메뉴 건너뛰기




Volumn 1620, Issue 1-3, 2003, Pages 125-132

Covalent coupling of reduced glutathione with ribose: Loss of cosubstrate ability to glutathione peroxidase

Author keywords

Amadori; Diabetes; Glutathione; Glycation; Mass spectrometry; Ribose

Indexed keywords

GLUTATHIONE; GLUTATHIONE PEROXIDASE; RIBOSE;

EID: 12244253350     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00525-1     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0025317268 scopus 로고
    • Glutathione: Toxicological implications
    • Reed D.J. Glutathione: toxicological implications. Annu. Rev. Pharmacol. Toxicol. 30:1990;603-631.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 603-631
    • Reed, D.J.1
  • 2
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 263:1988;17205-17208.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 6
    • 0032062824 scopus 로고    scopus 로고
    • Identification of deoxy-D-fructosyl phosphatidylethanolamine as a non-enzymic glycation product of phosphatidylethanolamine and its occurrence in human blood plasma and red blood cells
    • Lertsiri S., Shiraishi M., Miyazawa T. Identification of deoxy-D-fructosyl phosphatidylethanolamine as a non-enzymic glycation product of phosphatidylethanolamine and its occurrence in human blood plasma and red blood cells. Biosci. Biotechnol. Biochem. 62:1998;893-901.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 893-901
    • Lertsiri, S.1    Shiraishi, M.2    Miyazawa, T.3
  • 7
    • 0025769713 scopus 로고
    • Non-enzymic glycation of human extracellular superoxide dismutases
    • Adachi T., Ohta H., Hirano K., Hayashi K., Marklund S.L. Non-enzymic glycation of human extracellular superoxide dismutases. Biochem. J. 279:1991;263-267.
    • (1991) Biochem. J. , vol.279 , pp. 263-267
    • Adachi, T.1    Ohta, H.2    Hirano, K.3    Hayashi, K.4    Marklund, S.L.5
  • 8
    • 0026482539 scopus 로고
    • Glycation (non-enzymic glycosylation) inactivates glutathione reductase
    • Blakytny R., Harding J. Glycation (non-enzymic glycosylation) inactivates glutathione reductase. Biochem. J. 288:1992;303-307.
    • (1992) Biochem. J. , vol.288 , pp. 303-307
    • Blakytny, R.1    Harding, J.2
  • 9
    • 0028075417 scopus 로고
    • ELISA for in vivo assessment of nonenzymatically glycated platelet glutathione peroxidase
    • Muruganandam A., Tannous M., Mutus B. ELISA for in vivo assessment of nonenzymatically glycated platelet glutathione peroxidase. Clin. Biochem. 27:1994;293-298.
    • (1994) Clin. Biochem. , vol.27 , pp. 293-298
    • Muruganandam, A.1    Tannous, M.2    Mutus, B.3
  • 10
    • 0027255884 scopus 로고
    • Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation
    • Hunt J.V., Bottoms M.A., Mitchinson M.J. Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Biochem. J. 291:1993;529-535.
    • (1993) Biochem. J. , vol.291 , pp. 529-535
    • Hunt, J.V.1    Bottoms, M.A.2    Mitchinson, M.J.3
  • 12
    • 0032971837 scopus 로고    scopus 로고
    • Advanced glycosylated end products and hyperglycemia in the pathogenesis of diabetic complications
    • Friedman E.A. Advanced glycosylated end products and hyperglycemia in the pathogenesis of diabetic complications. Diabetes Care. 22:1999;B65-B71.
    • (1999) Diabetes Care , vol.22
    • Friedman, E.A.1
  • 13
    • 0028897751 scopus 로고
    • Diabetes mellitus, hypertension and cardiovascular disease: Which role for oxidative stress?
    • Guigliano D., Ceriello A., Paolisso G. Diabetes mellitus, hypertension and cardiovascular disease: which role for oxidative stress? Metabolism. 44:1995;363-368.
    • (1995) Metabolism , vol.44 , pp. 363-368
    • Guigliano, D.1    Ceriello, A.2    Paolisso, G.3
  • 14
    • 0022358787 scopus 로고
    • Platelet glutathione and thromboxane synthesis in diabetes
    • Thomas G., Skrinska V., Lucas F.V., Schumacher O.P. Platelet glutathione and thromboxane synthesis in diabetes. Diabetes. 34:1985;951-954.
    • (1985) Diabetes , vol.34 , pp. 951-954
    • Thomas, G.1    Skrinska, V.2    Lucas, F.V.3    Schumacher, O.P.4
  • 15
    • 0033010117 scopus 로고    scopus 로고
    • Resistance to glutathione depletion in diabetic and non-diabetic human erythrocytes in vitro
    • Coleman M.D., Rustioni C. Resistance to glutathione depletion in diabetic and non-diabetic human erythrocytes in vitro. J. Pharm. Pharmacol. 51:1999;21-25.
    • (1999) J. Pharm. Pharmacol. , vol.51 , pp. 21-25
    • Coleman, M.D.1    Rustioni, C.2
  • 16
    • 0028234886 scopus 로고
    • Rapid determination of glutathione status in fish liver using high-performance liquid chromatography and electrochemical detection
    • Rodriguez-Ariza A., Toribio F., Lopez-Barea J. Rapid determination of glutathione status in fish liver using high-performance liquid chromatography and electrochemical detection. J. Chromatogr., B Biomed. Sci. Appl. 656:1994;311-318.
    • (1994) J. Chromatogr., B Biomed. Sci. Appl. , vol.656 , pp. 311-318
    • Rodriguez-Ariza, A.1    Toribio, F.2    Lopez-Barea, J.3
  • 18
    • 0024322509 scopus 로고
    • Glutathione measurement by high-performance liquid chromatography separation and fluorimetric detection of the glutathione-orthophtalaldehyde adduct
    • Neuschwander-Tetri B.A., Roll F.J. Glutathione measurement by high-performance liquid chromatography separation and fluorimetric detection of the glutathione-orthophtalaldehyde adduct. Anal. Biochem. 179:1989;236-241.
    • (1989) Anal. Biochem. , vol.179 , pp. 236-241
    • Neuschwander-Tetri, B.A.1    Roll, F.J.2
  • 19
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia D.E., Valentine W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70:1967;158-169.
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 20
    • 0019796775 scopus 로고
    • Reaction of monosaccharides with proteins: Possible evolutionary significance
    • Bunn H.F., Higgins P.J. Reaction of monosaccharides with proteins: possible evolutionary significance. Science. 213:1981;222-224.
    • (1981) Science , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 21
    • 0021983381 scopus 로고
    • Aldehydes or dicarbonyls in non-enzymic glycosylation of proteins
    • Beswick H.T., Harding J.J. Aldehydes or dicarbonyls in non-enzymic glycosylation of proteins. Biochem. J. 226:1985;385-389.
    • (1985) Biochem. J. , vol.226 , pp. 385-389
    • Beswick, H.T.1    Harding, J.J.2
  • 22
    • 0029995384 scopus 로고    scopus 로고
    • Kinetics of nonenzymatic glycation of ribonuclease A leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-amadori studies
    • Khalifah R.J., Todd P., Ashley Booth A., Yang S.X., Mott J.D., Hudson B.G. Kinetics of nonenzymatic glycation of ribonuclease A leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-amadori studies. Biochemistry. 35:1996;4645-4654.
    • (1996) Biochemistry , vol.35 , pp. 4645-4654
    • Khalifah, R.J.1    Todd, P.2    Ashley Booth, A.3    Yang, S.X.4    Mott, J.D.5    Hudson, B.G.6
  • 23
    • 0028873846 scopus 로고
    • Non-enzymatic glycation of fibrous collagen: Reaction products of glucose and ribose
    • Bailey A.J., Sims T.J., Avery N.C., Halligan E.P. Non-enzymatic glycation of fibrous collagen: reaction products of glucose and ribose. Biochem. J. 305:1995;385-390.
    • (1995) Biochem. J. , vol.305 , pp. 385-390
    • Bailey, A.J.1    Sims, T.J.2    Avery, N.C.3    Halligan, E.P.4
  • 24
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix
    • Sell D.R., Monnier V.M. Structure elucidation of a senescence cross-link from human extracellular matrix. J. Biol. Chem. 264:1989;21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 25
    • 0025948114 scopus 로고
    • Mechanism of formation of the maillard protein cross-link pentosidine
    • Grandhee S.K., Monnier V.M. Mechanism of formation of the maillard protein cross-link pentosidine. J. Biol. Chem. 266:1991;11649-11653.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11649-11653
    • Grandhee, S.K.1    Monnier, V.M.2
  • 26
    • 0026501919 scopus 로고
    • Chromatographic quantitation of plasma and erythrocyte pentosidine in diabetic and uremic subjects
    • Odetti P., Fogarty J., Sell D.R., Monnier V.M. Chromatographic quantitation of plasma and erythrocyte pentosidine in diabetic and uremic subjects. Diabetes. 41:1992;153-159.
    • (1992) Diabetes , vol.41 , pp. 153-159
    • Odetti, P.1    Fogarty, J.2    Sell, D.R.3    Monnier, V.M.4
  • 28
    • 0025174842 scopus 로고
    • End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen
    • Sell D.R., Monnier V.M. End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen. J. Clin. Invest. 85:1990;380-384.
    • (1990) J. Clin. Invest. , vol.85 , pp. 380-384
    • Sell, D.R.1    Monnier, V.M.2
  • 29
    • 0026315675 scopus 로고
    • Effect of protein concentration on the formation of glycated albumin and fructosamine
    • Lamb E., Mainwaring-Burton R., Dawnay A. Effect of protein concentration on the formation of glycated albumin and fructosamine. Clin. Chem. 37:1991;2138-2139.
    • (1991) Clin. Chem. , vol.37 , pp. 2138-2139
    • Lamb, E.1    Mainwaring-Burton, R.2    Dawnay, A.3
  • 31
    • 0000704119 scopus 로고
    • The selenoprotein glutathione peroxidase
    • D. Dolphin, R. Poulson, & O. Avramovic. New-York: Wiley
    • Flohé L. The selenoprotein glutathione peroxidase. Dolphin D., Poulson R., Avramovic O. Glutathione: Chemical, Biochemical and Medical Aspects. 1989;643-731 Wiley, New-York.
    • (1989) Glutathione: Chemical, Biochemical and Medical Aspects , pp. 643-731
    • Flohé, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.