Binding patterns of vanadium ions with different valence states to human serum transferrin studied by HPLC/high-resolution ICP-MS

Biochemical and Biophysical Research Communications

Volumn 296, Issue 5, 2002, Pages 1207-1214

  Nagaoka, Megumi Hamano ^a   Yamazaki, Takeshi ^a   Maitani, Tamio ^a  

^a NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

Author keywords

Binding affinity; High resolution inductively coupled plasma mass spectrometry; HR ICP MS; ICP MS; Open form; Transferrin; Valence state; Vanadium

Indexed keywords

BICARBONATE; PLASMA PROTEIN; TRANSFERRIN; VANADIUM;

ARTICLE; BINDING AFFINITY; COMPARATIVE STUDY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN BINDING;

APOPROTEINS; BICARBONATES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; INSULIN; IONS; KINETICS; MASS SPECTROMETRY; PROTEIN BINDING; SENSITIVITY AND SPECIFICITY; TRANSFERRIN; UREA; VANADIUM;

MAMMALIA;

EID: 0036387123     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02067-3     Document Type: Article

References (32)

1. J.M. Aramini, J.A. Saponja, H.J. Vogel, Spectroscopic studies of the interaction of aluminum(III) with transferrins, Coord. Chem. Rev. 149 (1996) 193-229.
2. P.F. Lindley, Transferrins, in: A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt (Eds.), Handbook of Metalloproteins, vol. 2, Wiley, Chichester, 2001, pp. 793-811.
3. B.F. Anderson, H.M. Baker, G.E. Norris, S.V. Rumball, E.N. Baker, Apolactoferrin structure demonstrates ligand-induced conformational change in transferrin, Nature 344 (1990) 784-787.
4. R.T. MacGillivray, E. Mendez, J.G. Shewale, S.K. Sinha, J. Lineback-Zins, K. Brew, 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.
5. D.C. Harris, P. Aisen, Iron-donating properties of transferrin, Biochemistry 14 (1975) 262-268.
6. C.A. Smith, B.F. Anderson, H.M. Baker, E.N. Baker, Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-A resolution, Biochemistry 31 (1992) 4527-4533.
7. H. Sun, M.C. Cox, H. Li, P.J. Sadler, Rationalisation of metal binding to transferrin: prediction of metal-protein stability constants, Structure and Bonding 88 (1997) 71-102.
8. M.H. Nagaoka, T. Maitani, 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.
9. M.H. Nagaoka, T. Maitani, Binding patterns of co-existing aluminium and iron to human serum transferrin studied by HPLC-high-resolution ICP-MS, Analyst 125 (2000) 1962-1965.
10. K. Schwarz, D.B. Milne, Growth effects of vanadium in the rat, Science 174 (1971) 426-428.
11. L.L. Hopkins Jr., H.E. Mohr, Vanadium as an essential nutrient, Fed. Proc. 33 (1974) 1773-1775.
12. C.E. Heyliger, A.G. Tahiliani, J.H. McNeill, Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats, Science 227 (1985) 1474-1477.
13. J. Meyerovitch, Z. Farfel, J. Sack, Y. Shechter, Oral administration of vanadate normalizes blood glucose levels in streptozotocin-treated rats. Characterization and mode of action, J. Biol. Chem. 262 (1987) 6658-6662.
14. S. Ramanadham, J.J. Mongold, R.W. Brownsey, G.H. Cros, J.H. McNeill, Oral vanadyl sulfate in the treatment of diabetes mellitus in rats, Am. J. Physiol. 257 (1989) H904-H911.
15. N. Cohen, M. Halberstam, P. Shlimovich, C.J. Chang, H. Shamoon, L. Rossetti, Oral vanadyl sulfate improves hepatic and peripheral insulin sensitivity in patients with non-insulin-dependent diabetes mellitus, J. Clin. Invest. 95 (1995) 2501-2509.
16. N.D. Chasteen, J.K. Grady, C.E. Holloway, Characterization of the binding, kinetics, and redox stability of vanadium(IV) and vanadium(V) protein complexes in serum, Inorg. Chem. 25 (1986) 2754-2760.
17. W.R. Harris, S.B. Friedman, D. Silberman, Behavior of vanadate and vanadyl ion in canine blood, J. Inorg. Biochem. 20 (1984) 157-169.
18. A. Butler, C.J. Carrano, Coordination chemistry of vanadium in biological systems, Coord. Chem. Rev. 109 (1991) 61-105.
19. R.F. Campbell, N.D. Chasteen, An anion binding study of vanadyl(IV) human serotransferrin. Evidence for direct linkage to the metal, J. Biol. Chem. 252 (1977) 5996-6001.
20. J. Mazurier, J.M. Lhoste, J. Montreuil, G. Spik, Comparative study of the iron-binding properties of human transferrins. II. Electron paramagnetic resonance of mixed metal complexes of human lactotransferrin, Biochim. Biophys. Acta 745 (1983) 44-49.
21. W.R. Harris, C.J. Carrano, Binding of vanadate to human serum transferrin, J. Inorg. Biochem. 22 (1984) 201-218.
22. N.D. Chasteen, Vanadium-protein interactions, Met. Ions Biol. Syst. 31 (1995) 231-247.
23. N. Jakubowski, L. Moens, F. Vanhaecke, Sector field mass spectrometers in ICP-MS, Spectrochim. Acta Part B 53 (1998) 1739-1763.
24. U. Giessmann, U. Greb, High resolution ICP-MS: a new concept for elemental mass spectrometry, Fresenius J. Anal. Chem. 350 (1994) 186-193.
25. N.M. Reed, R.O. Cairns, R.C. Hutton, Y. Takaku, Characterization of polyatomic ion interferences in inductively coupled plasma mass spectrometry using a high resolution mass spectrometer, J. Anal. At. Spectrom. 9 (1994) 881-896.
26. N.D. Chasteen, E.M. Lord, H.J. Thompson, J.K. Grady, Vanadium complexes of transferrin and ferritin in the rat, Biochim. Biophys. Acta 884 (1986) 84-92.
27. N.D. Chasteen, J. Williams, The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrin, Biochem. J. 193 (1981) 717-727.
28. I. Bertini, G. Canti, C. Luchinat, Preparation and characterization of the vanadium(III) derivative of transferrin, Inorg. Chim. Acta 67(1982) L21-L23.
29. M.H. Nagaoka, T. Maitani, Effects of sialic acid residues of transferrin on the binding with aluminum and iron studied by HPLC/high-resolution ICP-MS, Biochim. Biophys. Acta 1526 (2001) 175-182.
30. 51V) coordination to human apotransferrin, J. Am. Chem. Soc. 111 (1989) 2802-2809.
31. J.A. Saponja, H.J. Vogel, Metal-ion binding properties of the transferrins: a vanadium-51 NMR study, J. Inorg. Biochem. 62 (1996) 253-270.
32. B.I. Posner, C.R. Yang, A. Shaver, Mechanism of insulin mimetic action of peroxovanadium compounds, in: A.S. Tracey, D.C. Crans (Eds.), Vanadium Compounds Chemistry, Biochemistry, and Therapeutic Applications, ACS Symposium Series, No. 711, American Chemical Society, Washington, DC, 1998, pp. 316-328.