel C. A., Geoghegan K. F., Pandit J. Identification, characterization, and crystal structure of the Omega class glutathione transferases. J. Biol. Chem. 2000; 275: 24798–24806
   Google Scholar
• Borst P., Evers R., Kool M., Wijnholds J. The multidrug resistance protein family. Biochim. Biophys. Acta 1999; 1461: 347–357
   Google Scholar
• Brigelius R., Muckel C., Akerboom T. P., Sies H. Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide. Biochem. Pharmacol. 1983; 32: 2529–2534
   Google Scholar
• Brigelius Flohe R., Traber M. G. Vitamin E: function and metabolism. FASEB J. 1999; 13: 1145–1155
   Google Scholar
• Brigelius Flohe R., Kelly F. J., Salonen J. T., Neuzil J., Zingg J. M., Azzi A. The European perspective on vitamin E: current knowledge and future research. Am. J. Clin. Nutr. 2002; 76: 703–716
   Google Scholar
• Burg D., Mulder G. J. Glutathione conjugates and their synthetic derivatives as inhibitors of glutathione-dependent enzymes involved in cancer and drug resistance. Drug Metab. Rev. 2002; 34: 821–863
   Google Scholar
• Burk R. F. Glutathione-dependent protection by rat liver microsomal protein against lipid peroxidation. Biochem. Biophys. Acta 1983; 757: 21–28
   Google Scholar
• Burton G. W., Traber M. G. Vitamin E: antioxidant activity, biokinetics, and bioavailability. Annu. Rev. Nutr. 1990; 10: 357–382
   Google Scholar
• Butkiewicz D., Grzybowska E., Phillips D. H., Hemminki K., Chorazy M. Polymorphisms of the GSTP1 and GSTM1 genes and PAH-DNA adducts in human mononuclear white blood cells. Environ. Mol. Mutagen. 2000; 35: 99–105
   Google Scholar
• Chan A. C. Vitamin E and atherosclerosis. J. Nutr. 1998; 128: 1593–1596
   Google Scholar
• Chang M., Shin Y. G., van Breemen R. B., Blond S. Y., Bolton J. L. Structural and functional consequences of inactivation of human glutathione S-transferase P1-1 mediated by the catechol metabolite of equine estrogens, 4-hydroxyequilenin. Biochemistry 2001; 40: 4811–4820
   Google Scholar
• Chaudiere J., Ferrari Iliou R. Intracellular antioxidants: from chemical to biochemical mechanisms. Food Chem. Toxicol. 1999; 37: 949–962
   Google Scholar
• Cheeseman K. H., Holley A. E., Kelly F. J., Wasil M., Hughes L., Burton G. Biokinetics in humans of RRR-alpha-tocopherol: the free phenol, acetate ester, and succinate ester forms of vitamin E. Free Radic. Biol. Med. 1995; 19: 591–598
   Google Scholar
• Chen L. H., Shiau C. C. Induction of glutathione-S-transferase activity by antioxidants in hepatocyte culture. Anticancer Res. 1989; 9: 1069–1072
   Google Scholar
• Chow C. K. On the formation and measurement of alpha-tocopherolquinone and alpha-tocopherolhydroquinone in rat tissues. Nutr. Rev. 1983; 41: 98–99
   Google Scholar
• Clough R. L., Yee B. G., Foote C. S. Chemistry of singlet oxygen. The unstable primary product of tocopherol photooxidation. J. Am. Soc. 1979; 101: 683–686
   Google Scholar
• Cooney R. V., Harwood P. J., Franke A. A., Narala K., Sundstrom A., Berggren P., Mordan L. J. Products of gamma-tocopherol reaction with NO2 and their formation in rat insulinoma (RINm5F) cells. Free Radic. Biol. Med. 1995; 19: 259–269
   Google Scholar
• Cornwell D. G., Huttner J. J., Milo G. E., Panganamala R. V., Sharma H. M., Geer J. C. Polyunsaturated fatty acids, vitamin E, and the proliferation of aortic smooth muscle cells. Lipids 1979; 14: 194–207
   Google Scholar
• Cornwell D. G., Williams M. V., Wani A. A., Wani G., Shen E., Jones K. H. Mutagenicity of tocopheryl quinones: evolutionary advantage of selective accumulation of dietary alpha-tocopherol. Nutr. Cancer 2002; 43: 111–118
   Google Scholar
• DeJong J. L., Morgenstern R., Jornvall H., DePierre J. W., Tu C. P. Gene expression of rat and human microsomal glutathione S-transferases. J. Biol. Chem. 1988; 263: 8430–8436
   Google Scholar
• Deneke S. M., Fanburg B. L. Regulation of cellular glutathione. Am. J. Physiol. 1989; 257: L163–L173
   Google Scholar
• Dickinson D., Forman H. Cellular glutathione and thiols metabolism. Biochem. Pharmacol. 2002; 64: 1019
   Google Scholar
• Dinkova-Kostova D. T., Talalay P. Persuasive evidence that quinone reductase type 1 (DT diaphorase) protects cells against the toxicity of electrophiles and reactive forms of oxygen. Free Radic. Biol. Med. 2000; 29: 231–240
   Google Scholar
• d'Ischia M., Novellino L. Nitric oxide-induced oxidation of alpha-tocopherol. Bioorg. Med. Chem. 1996; 4: 1747–1753
   Google Scholar
• Douglas K. T. Mechanism of action of glutathione-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 1987; 59: 103–167
   Google Scholar
• Drevon C. A. Absorption, transport and metabolism of vitamin E. Free Radic. Res. Commun. 1991; 14: 229–246
   Google Scholar
• Eaton D. L., Bammler T. K. Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol. Sci. 1999; 49: 156–164
   Google Scholar
• Eder K., Flader D., Hirche F., Brandsch C. Excess dietary vitamin E lowers the activities of antioxidative enzymes in erythrocytes of rats fed salmon oil. J. Nutr. 2002; 132: 3400–3404
   Google Scholar
• Evans H. M., Bishop K. S. On the relationship between fertility and nutrition. J. Metab. Sci. 1922; 1: 319–356
   Google Scholar
• Evans P., Halliwell B. Micronutrients: oxidant/antioxidant status. Br. J. Nutr. 2001; 85(Suppl. 2)S67–S74
   Google Scholar
• Evans H. M., Emerson O. H., Emerson G. A. The isolation from wheat-germ oil of an alcohol, alpha-tocopherol, having the properties of vitamin E. J. Biol. Chem. 1936; 113: 319
   Google Scholar
• Fernholz E. On the constitution of alpha-tocopherol. J. Am. Chem. Soc. 1938; 60: 700–705
   Google Scholar
• Filomeni G., Rotilio G., Ciriolo M. Cell signaling and the glutathione redox system. Biochem. Pharmacol. 2002; 64: 1057
   Google Scholar
• Flohe L. Glutathione peroxidase. Basic Life Sci. 1988; 49: 663–668
   Google Scholar
• Gerk P. M., Vore M. Regulation of expression of the multidrug resistance-associated protein 2 (MRP2) and its role in drug disposition. J. Pharmacol. Exp. Ther. 2002; 302: 407–415
   Google Scholar
• Giamvala D. H., Church D. F., Pryor W. A. Kinetics of ozonation. Reactions of ozone with alpha-tocopherol and oleate and linoleate esters in carbon tetrachloride and in aqueous micellar solvents. J. Am. Chem. Soc. 1986; 108: 6646–6651
   Google Scholar
• Girotti A. W. Mechanisms of lipid peroxidation. J. Free Radic. Biol. Med. 1985; 1: 87–95
   Google Scholar
• Graham K. S., Reddy C. C., Scholz R. W. Reduced glutathione effects on alpha-tocopherol concentration of rat liver microsomes undergoing NADPH-dependent lipid peroxidation. Lipids 1989; 24: 909–914
   Google Scholar
• Griffith O. W., Meister A. Glutathione: interorgan translocation, turnover, and metabolism. Proc. Natl Acad. Sci. USA 1979; 76: 5606–5610
   Google Scholar
• Guthenberg C., Mannervik B. Glutathione S-transferase (transferase pi) from human placenta is identical or closely related to glutathione S-transferase (transferase rho) from erythrocytes. Biochim. Biophys. Acta 1981; 661: 255–260
   Google Scholar
• Haaften van R. I. M., Evelo C. T., Haenen G. R. M. M., Bast A. No reduction of alpha-tocopherol quinone by glutathione in rat liver microsomes. Biochem. Pharmacol. 2001a; 61: 715–719
   Google Scholar
• Haaften van R. I. M., Evelo C. T. A., Penders J., Eijnwachter M. P. F., Haenen G. R. M. M., Bast A. Inhibition of human glutathione S-transferase P1-1 by tocopherols and alpha-tocopherol derivatives. Biochim. Biophys. Acta 2001b; 1548: 23–28
   Google Scholar
• Haaften van R. I. M., Evelo C. T. A., Haenen G. R. M. M., Bast A. Alpha-tocopherol inhibits human glutathione S-transferase pi. Biochem. Biophys. Res. Commun. 2001c; 280: 631–633
   Google Scholar
• Haaften van R. I. M., Haenen G. R. M. M., Evelo C. T. A., Bast A. Tocotrienols inhibit human glutathione S-transferase P1-1. Int. Union Biochem. Mol. Biol. Life 2002; 54: 81–84
   Google Scholar
• Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974; 249: 7130–7139
   Google Scholar
• Haenen G. R. M. M., Bast A. Protection against lipid peroxidation by a microsomal glutathione-dependent labile factor. Fed. Eur. Biochem. Soc. 1983; 159: 24–28
   Google Scholar
• Haenen G. R. M. M., Tai Tin Tsoi J. N. L., Vermeulen N. P. E., Timmerman H., Bast A. 4-Hydroxy-2,3-trans-nonenal stimulates microsomal lipid peroxidation by reducing the glutathione-dependent protection. Arch. Biochem. Biophys. 1987; 259: 449–456
   Google Scholar
• Haenen G. R., Vermeulen N. P., Tai Tin Tsoi J. N., Ragetli H. M., Timmerman H., Blast A. Activation of the microsomal glutathione-S-transferase and reduction of the glutathione dependent protection against lipid peroxidation by acrolein. Biochem. Pharmacol. 1988; 37: 1933–1938
   Google Scholar
• Haenen G. R., Vermeulen N. P., Timmerman H., Bast A. Effect of thiols on lipid peroxidation in rat liver microsomes. Chem.-Biol. Interact. 1989; 71: 201–212
   Google Scholar
• Haenen G. R. M. M., Bastiaans H. M. M., Bast A. Mechanism of the glutathione-dependent protection against microsomal lipid peroxidation. Oxygen Radicals, K. Yagi, M. Kondo, E. Niki, Yoshikawa, T. Exerpta Medica, Amsterdam 1992; 731–736
   Google Scholar
• Halliwell B. How to characterize an antioxidant: an update. Biochem. Soc. Symp. 1995; 61: 73–101
   Google Scholar
• Halliwell B. The antioxidant paradox. Lancet 2000; 355: 1179–1180
   Google Scholar
• Halliwell B., Gutteridge J. M. C. Antioxidant defences. Free Radicals in Biology and Medicine, B. Halliwell, J. M. C. Gutteridge. Oxford University Press, Inc., New York 1999; 105–245
   Google Scholar
• Hayashi T., Kanetoshi A., Nakamura M., Tamura M., Shirahama H. Reduction of alpha-tocopherolquinone to alpha-tocopherolhydroquinone in rat hepatocytes. Biochem. Pharmacol. 1992; 44: 489–493
   Google Scholar
• Hayes J. D., McLellan L. I. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic. Res. 1999; 31: 273–300
   Google Scholar
• Hayes J. D., Pulford D. J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 1995; 30: 445–600
   Google Scholar
• Hogg N. H., Joseph J., Kalyanaraman B. The oxidation of alpha-tocopherol and trolox by peroxynitrite. Arch. Biochem. Biophys. 1994; 314: 153–158
   Google Scholar
• Horbach M. E., Sies H., Akerboom T. P. Identification of a hepatic plasma membrane glutathione S-transferase activated by N-ethylmaleimide. Biochim. Biophys. Acta 1993; 1148: 61–66
   Google Scholar
• Hosomi A., Arita M., Sato Y., Kiyose C., Ueda T., Igarashi O., Arai H., Inoue K. Affinity for alpha-tocopherol transfer protein as a determinant of the biological activities of vitamin E analogs. Fed. Eur. Biochem. Soc. 1997; 409: 105–108
   Google Scholar
• Houte van H., De Hoffmann E., Van Veldhoven P. P., Mannaerts G. P., Carchon H., Baes M. I., Declercq P. E. Oxidative catabolism of alpha-tocopherol in rat liver microsomes. Lipids 2001; 36: 367–372
   Google Scholar
• Hughes P. E., Tove S. B. Synthesis of alpha-tocopherolquinone by the rat and its reduction by mitochondria. J. Biol. Chem. 1980; 255: 7095–7097
   Google Scholar
• Iersel van M. L., Ploemen J. P., Lo-Bello M., Federici G., van-Bladeren P. J. Interactions of alpha, beta-unsaturated aldehydes and ketones with human glutathione S-transferase P1-1. Chem.-Biol. Interact. 1997; 108: 67–78
   Google Scholar
• Jakobsson P. J., Morgenstern R., Mancini J., Ford Hutchinson A., Persson B. Common structural features of MAPEG—a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci. 1999; 8: 689–692
   Google Scholar
• Jakobsson P. J., Morgenstern R., Mancini J., Ford Hutchinson A., Persson B. Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. Am. J. Respir. Crit. Care Med. 2000; 161: S20–S24
   Google Scholar
• Jakoby W. B. The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 1978; 46: 383–414
   Google Scholar
• Ji Y., Bennett B. M. Activation of microsomal glutathione S-transferase by peroxynitrite. Mol. Pharmacol. 2002; 63: 136–146
   Google Scholar
• Ji Y., Toader V., Bennett B. M. Regulation of microsomal and cytosolic glutathione S-transferase activities by S-nitrosylation. Biochem. Pharmacol. 2002; 63: 1397–1404
   Google Scholar
• Jiang Q., Elson Schwab I., Courtemanche C., Ames B. N. Gamma-tocopherol and its major metabolite, in contrast to alpha-tocopherol, inhibit cyclooxygenase activity in macrophages and epithelial cells. Proc. Natl Acad. Sci. USA 2000; 97: 11494–11499
   Google Scholar
• Jones K. H., Liu J. J., Roehm J. S., Eckel J. J., Eckel T. T., Stickrath C. R., Triola C. A., Jiang Z., Bartoli G. M., Cornwell D. G. Gamma-tocopheryl quinone stimulates apoptosis in drug-sensitive and multidrug-resistant cancer cells. Lipids 2002; 37: 173–184
   Google Scholar
• Kamal-Eldin A., Appelqvist L. A. The chemistry and antioxidant properties of tocopherols and tocotrienols. Lipids 1996; 31: 671–701
   Google Scholar
• Kantoci D., Wechter W. J., Murray D. J., Dewind S. A., Borchardt D., Khan S. I. Endogenous natriuretic factors 6: the stereochemistry of a natriuretic γ-tocopherol metabolite LLU-α. J. Pharmacol. Exp. Ther. 1997; 282: 648–656
   Google Scholar
• Kappus H., Diplock A. T. Tolerance and safety of vitamin E: a toxicological position report. Free Radic. Biol. Med. 1992; 13: 55–74
   Google Scholar
• Keen J. H., Habig W. H., Jakoby W. B. Mechanism for the several activities of the glutathione S-transferases. J. Biol. Chem. 1976; 251: 6183–6188
   Google Scholar
• Ketterer B. Glutathione S-transferases and prevention of cellular free radical damage. Free Radic. Res. 1998; 28: 647–658
   Google Scholar
• Khor H. T., Ng T. T. Effects of administration of alpha-tocopherol and tocotrienols on serum lipids and liver HMG CoA reductase activity. Int. J. Food Sci. Nutr. 2000; 51: S3–S11
   Google Scholar
• Kohar I., Baca M., Suarna C., Stocker R., Southwell-Keely P. T. Is alpha-tocopherol a reservoir for alpha-tocopheryl hydroquinone?. Free Radic. Biol. Med. 1995; 19: 197–207
   Google Scholar
• Kondo T., Yoshida K., Urata Y., Goto S., Gasa S., Taniguchi N. Gamma-glutamylcysteine synthetase and active transport of glutathione S-conjugate are responsive to heat shock in K562 erythroid cells. J. Biol. Chem. 1993; 268: 20366–20372
   Google Scholar
• Krendel D. A., Gilchrist J. M., Johnson A. O., Bossen E. H. Isolated deficiency of vitamin E with progressive neurologic deterioration. Neurology 1987; 37: 538–540
   Google Scholar
• Laplante P., Vanasse M., Michaud J., Geoffroy G., Brochu P. A progressive neurological syndrome associated with an isolated vitamin E deficiency. Can. J. Neurol. Sci. 1984; 11: 561–564
   Google Scholar
• Larnaout A., Belal S., Zouari M., Fki M., Ben Hamida C., Goebel H. H., Ben Hamida M., Hentati F. Friedreich's ataxia with isolated vitamin E deficiency: a neuropathological study of a Tunisian patient. Acta Neuropathol. 1997; 93: 633–637
   Google Scholar
• Lash L. H. Role of renal metabolism in risk to toxic chemicals. Environ. Health Perspect. 1994; 102(Suppl. 11)75–79
   Google Scholar
• Liebler D. C. The role of metabolism in the antioxidant function of vitamin E. Crit. Rev. Toxicol. 1993; 23: 147–169
   Google Scholar
• Liebler D. C. Antioxidant chemistry of alpha-tocopherol in biological systems. Roles of redox cycles and metabolism. Sub-cellular Biochemistry: Reviews and Essays with the Structure, Function, Genetics, Biogenesis and Evolution of Sub-cellular Components, Quinn, P.S., Kagan, V.E. Plenum Press, New York 1998; Vol. 30: 301–317
   Google Scholar
• Liebler D. C., Burr J. A. Antioxidant reactions of alpha-tocopherolhydroquinone. Lipids 2000; 35: 1045–1047
   Google Scholar
• Liebler D. C., Matsumoto S., Iitaka Y., Matsuo M. Reactions of vitamin E and its model compound 2,2,5,7,8-pentamethylchroman-6-ol with ozone. Chem. Res. Toxicol. 1993; 6: 69–74
   Google Scholar
• Lindsey J. A., Zhang H. F., Kaseki H., Morisaki N., Sato T., Cornwell D. G. Fatty acid metabolism and cell proliferation. VII. Antioxidant effects of tocopherols and their quinones. Lipids 1985; 20: 151–157
   Google Scholar
• Lundqvist G., Yucel Lindberg T., Morgenstern R. The oligomeric structure of rat liver microsomal glutathione transferase studied by chemical cross-linking. Biochim. Biophys. Acta 1992; 1159: 103–108
   Google Scholar
• Maiorino M., Zamburlini A., Roveri A., Ursini F. Prooxidant role of vitamin E in copper induced lipid peroxidation. Fed. Eur. Biochem. Soc. 1993; 330: 174–176
   Google Scholar
• Mannervik B. The isoenzymes of glutathione transferase. Adv. Enzymol. Relat. Areas Mol. Biol. 1985; 57: 357–417
   Google Scholar
• Mannervik B., Awasthi Y. C., Board P. G., Hayes J. D., Di-Ilio C., Ketterer B., Listowsky I., Morgenstern R., Muramatsu M., Pearson W. R. Nomenclature for human glutathione transferases [letter]. Biochem. J. 1992; 282: 305–306
   Google Scholar
• Manson J. E., Bassuk S. S., Stampfer M. J. Does vitamin E supplementation prevent cardiovascular events?. J. Women's Health 2003; 12: 123–136
   Google Scholar
• Marchioli R. Dietary supplementation with n−3 polyunsaturated fatty acids and vitamin E after myocardial infarction: results of the GISSI-Prevenzione trial. Lancet 1999; 354: 447–455
   Google Scholar
• Mason K. E. Differences in testis injury and repair after vitamin A-deficiency, vitamin E-deficiency, and inanition. Am. J. Anat. 1933; 52: 153–227
   Google Scholar
• Matsuo M., Matsumoto S. Oxygenations of vitamin E (alpha-tocopherol) and its model compound 2,2,5,7,8-pentamethylchroman-6-ol in the presence of the superoxide radical solubilized in aprotic solvents: unique epoxidations and recyclizations. J. Org. Chem. 1987; 52: 3514–3520
   Google Scholar
• McCay P. B., Gibson D. D., Fong K., Hornbrook K. R. Effect of glutathione peroxidase activity on lipid peroxidation in biological membranes. Biochim. Biophys. Acta 1976; 431: 459–468
   Google Scholar
• McCay P. B., Brueggemann G., Lai E. K., Powell S. R. Evidence that alpha-tocopherol functions cyclically to quench free radicals in hepatic microsomes. Ann. NY Acad. Sci. 1989; 570: 32–45
   Google Scholar
• Meagher E. A. Treatment of atherosclerosis in the new millennium: is there a role for vitamin E?. Prev. Cardiol. 2003; 6: 85–90
   Google Scholar
• Mehlert A., Diplock A. T. The glutathione S-transferases in selenium and vitamin E deficiency. Biochem. J. 1985; 227: 823–831
   Google Scholar
• Meydani M. Vitamin E. Lancet 1995; 345: 170–175
   Google Scholar
• Mills G. C. Hemoglobin catabolism I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J. Biol. Chem. 1957; 229: 189–197
   Google Scholar
• Minotti G., Aust S. D. Redox cycling of iron and lipid peroxidation. Lipids 1992; 27: 219–226
   Google Scholar
• Moellering D., Mc Andrew J., Patel R. P., Forman H. J., Mulcahy R. T., Jo H., Darley Usmar V. M. The induction of GSH synthesis by nanomolar concentrations of NO in endothelial cells: a role for gamma-glutamylcysteine synthetase and gamma-glutamyl transpeptidase. Fed. Eur. Biochem. Soc. Lett. 1999; 448: 292–296
   Google Scholar
• Moore A. N. J., Ingold K. U. Alpha-tocopherol quinone is converted into vitamin E in man. Free Radic. Biol. Med. 1997; 22: 931–934
   Google Scholar
• Morari E. C., Leite J. L., Granja F., Da-Assumpcao L. V., Ward L. S. The null genotype of glutathione S-transferase M1 and T1 locus increases the risk for thyroid cancer. Cancer Epidemiol. Biomark. Prev. 2002; 11: 1485–1488
   Google Scholar
• Morgenstern R., DePierre J. W., Ernster L. Activation of microsomal glutathione S-transferase activity by sulfhydryl reagents. Biochem. Biophys. Res. Commun. 1979; 87: 657–663
   Google Scholar
• Morgenstern R., Guthenberg C., Depierre J. W. Microsomal glutathione S-transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione S-transferases A, B and C. Eur. J. Biochem. 1982; 128: 243–248
   Google Scholar
• Morgenstern R., Lundqvist G., Andersson G., Balk L., DePierre J. W. The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochem. Pharmacol. 1984; 33: 3609–3614
   Google Scholar
• Mulcahy R. T., Gipp J. J. Identification of a putative antioxidant response element in the 5′-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem. Biophys. Res. Commun. 1995; 209: 227–233
   Google Scholar
• Napoli C., Leccese M., Palumbo G., Nigris F. D., Chiariello P., Zuliani P., Somma P., Di Loreto M., De Matteis C., Cacciatore F., Abete P., Liguori A., Chiariello M., D'Armiento F. P. Effects of vitamin E and HMG-CoA reductase inhibition on cholesteryl ester transfer protein and lecithin-cholesterol acyltransferase in hypercholesterolemia. Coron. Artery Dis. 1998; 9: 257–264
   Google Scholar
• Neefjes V. M., Evelo C. T., Baars L. G., Blanco C. E. Erythrocyte glutathione S transferase as a marker of oxidative stress at birth. Arch. Dis. Childhood 1999; 81: F130–F133
   Google Scholar
• Nishihira J., Ishibashi T., Sakai M., Nishi S., Kumazaki T., Hatanaka Y., Tsuda S., Hikichi K. Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47. Biochem. Biophys. Res. Commun. 1992; 188: 424–432
   Google Scholar
• Noguchi N., Watanabe A., Shi H. Diverse functions of antioxidants. Free Radic. Res. 2000; 33: 809–817
   Google Scholar
• Olson R. E., Carpenter P. C. The regulatory function of vitamin E. Adv. Enzyme Regul. 1967; 5: 325–334
   Google Scholar
• Ong F. B., Wan-Ngah W. Z., Shamaan N. A., Md-Top A. G., Marzuki A., Khalid A. K. Glutathione S-transferase and gamma-glutamyl transpeptidase activities in cultured rat hepatocytes treated with tocotrienol and tocopherol. Comp. Biochem. Physiol. C 1993; 106: 237–240
   Google Scholar
• Ouwerkerk-Mahadevan S., Mulder G. J. Inhibition of glutathione conjugation in the rat in vivo by analogues of glutathione conjugates. Chem.-Biol. Interact. 1998; 111–112: 163–176
   Google Scholar
• Packer L., Weber S. U., Rimbach G. Molecular aspects of alpha-tocotrienol antioxidant action and cell signalling. J. Nutr. 2001; 131: 369s–373s
   Google Scholar
• Paolicchi A., Dominici S., Pieri L., Maellaro E., Pompella A. Glutathione catabolism as a signaling mechanism. Biochem. Pharmacol. 2002; 64: 1027
   Google Scholar
• Parker R. S. Dietary and biochemical aspects of vitamin E. Adv. Food Nutr. Res. 1989; 33: 157–232
   Google Scholar
• Parker R. S., Swanson J. E. A novel 5′-carboxychroman metabolite of alpha-tocopherol secreted by HEPG2 cells and excreted in human urine. Biochem. Biophys. Res. Commun. 2000; 269: 580–583
   Google Scholar
• Parks E., Traber M. G. Mechanisms of vitamin E regulation: research over the past decade and focus on the future. Antioxid. Redox Signaling 2000; 2: 405–412
   Google Scholar
• Patel J. M., Edwards D. A. Vitamin E, membrane order, and antioxidant behavior in lung microsomes and reconstituted lipid vesicles. Toxicol. Appl. Pharmacol. 1988; 96: 101–114
   Google Scholar
• Pearce B. C., Parker R. A., Deason M. E., Qureshi A., Wright J. J. K. Hypocholesterolemic activity of synthetic and natural tocotrienols. J. Med. Chem. 1992; 35: 3595–3606
   Google Scholar
• Pearce B. C., Parker R. A., Deason M. E., Dischino D. D., Gillespie E., Qureshi A., Volk K., Wright J. J. K. Inhibitors of cholesterol biosynthesis. Hypocholesterolemic and antioxidant activities of benzopyran and tetrahydronaphthalene analogues of the tocotrienols. J. Med. Chem. 1994; 37: 526–541
   Google Scholar
• Pope S. A. S., Burtin G. E., Clayton P. T., Madge D. J., Muller D. P. R. New synthesis of (±)-alpha-CMBHC and its confirmation as a metabolite of alpha-tocopherol (vitamin E). Bioorg. Med. Chem. 2001; 9: 1337–1343
   Google Scholar
• Poppel van G., Vogel de N., Bladeren van P. J., Kok F. J. Increased cytogenetic damage in smokers deficient in glutathione S-transferase isozyme mu. Carcinogenesis 1992; 13: 303–305
   Google Scholar
• Prohaska J. R. The glutathione peroxidase activity of glutathione S-transferases. Biochim. Biophys. Acta 1980; 611: 87–98
   Google Scholar
• Qureshi A., Bradlow B. A., Brace L., Manganello J., Peterson D. M., Pearce B. C., Wright J. J. K., Gapor A., Elson C. E. Response of hypercholesterolemic subjects to administration of tocotrienols. Lipids 1995; 30: 1171–1177
   Google Scholar
• Qureshi A., Pearce B. C., Nor R. M., Gapor A., Peterson D. M., Elson C. E. Dietary alpha-tocopherol attenuates the impact of gamma-tocotrienol on hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in chickens. J. Nutr. 1996; 126: 389–394
   Google Scholar
• Qureshi A. A., Sami S. A., Salser W. A., Khan F. A. Dose-dependent suppression of serum cholesterol by tocotrienol-rich fraction (TRF25) of rice bran in hypercholesterolemic humans. Atherosclerosis 2002; 161: 199–207
   Google Scholar
• Rahman I., Bel A., Mulier B., Lawson M. F., Harrison D. J., Macnee W., Smith C. A. Transcriptional regulation of gamma-glutamylcysteine synthetase-heavy subunit by oxidants in human alveolar epithelial cells. Biochem. Biophys. Res. Commun. 1996; 229: 832–837
   Google Scholar
• Reddy C. C., Scholz R. W., Thomas C. E., Edward J. M. Vitamin E dependent reduced glutathione inhibition of rat liver microsomal lipid peroxidation. Life Sci. 1982; 31: 571–576
   Google Scholar
• Reed D. J., Fariss M. W. Glutathione depletion and susceptibility. Pharmacol. Rev. 1984; 36: 25s–33s
   Google Scholar
• Ricciarelli R., Zingg J., Azzi A. The 80th anniversary of vitamin E: beyond its antioxidant properties. Biol. Chem. 2002; 383: 457–465
   Google Scholar
• Richman P. G., Meister A. Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J. Biol. Chem. 1975; 250: 1422–1426
   Google Scholar
• Rowntree L. G., Steinberg A., Dorrance G. M., Ciccone E. F. Sarcoma in rats from the ingestion of a crude wheat-germ oil made by ether extraction. Am. J. Cancer 1937; 31: 359–372
   Google Scholar
• Salagovic J., Kalina I., Stubna J., Habalova V., Hrivnak M., Valansky L., Kohut A., Biros E. Genetic polymorphism of glutathione S-transferase M1 and T1 as a risk factor in lung and bladder cancers. Neoplasma 1998; 45: 312–317
   Google Scholar
• Salinas A. E., Wong M. G. Glutathione S-transferases—a review. Curr. Med. Chem. 1999; 6: 279–309
   Google Scholar
• Sato Y., Hagiwara K., Arai H., Inoue K. Purification and characterization of the alpha-tocopherol transfer protein from rat liver. Fed. Eur. Biochem. Soc. 1991; 288: 41–45
   Google Scholar
• Scholz R. W., Graham K. S., Gumpricht E., Reddy C. C. Mechanism of interaction of vitamin E and glutathione in the protection against membrane lipid peroxidation. Ann. NY Acad. Sci. 1989; 570: 514–517
   Google Scholar
• Scholz R. W., Reddy P. V., Wynn M. K., Graham K. S., Liken A. D., Gumpricht E., Reddy C. C. Glutathione-dependent factors and inhibition of rat liver microsomal lipid peroxidation. Free Radic. Biol. Med. 1997; 23: 815–828
   Google Scholar
• Schultz M., Dutta S., Tew K. D. Inhibitors of glutathione S-transferases as therapeutic agents. Adv. Drug Deliv. Rev. 1997; 26: 91–104
   Google Scholar
• Seelig G. F., Simondsen R. P., Meister A. Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits. J. Biol. Chem. 1984; 259: 9345–9347
   Google Scholar
• Sevanian A., Muakkassah Kelly S. F., Montestruque S. The influence of phospholipase A2 and glutathione peroxidase on the elimination of membrane lipid peroxides. Arch. Biochem. Biophys. 1983; 223: 441–452
   Google Scholar
• Shen H. X., Tamai K., Satoh K., Hatayama I., Tsuchida S., Sato K. Modulation of class Pi glutathione transferase activity by sulfhydryl group modification. Arch. Biochem. Biophys. 1991; 286: 178–182
   Google Scholar
• Shi H., Noguchi N., Niki E. Comparative study of antioxidative action of alpha-tocopheryl hydroquinone, ubiquinol, and alpha-tocopherol against lipid peroxidation. Free Radic. Biol. Med. 1999; 27: 334–346
   Google Scholar
• Shuker D. E., Atkin W., Bingham S. A., Leuratti C., Singh R. Malondialdehyde–DNA adducts in relation to diet and disease risk—a brief overview of recent results. IARC Sci. Publ. 2002; 156: 475–480
   Google Scholar
• Siegel D., Bolton E. M., Burr J. A., Liebler D. C., Ross D. The reduction of alpha-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of alpha-tocopherolhydroquinone as a cellular antioxidant. Mol. Pharmacol. 1997; 52: 300–305
   Google Scholar
• Sies H., Stahl W., Sundquist A. R. Antioxidant functions of vitamins: vitamins E and C, beta-carotene, and other carotenoids. Ann. NY Acad. Sci. 1992; 669: 7–20
   Google Scholar
• Sontag T. J., Parker R. S. Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. J. Biol. Chem. 2002; 277: 25290–25296
   Google Scholar
• Stark A. A., Zeiger E., Pagano D. A. Glutathione metabolism by gamma-glutamyltranspeptidase leads to lipid peroxidation: characterization of the system and relevance to hepatocarcinogenesis. Carcinogenesis 1993; 14: 183–189
   Google Scholar
• Stephens N. G., Parsons A., Schofield P. M. Randomised controlled trial of vitamin E in patients with coronary disease: Cambridge Heart Antioxidant Study (CHAOS). Lancet 1996; 347: 781–786
   Google Scholar
• Stocker A., Zimmer S., Spycher S. E., Azzi A. Identification of a novel cytosolic tocopherol-binding protein: structure, specificity, and tissue distribution. Int. Union Biochem. Mol. Biol. Life 1999; 48: 49–55
   Google Scholar
• Stone W. L., Dratz E. A. Increased glutathione-S-transferase activity in antioxidant-deficient rats. Biochim. Biophys. Acta 1980; 631: 503–506
   Google Scholar
• Stumpf D. A., Sokol R., Bettis D., Neville H., Ringel S., Angelini C., Bell R. Friedreich's disease: V. Variant form with vitamin E deficiency and normal fat absorption. Neurology 1987; 37: 68–74
   Google Scholar
• Suarna C., Southwell-Keely P. New oxidation products of alpha-tocopherol. Lipids 1988; 23: 137–139
   Google Scholar
• Suarna C., Craig D. C., Cross K. J., Southwell-Keely P. Oxidations of vitamin E (alpha-tocopherol) and its model compound 2,2,5,7,8-pentamethyl-6-hydroxychroman. A new dimer. J. Org. Chem. 1988; 53: 1281–1284
   Google Scholar
• Suarna C., Baca M., Southwell-Keely P. Oxidation of the alpha-tocopherol model compound 2,2,5,7,8-pentamethyl-6-chromanol in the presence of alcohols. Lipids 1992; 27: 447–453
   Google Scholar
• Suzuki H., Sugiyama Y. Excretion of GSSG and glutathione conjugates mediated by MRP1 and cMOAT/MRP2. Semin. Liver Dis. 1998; 18: 359–376
   Google Scholar
• Tampo Y., Yonaha M. Vitamin E and glutathione are required for preservation of microsomal glutathione S-transferase from oxidative stress in microsomes. Pharmacol. Toxicol. 1990; 66: 259–265
   Google Scholar
• Tasinato A., Boscoboinik D., Bartoli G. M., Maroni P., Azzi A. d-alpha-tocopherol inhibition of vascular smooth muscle cell proliferation occurs at physiological concentrations, correlates with protein kinase C inhibition, and is independent of its antioxidant properties. Proc. Natl Acad. Sci. USA 1995; 92: 12190–12194
   Google Scholar
• Taylor M. W., Nelson V. E. Some observations on ferric chloride addition to the diet. Proc. Soc. Exp. Biol. Med. 1930; 27: 764
   Google Scholar
• Theriault A., Chao J. T., Wang Q., Gapor A., Adeli K. Tocotrienol: a review of its therapeutic potential. Clin. Biochem. 1999; 32: 309–319
   Google Scholar
• Thornton D. E., Jones K. H., Jiang Z., Zhang H., Liu G., Cornwell D. G. Antioxidant and cytotoxic tocopheryl quinones in normal and cancer cells. Free Radic. Biol. Med. 1995; 18: 963–976
   Google Scholar
• Traber M. G., Arai H. Molecular mechanisms of vitamin E transport. Annu. Rev. Nutr. 1999; 19: 343–355
   Google Scholar
• Traber M. G., Packer L. Vitamin E: beyond antioxidant function. Am. J. Clin. Nutr. 1995; 62(Suppl.)1501S–1509S
   Google Scholar
• Traber M. G., Winklhofer Roob B. M., Roob J. M., Khoschsorur G., Aigner R., Cross C., Ramakrishnan R., Brigelius Flohe R. Vitamin E kinetics in smokers and nonsmokers. Free Radic. Biol. Med. 2001; 31: 1368–1374
   Google Scholar
• Urata Y., Yamamoto H., Goto S., Tsushima H., Akazawa S., Yamashita S., Nagataki S., Kondo T. Long exposure to high glucose concentration impairs the responsive expression of gamma-glutamylcysteine synthetase by interleukin-1beta and tumor necrosis factor-alpha in mouse endothelial cells. J. Biol. Chem. 1996; 271: 15146–15152
   Google Scholar
• Ursini F., Maiorino M., Valente M., Ferri L., Gregolin C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta 1982; 710: 197–211
   Google Scholar
• Wang X., Quinn P. J. Vitamin E and its function in membranes. Prog. Lipid Res. 1999; 38: 309–336
   Google Scholar
• Wang X., Quinn P. J. The location and function of vitamin E in membranes (Review). Mol. Membr. Biol. 2000; 17: 143–156
   Google Scholar
• Wardman P. Conjugation and oxidation of glutathione via thiyl free radicals. Glutathione Conjugation. Mechanisms and Biological Significance, H. Sies, B. Ketterer. Academic Press, London 1988; 44–72
   Google Scholar
• Wechter W. J., Kantoci D., Murray E. D. J., D'Amico D., Jung M. E., Wang W. H. A new endogenous natriuretic factor: LLU-alpha. Proc. Natl Acad. Sci. USA 1996; 93: 6002–6007
   Google Scholar
• Weinberg R. B., VanderWerken B. S., Anderson R. A., Stegner J. E., Thomas M. J. Pro-oxidant effect of vitamin E in cigarette smokers consuming a high polyunsaturated fat diet. Arterioscler. Thromb. Vasc. Biol. 2001; 21: 1029–1033
   Google Scholar
• Whitfield J. B. Gamma glutamyl transferase. Crit. Rev. Clin. Lab. Sci. 2001; 38: 263–355
   Google Scholar
• Wijesundara M. B. J., Berger S. The redox pair vitamin E and vitamin C, a 13C-NMR study. Liebigs Ann. Chem. 1994; 1239–1241
   Google Scholar
• Wild A. C., Mulcahy R. T. Regulation of gamma-glutamylcysteine synthetase subunit gene expression: insights into transcriptional control of antioxidant defenses. Free Radic. Res. 2000; 32: 281–301
   Google Scholar
• Woods J. S., Ellis M. E. Up-regulation of glutathione synthesis in rat kidney by methyl mercury. Relationship to mercury-induced oxidative stress. Biochem. Pharmacol. 1995; 50: 1719–1724
   Google Scholar
• Yusuf S. Vitamin E supplementation and cardiovascular events in high-risk patients. The Heart Outcomes Prevention Study Investigators. N. Engl. J. Med. 2000; 342: 154–160
   Google Scholar
• Zimmer S., Stocker A., Sarbolouki M. N., Spycher S. E., Sassoon J., Azzi A. A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization. J. Biol. Chem. 2000; 275: 25672–25680
   Google Scholar