메뉴 건너뛰기




Volumn 421, Issue , 2013, Pages 170-176

Glycation of human erythrocyte glutathione peroxidase: Effect on the physical and kinetic properties

Author keywords

Dl Glyceraldehyde; Glycation; Human erythrocyte glutathione peroxidase; Methyglyoxal; Oxidative stress

Indexed keywords

AMINO ACID; ASPARTYLTYROSYLTHREONYLGLUTAMYLMETHIONYLASPARAGYLGLUTAMYLLEUCYLGLUTAMYLARGININE; FRUCTOSE; GALACTOSE; GLUCOSE; GLUTATHIONE PEROXIDASE; GLYCERALDEHYDE; GLYOXAL; LYSYLVALYLLEUCYLGLYCYLALANYLPHENYLALANYLSERYLASPARTYLGLYCYLLEUCYLALANYLHISTIDYLLEUCYLASPARTYLASPARAGYLLEUCYLLYSINE; METHYLGLYOXAL; PHENYLALANYLLEUCYLVALYLGLYCYLPROLYLASPARTYLGLYCYLVALYLPROLYLLEUCYLARGINYLARGININE; UNCLASSIFIED DRUG; VALYLLEUCYLGLCYLALANYLPHENYLALANYLSERYLASPARTYLGLYCYLLEUCYLALANYLHISTIDYLLEUCYLASPARTYLARGINYLLEUCYLLYSINE;

EID: 84876327840     PISSN: 00098981     EISSN: 18733492     Source Type: Journal    
DOI: 10.1016/j.cca.2013.02.032     Document Type: Article
Times cited : (26)

References (41)
  • 1
    • 0000916315 scopus 로고
    • Action des acides amines sur les sucres: Formation des melanoidines par voie methodologique
    • Maillard L.C. Action des acides amines sur les sucres: Formation des melanoidines par voie methodologique. C R Hebd Acad Sci 1912, 154:66-68.
    • (1912) C R Hebd Acad Sci , vol.154 , pp. 66-68
    • Maillard, L.C.1
  • 2
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation endproducts: a review
    • Singh R., Barden A., Mori T., Beilin L. Advanced glycation endproducts: a review. Diabetologia 2001, 44:129-146.
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 3
    • 0024246725 scopus 로고    scopus 로고
    • Methods for assaying nonenzymatic glycosylation
    • Furth A.J. Methods for assaying nonenzymatic glycosylation. Anal Biochem 1998, 175:347-360.
    • (1998) Anal Biochem , vol.175 , pp. 347-360
    • Furth, A.J.1
  • 4
    • 0030477949 scopus 로고    scopus 로고
    • Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes
    • Paul R.G., Bailey A.J. Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes. Int J Biochem Cell Biol 1996, 28:1297-1310.
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1297-1310
    • Paul, R.G.1    Bailey, A.J.2
  • 5
    • 0029967887 scopus 로고    scopus 로고
    • Chronic dosing with aminoguanidine and novel advanced glycosylation end product-formation inhibitors ameliorates cross-linking of tail tendon collagen in STZ-induced diabetic rats
    • Kochakian M. Chronic dosing with aminoguanidine and novel advanced glycosylation end product-formation inhibitors ameliorates cross-linking of tail tendon collagen in STZ-induced diabetic rats. Diabetes 1996, 45:1694-1700.
    • (1996) Diabetes , vol.45 , pp. 1694-1700
    • Kochakian, M.1
  • 6
    • 0031693632 scopus 로고    scopus 로고
    • Cross-linking of proteins by Maillard processes-model reactions of d-glucose or methylglyoxal with butylamine and guanidine derivatives
    • Lederer M.O., Gerum F., Severin T. Cross-linking of proteins by Maillard processes-model reactions of d-glucose or methylglyoxal with butylamine and guanidine derivatives. Bioorg Med Chem 1998, 6:993-1002.
    • (1998) Bioorg Med Chem , vol.6 , pp. 993-1002
    • Lederer, M.O.1    Gerum, F.2    Severin, T.3
  • 7
    • 0021231172 scopus 로고
    • Nonenzymatic glycosylation and the pathogenesis of diabetic complications
    • Brownlee M., Vlassara H., Cerami A. Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann Intern Med 1984, 101:527-537.
    • (1984) Ann Intern Med , vol.101 , pp. 527-537
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 8
    • 11144324314 scopus 로고    scopus 로고
    • Advanced glycation end products-role in pathology of diabetic complications
    • Ahmed N. Advanced glycation end products-role in pathology of diabetic complications. Diabetes Res Clin Pract 2005, 67:3-21.
    • (2005) Diabetes Res Clin Pract , vol.67 , pp. 3-21
    • Ahmed, N.1
  • 10
    • 0042697530 scopus 로고    scopus 로고
    • Glycation and diabetes: the RAGE connection
    • Hudson B.I., Hofmann M.A., Bucciarelli L., et al. Glycation and diabetes: the RAGE connection. Curr Sci 2002, 83:1515-1521.
    • (2002) Curr Sci , vol.83 , pp. 1515-1521
    • Hudson, B.I.1    Hofmann, M.A.2    Bucciarelli, L.3
  • 11
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • McCance D., Dyer D.G., Dunn J.A., et al. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 1993, 91:2470-2478.
    • (1993) J Clin Invest , vol.91 , pp. 2470-2478
    • McCance, D.1    Dyer, D.G.2    Dunn, J.A.3
  • 12
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer
    • Wiseman H., Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem J 1996, 313:17-29.
    • (1996) Biochem J , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 13
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications
    • Baynes J.W., Thorpe S.R. Role of oxidative stress in diabetic complications. Diabetes 1999, 48:1-9.
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 14
    • 0032904389 scopus 로고    scopus 로고
    • Alterations in enzymatic antioxidant defense in diabetes mellitus-a rational approach
    • Szaleczky E., Prechl J., Feher J., Somogyi A. Alterations in enzymatic antioxidant defense in diabetes mellitus-a rational approach. Postgrad Med J 1999, 75:13-17.
    • (1999) Postgrad Med J , vol.75 , pp. 13-17
    • Szaleczky, E.1    Prechl, J.2    Feher, J.3    Somogyi, A.4
  • 15
    • 0022272481 scopus 로고
    • Glutathione peroxidase
    • Mannervik B. Glutathione peroxidase. Methods Enzymol 1985, 113:490-495.
    • (1985) Methods Enzymol , vol.113 , pp. 490-495
    • Mannervik, B.1
  • 16
    • 70449174079 scopus 로고
    • Hemoglobin metabolism I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative damage
    • Mills G.C. Hemoglobin metabolism I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative damage. J Biol Chem 1957, 229:189-197.
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 17
    • 0000485273 scopus 로고
    • The purification and properties of glutathione peroxidase of erthrocytes
    • Mills G.C. The purification and properties of glutathione peroxidase of erthrocytes. J Biol Chem 1958, 234:502-506.
    • (1958) J Biol Chem , vol.234 , pp. 502-506
    • Mills, G.C.1
  • 18
    • 0006466759 scopus 로고
    • Hemoglobin catabolism, II. The protection of hemoglobin from oxidative breakdown in the intact erythrocyte
    • Mills G.C., Randall H.P. Hemoglobin catabolism, II. The protection of hemoglobin from oxidative breakdown in the intact erythrocyte. J Biol Chem 1958, 232:589-598.
    • (1958) J Biol Chem , vol.232 , pp. 589-598
    • Mills, G.C.1    Randall, H.P.2
  • 19
    • 0014422738 scopus 로고
    • An intracellular GSH-peroxidase with a lipid peroxide substrate
    • Little C., O'Brien P.J. An intracellular GSH-peroxidase with a lipid peroxide substrate. Biochem Biophys Res Commun 1968, 31:145-150.
    • (1968) Biochem Biophys Res Commun , vol.31 , pp. 145-150
    • Little, C.1    O'Brien, P.J.2
  • 20
    • 0014694711 scopus 로고
    • Reduction of linolenic acid hydroperoxide by a glutathione peroxidase
    • Christophersen B.O. Reduction of linolenic acid hydroperoxide by a glutathione peroxidase. Biochim Biophys Acta 1969, 176:463-470.
    • (1969) Biochim Biophys Acta , vol.176 , pp. 463-470
    • Christophersen, B.O.1
  • 21
    • 0016769483 scopus 로고
    • Purification and properties of human erythrocyte glutathione peroxidase
    • Awasthi Y.C., Beutler E., Srivastava S.K. Purification and properties of human erythrocyte glutathione peroxidase. J Biol Chem 1975, 250:5144-5149.
    • (1975) J Biol Chem , vol.250 , pp. 5144-5149
    • Awasthi, Y.C.1    Beutler, E.2    Srivastava, S.K.3
  • 22
    • 25444488287 scopus 로고    scopus 로고
    • Nonenzymatic glycation of DNA nucleosides with reducing sugars
    • Dutta U., Cohenford M.A., Dain J.A. Nonenzymatic glycation of DNA nucleosides with reducing sugars. Anal Biochem 2005, 345:171-180.
    • (2005) Anal Biochem , vol.345 , pp. 171-180
    • Dutta, U.1    Cohenford, M.A.2    Dain, J.A.3
  • 23
    • 77958452161 scopus 로고    scopus 로고
    • Monitoring nonenzymatic glycation of human immunoglobulin G by methylglyoxal and glyoxal: a spectroscopic study
    • Pampati P.K., Suravajjala S., Dain J.A. Monitoring nonenzymatic glycation of human immunoglobulin G by methylglyoxal and glyoxal: a spectroscopic study. Anal Biochem 2011, 408:59-63.
    • (2011) Anal Biochem , vol.408 , pp. 59-63
    • Pampati, P.K.1    Suravajjala, S.2    Dain, J.A.3
  • 24
    • 43449094351 scopus 로고    scopus 로고
    • Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in ageing and disease
    • Thornalley P.J. Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in ageing and disease. Drug Metabol Drug Interact 2008, 23:125-150.
    • (2008) Drug Metabol Drug Interact , vol.23 , pp. 125-150
    • Thornalley, P.J.1
  • 25
    • 42549117517 scopus 로고    scopus 로고
    • The dicarbonyl proteome: proteins susceptible to dicarbonyl glycation at functional sites in health, aging, and disease
    • Rabbani N., Thornalley P.J. The dicarbonyl proteome: proteins susceptible to dicarbonyl glycation at functional sites in health, aging, and disease. Ann N Y Acad Sci 2008, 1126:124-127.
    • (2008) Ann N Y Acad Sci , vol.1126 , pp. 124-127
    • Rabbani, N.1    Thornalley, P.J.2
  • 26
    • 0343907218 scopus 로고    scopus 로고
    • Protein modification by a Maillard reaction intermediate methylglyoxal: immunochemical detection of fluorescent 5-methylimidazolone derivatives in vivo
    • Uchida K., Khor O.T., Oya T., Osawa T., Yasuda Y., Miyata T. Protein modification by a Maillard reaction intermediate methylglyoxal: immunochemical detection of fluorescent 5-methylimidazolone derivatives in vivo. FEBS Lett 1997, 410:313-318.
    • (1997) FEBS Lett , vol.410 , pp. 313-318
    • Uchida, K.1    Khor, O.T.2    Oya, T.3    Osawa, T.4    Yasuda, Y.5    Miyata, T.6
  • 27
    • 3342948649 scopus 로고    scopus 로고
    • Alternative routes for the formation of glyceraldehyde-derived AGEs (TAGE) in vivo
    • Takeuchi M., Yamagishi S. Alternative routes for the formation of glyceraldehyde-derived AGEs (TAGE) in vivo. Med Hypotheses 2004, 63:453-455.
    • (2004) Med Hypotheses , vol.63 , pp. 453-455
    • Takeuchi, M.1    Yamagishi, S.2
  • 28
    • 0028324241 scopus 로고
    • Glycation of albumin: reaction with glucose, fructose, dl-glyceraldehydelactose, ribose or glyceraldehyde measured using four methods
    • Syrovy I. Glycation of albumin: reaction with glucose, fructose, dl-glyceraldehydelactose, ribose or glyceraldehyde measured using four methods. J Biochem Biophys Methods 1994, 28:115-121.
    • (1994) J Biochem Biophys Methods , vol.28 , pp. 115-121
    • Syrovy, I.1
  • 29
    • 84855852834 scopus 로고    scopus 로고
    • Monitoring the effect of glyoxal and methylglyoxal glycation on the secondary structure of human serum albumin: an analysis based on CD, ESI-MALDI-TOF/MS, thermal melting profiles and UV fluorescence spectroscopy
    • Li Y., Cohenford M.A., Dutta U., Dain J.A. Monitoring the effect of glyoxal and methylglyoxal glycation on the secondary structure of human serum albumin: an analysis based on CD, ESI-MALDI-TOF/MS, thermal melting profiles and UV fluorescence spectroscopy. FASEB J 2008, 22:1057.13.
    • (2008) FASEB J , vol.22
    • Li, Y.1    Cohenford, M.A.2    Dutta, U.3    Dain, J.A.4
  • 30
    • 0032969493 scopus 로고    scopus 로고
    • Advanced glycation in d-lactose induced mouse aging model
    • Song X., Bao M., Li D., Li Y.M. Advanced glycation in d-lactose induced mouse aging model. Mech Ageing Dev 1999, 108:239-251.
    • (1999) Mech Ageing Dev , vol.108 , pp. 239-251
    • Song, X.1    Bao, M.2    Li, D.3    Li, Y.M.4
  • 31
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0016167076 scopus 로고
    • The Direct Linear Plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal R., Cornish-Bowden A. The Direct Linear Plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem J 1974, 139:715-720.
    • (1974) Biochem J , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 34
    • 33845184448 scopus 로고
    • Preparation and evaluation of packed capillary liquid chromatography columns with inner diameters from 20 to 50μm
    • Kennedy R.T., Jorgensen J.W. Preparation and evaluation of packed capillary liquid chromatography columns with inner diameters from 20 to 50μm. Anal Chem 1989, 61:1128-1135.
    • (1989) Anal Chem , vol.61 , pp. 1128-1135
    • Kennedy, R.T.1    Jorgensen, J.W.2
  • 35
    • 0034176220 scopus 로고    scopus 로고
    • ω-carboxymethylarginine as a novel acid-labile advanced glycation end product in collagen
    • ω-carboxymethylarginine as a novel acid-labile advanced glycation end product in collagen. Biochem J 2000, 347:23-27.
    • (2000) Biochem J , vol.347 , pp. 23-27
    • Lijima, K.1    Murata, M.2    Takahara, H.3    Irie, S.4    Fujimoto, D.5
  • 36
    • 0037306962 scopus 로고    scopus 로고
    • Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185
    • Park Y.S., Koh Y.H., Takahashi M., et al. Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185. Free Radic Res 2003, 37:205-211.
    • (2003) Free Radic Res , vol.37 , pp. 205-211
    • Park, Y.S.1    Koh, Y.H.2    Takahashi, M.3
  • 37
    • 33845927118 scopus 로고    scopus 로고
    • Peptide mapping of human hemoglobin modified minimally by methylglyoxal in vitro
    • Chen Y., Ahmed N., Thornalley P.J. Peptide mapping of human hemoglobin modified minimally by methylglyoxal in vitro. Ann N Y Acad Sci 2005, 1043:905.
    • (2005) Ann N Y Acad Sci , vol.1043 , pp. 905
    • Chen, Y.1    Ahmed, N.2    Thornalley, P.J.3
  • 39
    • 0030694740 scopus 로고    scopus 로고
    • Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase
    • Yan H., Harding J.J. Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase. Biochem J 1997, 328:599-605.
    • (1997) Biochem J , vol.328 , pp. 599-605
    • Yan, H.1    Harding, J.J.2
  • 40
    • 34247540770 scopus 로고    scopus 로고
    • Lack of the antioxidant enzyme glutathione peroxidase-1 accelerates atherosclerosis in diabetic apolipoprotein E - deficient mice
    • Lewis P., Stefanovic N., Pete J., et al. Lack of the antioxidant enzyme glutathione peroxidase-1 accelerates atherosclerosis in diabetic apolipoprotein E - deficient mice. Circulation 2007, 115:2178-2187.
    • (2007) Circulation , vol.115 , pp. 2178-2187
    • Lewis, P.1    Stefanovic, N.2    Pete, J.3
  • 41
    • 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 1967, 70:158-169.
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.