메뉴 건너뛰기




Volumn 1526, Issue 2, 2001, Pages 175-182

Effects of sialic acid residues of transferrin on the binding with aluminum and iron studied by HPLC/high-resolution ICP-MS

Author keywords

Aluminum; Carbohydrate deficient transferrin; High resolution inductively coupled plasma mass spectrometry; Iron; Sialidase; Transferrin

Indexed keywords

ALUMINUM; ALUMINUM CITRATE; ALUMINUM DERIVATIVE; ALUMINUM OXALATE; ASIALOTRANSFERRIN; BICARBONATE; CARBOHYDRATE DEFICIENT TRANSFERRIN; FERRIC ION; GLYCAN; IRON BINDING PROTEIN; IRON CITRATE; IRON DERIVATIVE; IRON OXALATE; SIALIC ACID; UNCLASSIFIED DRUG;

EID: 0343408359     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(01)00124-6     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0026500973 scopus 로고
    • Effects of dietary aluminum excess and manganese deficiency on neurobehavioral endpoints in adult mice
    • Golub M.S., Han B., Keen C.L., Gershwin M.E. Effects of dietary aluminum excess and manganese deficiency on neurobehavioral endpoints in adult mice. Toxicol. Appl. Pharmacol. 112:1992;154-160.
    • (1992) Toxicol. Appl. Pharmacol. , vol.112 , pp. 154-160
    • Golub, M.S.1    Han, B.2    Keen, C.L.3    Gershwin, M.E.4
  • 2
    • 0028314475 scopus 로고
    • Alzheimer's-disease-like changes in τ protein processing association with aluminium accumulation in brains of renal dialysis patients
    • Harrington C.R., Wischik C.M., McArthur F.K., Taylor G.A., Edwardson J.A., Candy J.M. Alzheimer's-disease-like changes in τ protein processing association with aluminium accumulation in brains of renal dialysis patients. Lancet. 343:1994;993-997.
    • (1994) Lancet , vol.343 , pp. 993-997
    • Harrington, C.R.1    Wischik, C.M.2    McArthur, F.K.3    Taylor, G.A.4    Edwardson, J.A.5    Candy, J.M.6
  • 3
    • 0345847831 scopus 로고    scopus 로고
    • Spectroscopic studies of the interaction of aluminum(III) with transferrins
    • Aramini J.M., Saponja J.A., Vogel H.J. Spectroscopic studies of the interaction of aluminum(III) with transferrins. Coord. Chem. Rev. 149:1996;193-229.
    • (1996) Coord. Chem. Rev. , vol.149 , pp. 193-229
    • Aramini, J.M.1    Saponja, J.A.2    Vogel, H.J.3
  • 5
    • 0025273624 scopus 로고
    • Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
    • Anderson B.F., Baker H.M., Norris G.E., Rumball S.V., Baker E.N. Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature. 344:1990;784-787.
    • (1990) Nature , vol.344 , pp. 784-787
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rumball, S.V.4    Baker, E.N.5
  • 7
    • 0020629655 scopus 로고
    • The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure
    • MacGillivray R.T., Mendez E., Shewale J.G., Sinha S.K., Lineback-Zins J., Brew K. The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J. Biol. Chem. 258:1983;3543-3553.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3543-3553
    • MacGillivray, R.T.1    Mendez, E.2    Shewale, J.G.3    Sinha, S.K.4    Lineback-Zins, J.5    Brew, K.6
  • 8
    • 0030087559 scopus 로고    scopus 로고
    • Separation of human serum transferrin isoforms by high-performance pellicular anion-exchange chromatography
    • Rohrer J.S., Avdalovic N. Separation of human serum transferrin isoforms by high-performance pellicular anion-exchange chromatography. Protein Expr. Purif. 7:1996;39-44.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 39-44
    • Rohrer, J.S.1    Avdalovic, N.2
  • 10
    • 0030561482 scopus 로고    scopus 로고
    • Capillary isoelectric focusing-electrospray ionization mass spectrometry for transferrin glycoforms analysis
    • Yang L., Tang Q., Harrata A.K., Lee C.S. Capillary isoelectric focusing-electrospray ionization mass spectrometry for transferrin glycoforms analysis. Anal. Biochem. 243:1996;140-149.
    • (1996) Anal. Biochem. , vol.243 , pp. 140-149
    • Yang, L.1    Tang, Q.2    Harrata, A.K.3    Lee, C.S.4
  • 11
    • 0027503288 scopus 로고
    • Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparagine-N-linked oligosaccharide transfer deficiency
    • Yamashita K., Ideo H., Ohkura T., Fukushima K., Yuasa I., Ohno K., Takeshita K. Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparagine-N-linked oligosaccharide transfer deficiency. J. Biol. Chem. 268:1993;5783-5789.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5783-5789
    • Yamashita, K.1    Ideo, H.2    Ohkura, T.3    Fukushima, K.4    Yuasa, I.5    Ohno, K.6    Takeshita, K.7
  • 12
    • 84878788105 scopus 로고
    • Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin
    • Spik G., Bayard B., Fournet B., Strecker G., Bouquelet S., Montreuil J. Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin. FEBS Lett. 50:1975;296-299.
    • (1975) FEBS Lett. , vol.50 , pp. 296-299
    • Spik, G.1    Bayard, B.2    Fournet, B.3    Strecker, G.4    Bouquelet, S.5    Montreuil, J.6
  • 14
    • 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. 37:1991;2029-2037.
    • (1991) Clin. Chem. , vol.37 , pp. 2029-2037
    • Stibler, H.1
  • 15
    • 0026629049 scopus 로고
    • Laboratory markers of ethanol intake and abuse: A critical appraisal
    • Mihas A.A., Tavassoli M. Laboratory markers of ethanol intake and abuse: a critical appraisal. Am. J. Med. Sci. 303:1992;415-428.
    • (1992) Am. J. Med. Sci. , vol.303 , pp. 415-428
    • Mihas, A.A.1    Tavassoli, M.2
  • 16
    • 0027991577 scopus 로고
    • Diagnostic utility of laboratory tests in alcoholic liver disease
    • Rosman A.S., Lieber C.S. Diagnostic utility of laboratory tests in alcoholic liver disease. Clin. Chem. 40:1994;1641-1651.
    • (1994) Clin. Chem. , vol.40 , pp. 1641-1651
    • Rosman, A.S.1    Lieber, C.S.2
  • 17
    • 0032941506 scopus 로고    scopus 로고
    • Structural studies on sugar chains of carbohydrate-deficient transferrin from patients with alcoholic liver disease using lectin affinity electrophoresis
    • Inoue T., Yamauchi M., Ohkawa K. Structural studies on sugar chains of carbohydrate-deficient transferrin from patients with alcoholic liver disease using lectin affinity electrophoresis. Electrophoresis. 20:1999;452-457.
    • (1999) Electrophoresis , vol.20 , pp. 452-457
    • Inoue, T.1    Yamauchi, M.2    Ohkawa, K.3
  • 18
    • 0028811533 scopus 로고
    • Serum carbohydrate-deficient transferrin: Mechanism of increase after chronic alcohol intake
    • Xin Y., Lasker J.M., Lieber C.S. Serum carbohydrate-deficient transferrin: mechanism of increase after chronic alcohol intake. Hepatology. 22:1995;1462-1468.
    • (1995) Hepatology , vol.22 , pp. 1462-1468
    • Xin, Y.1    Lasker, J.M.2    Lieber, C.S.3
  • 20
    • 0343169741 scopus 로고    scopus 로고
    • Carbohydrate-deficient transferrin and sialidase levels in coronary heart disease
    • Sonmez H., Ozturk Z.G., Ulutin T., Domanic N., Kokoglu E. Carbohydrate-deficient transferrin and sialidase levels in coronary heart disease. Thromb. Res. 99:2000;311-315.
    • (2000) Thromb. Res. , vol.99 , pp. 311-315
    • Sonmez, H.1    Ozturk, Z.G.2    Ulutin, T.3    Domanic, N.4    Kokoglu, E.5
  • 21
    • 0343365100 scopus 로고    scopus 로고
    • Biochemical speciation analysis by hyphenated techniques
    • Lobinski R., Szpunar J. Biochemical speciation analysis by hyphenated techniques. Anal. Chim. Acta. 400:1999;321-332.
    • (1999) Anal. Chim. Acta , vol.400 , pp. 321-332
    • Lobinski, R.1    Szpunar, J.2
  • 23
    • 0000030325 scopus 로고
    • High resolution ICP-MS: A new concept for elemental mass spectrometry
    • Giessmann U., Greb U. High resolution ICP-MS: a new concept for elemental mass spectrometry. Fresenius J. Anal. Chem. 350:(007):1994;186-193.
    • (1994) Fresenius J. Anal. Chem. , vol.350 , Issue.7 , pp. 186-193
    • Giessmann, U.1    Greb, U.2
  • 26
    • 0008128130 scopus 로고
    • The thiobarbituric acid assay of sialic acids
    • Warren L. The thiobarbituric acid assay of sialic acids. J. Biol. Chem. 234:1959;1971-1975.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1971-1975
    • Warren, L.1
  • 27
    • 0033710947 scopus 로고    scopus 로고
    • Binding patterns of co-existing aluminium and iron to human serum transferrin studied by HPLC/high resolution ICP-MS
    • Nagaoka M.H., Maitani T. Binding patterns of co-existing aluminium and iron to human serum transferrin studied by HPLC/high resolution ICP-MS. Analyst. 125:2000;1962-1965.
    • (2000) Analyst , vol.125 , pp. 1962-1965
    • Nagaoka, M.H.1    Maitani, T.2
  • 28
    • 0019540098 scopus 로고
    • The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrin
    • Chasteen N.D., Williams J. The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrin. Biochem. J. 193:1981;717-727.
    • (1981) Biochem. J. , vol.193 , pp. 717-727
    • Chasteen, N.D.1    Williams, J.2
  • 29
    • 0034684258 scopus 로고    scopus 로고
    • Differed preferential iron-binding lobe in human transferrin depending on the presence of bicarbonate detected by HPLC/high-resolution inductively coupled plasma mass spectrometry
    • Nagaoka M.H., Maitani T. Differed preferential iron-binding lobe in human transferrin depending on the presence of bicarbonate detected by HPLC/high-resolution inductively coupled plasma mass spectrometry. Biochim. Biophys. Acta. 1523:2000;182-188.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 182-188
    • Nagaoka, M.H.1    Maitani, T.2
  • 30
    • 0031435634 scopus 로고    scopus 로고
    • Serum oxalate microassay using chemiluminescence detection
    • Gaulier J.M., Cochat P., Lardet G., Vallon J.J. Serum oxalate microassay using chemiluminescence detection. Kidney Int. 52:1997;1700-1703.
    • (1997) Kidney Int. , vol.52 , pp. 1700-1703
    • Gaulier, J.M.1    Cochat, P.2    Lardet, G.3    Vallon, J.J.4
  • 31
    • 0030008682 scopus 로고    scopus 로고
    • Anion binding by transferrins: Importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin
    • Baker H.M., Anderson B.F., Brodie A.M., Shongwe M.S., Smith C.A., Baker E.N. Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin. Biochemistry. 35:1996;9007-9013.
    • (1996) Biochemistry , vol.35 , pp. 9007-9013
    • Baker, H.M.1    Anderson, B.F.2    Brodie, A.M.3    Shongwe, M.S.4    Smith, C.A.5    Baker, E.N.6
  • 32
    • 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. 253:1978;1930-1937.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 33
    • 0000048176 scopus 로고
    • Equilibrium constants for the binding of aluminum to human serum transferrin
    • Harris W.R., Sheldon J. Equilibrium constants for the binding of aluminum to human serum transferrin. Inorg. Chem. 29:1990;119-124.
    • (1990) Inorg. Chem. , vol.29 , pp. 119-124
    • Harris, W.R.1    Sheldon, J.2
  • 35
    • 0033061589 scopus 로고    scopus 로고
    • Oxalate kinetics and reversal of the complications after orthotopic liver transplantation in a patient with primary hyperoxalosis type 1 awaiting renal transplantation
    • Bastani B., Mistry B.M., Nahass G.T., Joh J., Dundoo G., Solomon H. Oxalate kinetics and reversal of the complications after orthotopic liver transplantation in a patient with primary hyperoxalosis type 1 awaiting renal transplantation. Am. J. Nephrol. 19:1999;64-69.
    • (1999) Am. J. Nephrol. , vol.19 , pp. 64-69
    • Bastani, B.1    Mistry, B.M.2    Nahass, G.T.3    Joh, J.4    Dundoo, G.5    Solomon, H.6
  • 36
    • 0021265943 scopus 로고
    • The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • Young S.P., Bomford A., Williams R. The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Biochem. J. 219:1984;505-510.
    • (1984) Biochem. J. , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 37
    • 0025947788 scopus 로고
    • Serum calcium oxalate saturation in patients on maintenance haemodialysis for primary hyperoxaluria or oxalosis-unrelated renal diseases
    • Marangella M., Petrarulo M., Vitale C., Daniele P.G., Sammartano S., Cosseddu D., Linari F. Serum calcium oxalate saturation in patients on maintenance haemodialysis for primary hyperoxaluria or oxalosis-unrelated renal diseases. Clin. Sci. 81:1991;483-490.
    • (1991) Clin. Sci. , vol.81 , pp. 483-490
    • Marangella, M.1    Petrarulo, M.2    Vitale, C.3    Daniele, P.G.4    Sammartano, S.5    Cosseddu, D.6    Linari, F.7
  • 38
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd P.M., Dwek R.A. Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32:1997;1-100.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 40
    • 0034673090 scopus 로고    scopus 로고
    • Mutation of the iron ligand His249 to Glu in the N-lobe of human transferrin abolishes the dilysine 'trigger' but does not significantly affect iron release
    • MacGillivray R.T., Bewley M.C., Smith C.A., He Q.-Y., Mason A.B., Woodworth R.C., Baker E.N. Mutation of the iron ligand His249 to Glu in the N-lobe of human transferrin abolishes the dilysine 'trigger' but does not significantly affect iron release. Biochemistry. 39:2000;1211-1216.
    • (2000) Biochemistry , vol.39 , pp. 1211-1216
    • MacGillivray, R.T.1    Bewley, M.C.2    Smith, C.A.3    He, Q.-Y.4    Mason, A.B.5    Woodworth, R.C.6    Baker, E.N.7
  • 41
    • 0033609501 scopus 로고    scopus 로고
    • Dual role of Lys206-Lys296 interaction in human transferrin N-lobe iron-release trigger and anion-binding site
    • He Q.-Y., Mason A.B., Tam B.M., MacGillivray R.T., Woodworth R.C. Dual role of Lys206-Lys296 interaction in human transferrin N-lobe iron-release trigger and anion-binding site. Biochemistry. 38:1999;9704-9711.
    • (1999) Biochemistry , vol.38 , pp. 9704-9711
    • He, Q.-Y.1    Mason, A.B.2    Tam, B.M.3    MacGillivray, R.T.4    Woodworth, R.C.5
  • 42
    • 0033961913 scopus 로고    scopus 로고
    • Transferrin and transferrin receptor function in brain barrier systems
    • Moos T., Morgan E.H. Transferrin and transferrin receptor function in brain barrier systems. Cell. Mol. Neurobiol. 20:2000;77-95.
    • (2000) Cell. Mol. Neurobiol. , vol.20 , pp. 77-95
    • Moos, T.1    Morgan, E.H.2
  • 43
    • 52849101975 scopus 로고    scopus 로고
    • Molecular modeling of human serum transferrin for rationalizing the changes in its physicochemical properties induced by iron binding. Implication of the mechanism of binding to its receptor
    • Yajima H., Sakajiri T., Kikuchi T., Morita M., Ishii T. Molecular modeling of human serum transferrin for rationalizing the changes in its physicochemical properties induced by iron binding. Implication of the mechanism of binding to its receptor. J. Protein Chem. 19:2000;215-223.
    • (2000) J. Protein Chem. , vol.19 , pp. 215-223
    • Yajima, H.1    Sakajiri, T.2    Kikuchi, T.3    Morita, M.4    Ishii, T.5
  • 44
    • 0031057660 scopus 로고    scopus 로고
    • Quantification of carbohydrate-deficient transferrin by ion-exchange chromatography with an enzymatically prepared calibrator
    • Renner F., Kanitz R.D. Quantification of carbohydrate-deficient transferrin by ion-exchange chromatography with an enzymatically prepared calibrator. Clin. Chem. 43:1997;485-490.
    • (1997) Clin. Chem. , vol.43 , pp. 485-490
    • Renner, F.1    Kanitz, R.D.2
  • 45
    • 0027173204 scopus 로고
    • Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins
    • Mason A.B., Miller M.K., Funk W.D., Banfield D.K., Savage K.J., Oliver R.W., Green B.N., MacGillivray R.T., Woodworth R.C. Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins. Biochemistry. 32:1993;5472-5479.
    • (1993) Biochemistry , vol.32 , pp. 5472-5479
    • Mason, A.B.1    Miller, M.K.2    Funk, W.D.3    Banfield, D.K.4    Savage, K.J.5    Oliver, R.W.6    Green, B.N.7    MacGillivray, R.T.8    Woodworth, R.C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.