메뉴 건너뛰기




Volumn 50, Issue 9, 2004, Pages 1640-1649

Effects of in vitro glycation on Fe3+ binding and Fe 3+ isoforms of transferrin

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC ION; FERROUS CHLORIDE; GLUCOSE; ISOPROTEIN; NITRILOTRIACETATE IRON; TRANSFERRIN;

EID: 4344640572     PISSN: 00099147     EISSN: None     Source Type: Journal    
DOI: 10.1373/clinchem.2004.033811     Document Type: Article
Times cited : (29)

References (53)
  • 3
    • 0028670369 scopus 로고
    • Purification of isotransferrins by concanavalin A Sepharose chromatography and preparative isoelectric focusing
    • van Noort WL, de Jong G, van Eijk HG. Purification of isotransferrins by concanavalin A Sepharose chromatography and preparative isoelectric focusing. Eur J Clin Chem Clin Biochem 1994;32:885-92.
    • (1994) Eur J Clin Chem Clin Biochem , vol.32 , pp. 885-892
    • Van Noort, W.L.1    De Jong, G.2    Van Eijk, H.G.3
  • 4
    • 0026682589 scopus 로고
    • The analysis of human serum transferrins with the Phastsystem: Quantitation of microheterogeneity
    • van Eijk HG, van Noort WL. The analysis of human serum transferrins with the Phastsystem: quantitation of microheterogeneity. Electrophoresis 1992;13:354-8.
    • (1992) Electrophoresis , vol.13 , pp. 354-358
    • Van Eijk, H.G.1    Van Noort, W.L.2
  • 5
    • 0020422695 scopus 로고
    • Superoxide-dependent formation of hydroxyl radical and lipid peroxidation in the presence of iron salts. Detection of 'catalytic' iron and anti-oxidant activity in extracellular fluids
    • Gutteridge JM, Rowley DA, Halliwell B. Superoxide-dependent formation of hydroxyl radical and lipid peroxidation in the presence of iron salts. Detection of 'catalytic' iron and anti-oxidant activity in extracellular fluids. Biochem J 1982;206:605-9.
    • (1982) Biochem J , vol.206 , pp. 605-609
    • Gutteridge, J.M.1    Rowley, D.A.2    Halliwell, B.3
  • 7
    • 0025732948 scopus 로고
    • Role of oxidative stress in the development of complications in diabetes
    • Baynes JW. Role of oxidative stress in the development of complications in diabetes. Diabetes 1991;40:405-12.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 8
    • 0027279232 scopus 로고
    • Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications
    • Wolff SP. Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications. Br Med Bull 1993;49:642-52.
    • (1993) Br Med Bull , vol.49 , pp. 642-652
    • Wolff, S.P.1
  • 9
    • 0024469459 scopus 로고
    • Deferoxamine therapy in high-ferritin diabetes
    • Cutler P. Deferoxamine therapy in high-ferritin diabetes. Diabetes 1989;38:1207-10.
    • (1989) Diabetes , vol.38 , pp. 1207-1210
    • Cutler, P.1
  • 10
    • 0031033103 scopus 로고    scopus 로고
    • Body iron stores are associated with serum insulin and blood glucose concentrations. Population study in 1,013 eastern Finnish men
    • Tuomainen TP, Nyyssönen K, Salonen R, Tervahauta A, Korpela H, Lakka T, et al. Body iron stores are associated with serum insulin and blood glucose concentrations. Population study in 1,013 eastern Finnish men. Diabetes Care 1997;20:426-8.
    • (1997) Diabetes Care , vol.20 , pp. 426-428
    • Tuomainen, T.P.1    Nyyssönen, K.2    Salonen, R.3    Tervahauta, A.4    Korpela, H.5    Lakka, T.6
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0035894425 scopus 로고    scopus 로고
    • A fluorescence-based one-step assay for serum non-transferrin-bound iron
    • Breuer W, Cabantchik ZI. A fluorescence-based one-step assay for serum non-transferrin-bound iron. Anal Biochem 2001;299:194-202.
    • (2001) Anal Biochem , vol.299 , pp. 194-202
    • Breuer, W.1    Cabantchik, Z.I.2
  • 15
    • 0031451545 scopus 로고    scopus 로고
    • The relation between chemically measured total iron-binding capacity concentrations and immunologically measured transferrin concentrations in human serum
    • Gambino R, Desvarieux E, Orth M, Matan H, Ackattupathil T, Lijoi E, et al. The relation between chemically measured total iron-binding capacity concentrations and immunologically measured transferrin concentrations in human serum. Clin Chem 1997;43:2408-12.
    • (1997) Clin Chem , vol.43 , pp. 2408-2412
    • Gambino, R.1    Desvarieux, E.2    Orth, M.3    Matan, H.4    Ackattupathil, T.5    Lijoi, E.6
  • 16
    • 0345712890 scopus 로고
    • Separation of human serum and cerebrospinal fluid transferrins in subfractions by isoelectric focusing with Phastsystem™ and quantitationswith the Ultroscan™ XL densitometer
    • van Noort WL, van Eijk HG. Separation of human serum and cerebrospinal fluid transferrins in subfractions by isoelectric focusing with Phastsystem™ and quantitationswith the Ultroscan™ XL densitometer. Sci Tools 1992;36:1-6.
    • (1992) Sci Tools , vol.36 , pp. 1-6
    • Van Noort, W.L.1    Van Eijk, H.G.2
  • 17
    • 0023732385 scopus 로고
    • Microheterogeneity of human serum transferrin: A biological phenomenon studied by isoelectric focusing in immobilized pH gradients
    • de Jong G, van Eijk HG. Microheterogeneity of human serum transferrin: a biological phenomenon studied by isoelectric focusing in immobilized pH gradients. Electrophoresis 1988;9:589-98.
    • (1988) Electrophoresis , vol.9 , pp. 589-598
    • De Jong, G.1    Van Eijk, H.G.2
  • 19
    • 0027485958 scopus 로고
    • The carbohydrate-deficient glycoprotein syndromes: An overview
    • Jaeken J, Carchon H. The carbohydrate-deficient glycoprotein syndromes: an overview. J Inherit Metab Dis 1993;16:813-20.
    • (1993) J Inherit Metab Dis , vol.16 , pp. 813-820
    • Jaeken, J.1    Carchon, H.2
  • 20
    • 0026331891 scopus 로고
    • Carbohydrate-deficient transferrin in serum: A new marker of potentially harmful alcohol consumption reviewed
    • Stibler H. Carbohydrate-deficient transferrin in serum: a new marker of potentially harmful alcohol consumption reviewed. Clin Chem 1991;37:2029-37.
    • (1991) Clin Chem , vol.37 , pp. 2029-2037
    • Stibler, H.1
  • 21
    • 0031677587 scopus 로고    scopus 로고
    • Smoking, obesity, and hypertension alter the dose-response curve and test sensitivity of carbohydrate-deficient transferrin as a marker of alcohol intake
    • Whitfield JB, Fletcher LM, Murphy TL, Powell LW, Halliday J, Heath AC, et al. Smoking, obesity, and hypertension alter the dose-response curve and test sensitivity of carbohydrate-deficient transferrin as a marker of alcohol intake. Clin Chem 1998;44:2480-9.
    • (1998) Clin Chem , vol.44 , pp. 2480-2489
    • Whitfield, J.B.1    Fletcher, L.M.2    Murphy, T.L.3    Powell, L.W.4    Halliday, J.5    Heath, A.C.6
  • 22
    • 0022538777 scopus 로고
    • Nonrandom distribution of iron in circulating human transferrin
    • Zak O, Aisen P. Nonrandom distribution of iron in circulating human transferrin. Blood 1986;68:157-61.
    • (1986) Blood , vol.68 , pp. 157-161
    • Zak, O.1    Aisen, P.2
  • 23
    • 0034111879 scopus 로고    scopus 로고
    • Transferrin microheterogeneity in human perilymph
    • Rauch SD. Transferrin microheterogeneity in human perilymph. The Laryngoscope 2000;110:545-52.
    • (2000) The Laryngoscope , vol.110 , pp. 545-552
    • Rauch, S.D.1
  • 24
    • 0029117744 scopus 로고
    • Effect of separation conditions on automated isoelectric focusing of carbohydrate-deficient transferrin and other human isotransferrins using the PhastSystem
    • Hackler R, Arndt T, Tilmann KO, Gressner AM. Effect of separation conditions on automated isoelectric focusing of carbohydrate-deficient transferrin and other human isotransferrins using the PhastSystem. Anal Biochem 1995;230:281-9.
    • (1995) Anal Biochem , vol.230 , pp. 281-289
    • Hackler, R.1    Arndt, T.2    Tilmann, K.O.3    Gressner, A.M.4
  • 25
    • 0040258965 scopus 로고
    • The specific binding of iron(III) and copper(II) to transferrin and conalbumin
    • Aasa R, Malmstroem BG, Saltman P. The specific binding of iron(III) and copper(II) to transferrin and conalbumin. Biochim Biophys Acta 1963;75:203-22.
    • (1963) Biochim Biophys Acta , vol.75 , pp. 203-222
    • Aasa, R.1    Malmstroem, B.G.2    Saltman, P.3
  • 26
    • 0021107162 scopus 로고
    • Thermodyncimic binding constants for gallium transferrin
    • Harris WR, Pecoraro VL. Thermodyncimic binding constants for gallium transferrin. Biochemistry 1983;22:292-9.
    • (1983) Biochemistry , vol.22 , pp. 292-299
    • Harris, W.R.1    Pecoraro, V.L.2
  • 27
    • 0020972548 scopus 로고
    • Thermodynamic binding constants of the zinc-human serum transferrin complex
    • Harris WR. Thermodynamic binding constants of the zinc-human serum transferrin complex. Biochemistry 1983;22:3920-6.
    • (1983) Biochemistry , vol.22 , pp. 3920-3926
    • Harris, W.R.1
  • 29
  • 30
    • 0028362372 scopus 로고
    • Structure-function relationship in the serotransferrin: The role of the pH on the conformational change and the metal ions release
    • Congiu-Castellano A, Barteri M, Castagnola M, Bianconi A, Borghi E, Della Longa S. Structure-function relationship in the serotransferrin: the role of the pH on the conformational change and the metal ions release. Biochem Biophys Res Commun 1994;198:646-52.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 646-652
    • Congiu-Castellano, A.1    Barteri, M.2    Castagnola, M.3    Bianconi, A.4    Borghi, E.5    Della Longa, S.6
  • 31
    • 0030719939 scopus 로고    scopus 로고
    • The pH dependent properties of metallotransferrins: A comparative study
    • Messori L, Poggetto GD, Monnanni R, Hirose J. The pH dependent properties of metallotransferrins: a comparative study. Biometals 1997;10:303-13.
    • (1997) Biometals , vol.10 , pp. 303-313
    • Messori, L.1    Poggetto, G.D.2    Monnanni, R.3    Hirose, J.4
  • 32
    • 0016669917 scopus 로고
    • 3+ by transferrin. Implications for the interlocking sites hypothesis
    • 3+ by transferrin. Implications for the interlocking sites hypothesis. J Biol Chem 1975;250:2182-8.
    • (1975) J Biol Chem , vol.250 , pp. 2182-2188
    • Schlabach, M.R.1    Bates, G.W.2
  • 33
    • 0037062620 scopus 로고    scopus 로고
    • The synergistic anion-binding sites of human transferrin: Chemical and physiological effects of site-directed mutagenesis
    • Zak O, Ikuta K, Aisen P. The synergistic anion-binding sites of human transferrin: chemical and physiological effects of site-directed mutagenesis. Biochemistry 2002;41:7416-23.
    • (2002) Biochemistry , vol.41 , pp. 7416-7423
    • Zak, O.1    Ikuta, K.2    Aisen, P.3
  • 34
    • 0015919687 scopus 로고
    • The reaction of ferric salts with transferrin
    • Bates GW, Schlabach MR. The reaction of ferric salts with transferrin. J Biol Chem 1973;248:3228-32.
    • (1973) J Biol Chem , vol.248 , pp. 3228-3232
    • Bates, G.W.1    Schlabach, M.R.2
  • 35
    • 0015217866 scopus 로고
    • The kinetics and mechanism of iron(III) exchange between chelates and transferrin. IV. The reaction of transferrin with iron(III) nitrilotriacetate
    • Bates GW, Wernicke J. The kinetics and mechanism of iron(III) exchange between chelates and transferrin. IV. The reaction of transferrin with iron(III) nitrilotriacetate. J Biol Chem 1971;246:3679-85.
    • (1971) J Biol Chem , vol.246 , pp. 3679-3685
    • Bates, G.W.1    Wernicke, J.2
  • 36
    • 0014216782 scopus 로고
    • The kinetics and mechanism of iron(III) exchange between chelates and transferrin. I. The complexes of citrate and nitrilotriacetic acid
    • Bates GW, Billups C, Saltman P. The kinetics and mechanism of iron(III) exchange between chelates and transferrin. I. The complexes of citrate and nitrilotriacetic acid. J Biol Chem 1967;242:2810-5.
    • (1967) J Biol Chem , vol.242 , pp. 2810-2815
    • Bates, G.W.1    Billups, C.2    Saltman, P.3
  • 37
    • 0026069823 scopus 로고
    • Receptor-modulated iron release from transferrin: Differential effects on N- and C-terminal sites
    • Bali PK, Aisen P. Receptor-modulated iron release from transferrin: differential effects on N- and C-terminal sites. Biochemistry 1991;30:9947-52.
    • (1991) Biochemistry , vol.30 , pp. 9947-9952
    • Bali, P.K.1    Aisen, P.2
  • 38
    • 0037199442 scopus 로고    scopus 로고
    • Differential effect of a His tag at the N- and C-termini: Functional studies with recombinant human serum transferrin
    • Mason AB, He QY, Halbrooks PJ, Evers SJ, Gumerov DR, Kaltashov IA, et al. Differential effect of a His tag at the N- and C-termini: functional studies with recombinant human serum transferrin. Biochemistry 2002;41:9448-54.
    • (2002) Biochemistry , vol.41 , pp. 9448-9454
    • Mason, A.B.1    He, Q.Y.2    Halbrooks, P.J.3    Evers, S.J.4    Gumerov, D.R.5    Kaltashov, I.A.6
  • 39
    • 0017885589 scopus 로고
    • Stoichiometric and site characteristics of the binding of iron to human transferrin
    • Aisen P, Leibman A, Zweier J. Stoichiometric and site characteristics of the binding of iron to human transferrin. J Biol Chem 1978;253:1930-7.
    • (1978) J Biol Chem , vol.253 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 40
    • 0022911361 scopus 로고
    • The influence of uncoordinated histidines on iron release from transferrin. A chemical modification study
    • Thompson CP, Grady JK, Chasteen ND. The influence of uncoordinated histidines on iron release from transferrin. A chemical modification study. J Biol Chem 1986;261:13128-34.
    • (1986) J Biol Chem , vol.261 , pp. 13128-13134
    • Thompson, C.P.1    Grady, J.K.2    Chasteen, N.D.3
  • 41
    • 0028263972 scopus 로고
    • Primary receptor-recognition site of human transferrin is in the C-terminal lobe
    • Zak O, Trinder D, Aisen P. Primary receptor-recognition site of human transferrin is in the C-terminal lobe. J Biol Chem 1994;269:7110-4.
    • (1994) J Biol Chem , vol.269 , pp. 7110-7114
    • Zak, O.1    Trinder, D.2    Aisen, P.3
  • 43
    • 0022341310 scopus 로고
    • Quantification of apo-, mono-, and diferric transferrin by polyacrylamide gradient gel electrophoresis in patients with disorders of iron metabolism
    • DiRusso SC, Check IJ, Hunter RL. Quantification of apo-, mono-, and diferric transferrin by polyacrylamide gradient gel electrophoresis in patients with disorders of iron metabolism. Blood 1985;66:1445-51.
    • (1985) Blood , vol.66 , pp. 1445-1451
    • DiRusso, S.C.1    Check, I.J.2    Hunter, R.L.3
  • 44
    • 0023904072 scopus 로고
    • Random distribution of iron among the two binding sites of transferrin in patients with various hematologic disorders
    • Beguin Y, Huebers HA, Finch CA. Random distribution of iron among the two binding sites of transferrin in patients with various hematologic disorders. Clin Chim Acta 1988;173:299-304.
    • (1988) Clin Chim Acta , vol.173 , pp. 299-304
    • Beguin, Y.1    Huebers, H.A.2    Finch, C.A.3
  • 45
    • 0018671415 scopus 로고
    • Distribution of iron between the binding sites of transferrin in serum: Methods and results in normal human subjects
    • Leibman A, Aisen P. Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects. Blood 1979;53:1058-65.
    • (1979) Blood , vol.53 , pp. 1058-1065
    • Leibman, A.1    Aisen, P.2
  • 46
    • 0018849946 scopus 로고
    • The distribution of iron between the metal-binding sites of transferrin human serum
    • Williams J, Moreton K. The distribution of iron between the metal-binding sites of transferrin human serum. Biochem J 1980;185:483-8.
    • (1980) Biochem J , vol.185 , pp. 483-488
    • Williams, J.1    Moreton, K.2
  • 47
    • 4344660249 scopus 로고
    • Chemical, clinical and immunological studies on the products of human plasma fractionation. XXXVII. The metal-combining globulin of human plasma
    • Surgenor DM, Koechlin BA, Strong LE. Chemical, clinical and immunological studies on the products of human plasma fractionation. XXXVII. The metal-combining globulin of human plasma. J Clin Invest 1949;28:73.
    • (1949) J Clin Invest , vol.28 , pp. 73
    • Surgenor, D.M.1    Koechlin, B.A.2    Strong, L.E.3
  • 48
    • 0032544387 scopus 로고    scopus 로고
    • Transition metals bind to glycated proteins forming redox active "glycochelates": Implications for the pathogenesis of certain diabetic complications
    • Qian M, Liu M, Eaton JW. Transition metals bind to glycated proteins forming redox active "glycochelates": implications for the pathogenesis of certain diabetic complications. Biochem Biophys Res Commun 1998;250:385-9.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 385-389
    • Qian, M.1    Liu, M.2    Eaton, J.W.3
  • 49
    • 0028987361 scopus 로고
    • Nonenzymatic glycation of transferrin: Decrease of iron-binding capacity and increase of oxygen radical production
    • Fujimoto S, Kawakami N, Ohara A. Nonenzymatic glycation of transferrin: decrease of iron-binding capacity and increase of oxygen radical production. Biol Pharm Bull 1995;18:396-400.
    • (1995) Biol Pharm Bull , vol.18 , pp. 396-400
    • Fujimoto, S.1    Kawakami, N.2    Ohara, A.3
  • 50
    • 0026760413 scopus 로고
    • Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: The important primary role for iron-binding and iron-oxidising proteins
    • Gutteridge JM, Quintan GJ. Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins. Biochim Biophys Acta 1992;1159:248-54.
    • (1992) Biochim Biophys Acta , vol.1159 , pp. 248-254
    • Gutteridge, J.M.1    Quintan, G.J.2
  • 51
    • 0034222359 scopus 로고    scopus 로고
    • The structural mechanism for iron uptake and release by transferrins
    • Hirose M. The structural mechanism for iron uptake and release by transferrins. Biosci Biotechnol Biochem 2000;64:1328-36.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1328-1336
    • Hirose, M.1
  • 52
    • 0023484114 scopus 로고
    • Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients
    • Austin GE, Mullins RH, Morin LG. Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients. Clin Chem 1987;33;2220-4.
    • (1987) Clin Chem , vol.33 , pp. 2220-2224
    • Austin, G.E.1    Mullins, R.H.2    Morin, L.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.