Transferrins: A mechanism for iron uptake by lactoferrin

European Journal of Biochemistry

Volumn 254, Issue 1, 1998, Pages 144-153

  Pakdaman, Rowchanak ^a   Petitjean, Michel ^a   El Hage Chahine, Jean Michel ^a  

^a UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Iron metabolism; Iron uptake; Lactoferrin; Relaxation kinetics; Transferrin

Indexed keywords

IRON; LACTOFERRIN; TRANSFERRIN;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; EQUILIBRIUM CONSTANT; FLUORESCENCE; IONIC STRENGTH; IRON TRANSPORT; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE;

BOVINAE;

EID: 0032523937     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540144.x     Document Type: Article

References (44)

1. Ainscough, E. W., Brodie, A. M., Plowman, J. E., Bloor, S. J., Loehr, J. S. & Loehr, T. M. (1980) Studies of human lactoferrin by electron paramagnetic resonance, fluorescence and resonance Raman spectroscopy, Biochemistry 19, 4072-4079.
2. Aisen, P. & Leibman, A. (1972) Lactolerrin and transferrin: a comparative study, Biochim. Biophys. Acta 257, 314-323.
3. Aisen, P. (1989) Physical biochemistry of the transferrins - Update, 1984-1988, Physical Bioinorganic Chemistry (Loehr, T., ed.) vol. 5, pp. 353-371, VCH, New York.
4. Aisen, P., Leibman, A. & Zweier, J. (1978) Stoichiometric and site characteristics of the binding of iron to human transferrin, J. Biol. Chem. 253, 1930-1937.
5. Anderson, B. F., Baker, H. M., Norris, G. E., Rumball, S. V. & Baker, E. N. (1990) Apolactoferrin structure demonstrates ligand-induced changes in transferrins, Nature 344, 784-786.
6. Anderson, B. F., Baker, H. M., Norris, G. E., Rice, W. R. & Baker, E. N. (1989) Structure of human lactoferrin - Crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Boil. 209, 711-734.
7. Baily, S., Evans, W. E., Garrat, R. C., Gorinsky, B., Hasnain, S., Horsburgh, C., Jhoti, H., Lindley, P. F., Mydin, A., Sarra, R. & Watson, J. L. (1988) Molecular structure of serum transferrin at 3.3 Å resolution, Biochemistry 27, 5804-5812.
8. Baker, E. N. & Lindley, P. K (1992) New perspectives on the structure and function of transferrins, Inorg. Biochem. 47, 147-160.
9. Baldwin, G. S. (1993) Comparison of transferrin sequences from different species, Comp. Biochem. Physiol. 106B, 203-218.
10. Bates, G. W. & Wernicke, J. (1971) The kinetic and mechanisms of iron(III) exchange between chelates and transferrin. J. Biol. Chem. 246, 3679-3685.
11. Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. & Tomita, M (1992) Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta 1121, 130-136.
12. Bellounis, L., Pakdaman, R. & El Hage Chahine, J. M. (1996) Apotransferrin proton dissociation and interactions with bicarbonate in neutral media, J. Phys. Org. Chem. 9, 111-118.
13. Bernasconi, C. F. (1976) Relaxation kinetics, Academic Press, New York.
14. Brouillard, R. (1980) How much an equilibrium can be shifted in a chemical relaxation experiment, J. Chem. Soc. Faraday Trans. 176, 583-587.
15. Chung, T. D. Y. & Raymond, K. N. (1993) The role of conformational changes in iron binding and release. J. Am. Chem. Soc. 115, 6765-6768.
16. 3+ between acetohydroxamic acid and transferrin. J. Biol. Chem. 257, 7560-7565.
17. 3+ between pyrophosphate and transferrin. Probing the nature of the intermediate complex with stopped-flow rapid multimixing. and electron paramagnetic resonance spectroscopy, J. Biol. Chem. 261, 4607-4614.
18. Dautry-Varsat, A., Cienchanover, A. & Lodish, H. F. (1983) pH and recycling of transferrin during receptor-mediated endocytosis, Proc. Natl Acad Sci. USA 80, 2258-2262.
19. Dewan, J. C., Mikami, B., Hirose, M. & Sacchettini, J. C. (1993) Structural evidence for pH-sensitive trigger in the hen ovotransferrin N-lobe. Implication for transferrin iron-release. Biochemistry 32, 11963-11968.
20. Egan, T. J., Ross, D. C., Purves, L. R. & Adams, L. P. (1992) Mechanism of iron-release from serum transferrin to pyrophosphate. Kinetic discrimination for two alternative mechanisms, Inorg. Chem. 31, 1994-1998.
21. Eigen, M. & DeMayer, L. (1973) in Techniques of chemistry (Weissenberger, A. & Hammes, G., eds) vol. 6, part 2, Wiley, New York.
22. El Hage Chahine, J. M. & Fain, D. (1993) The mechanism of iron-transferrin interactions - Uptake of the iron nitrilotriacetic acid complex, J. Chem. Soc. Dalton Trans., 3137-3143.
23. El Hage Chahine, J. M. & Fain, D. (1994) The mechanism of iron release from transferrin - Slow proton induced loss of nitrilotriacetatoiron(III) complex in acidic media, Eur. J. Biochem. 223, 581-587.
24. El Hage Chahine, J. M. & Pakdaman, R. (1995) Transferrin, a mechanism tor iron release, Eur. J. Biochem. 230, 1101-1110.
25. El Hage Chahine, J. M. (1990) Kinetics and thermodynamics of the structural transformations of thiamine in aqueous media. Part 5 - Interaction of thiamine with SDS micelles, J. Chem. Soc. Perkin Trans. 2 1045-1050.
26. Faber, H. R., Bland, T., Day, C. L., Norris, G. E., Tweedie, J. W. & Baker, E. N. (1996) Altered domain closure and iron binding in transferrins - The crystal structure of the asp60ser mutant of the amino-terminal half-molecule of human lactoferrin, J. Mol. Biol, 256, 352-363.
27. Gilmour, A. D., Cassidy, J. K. & McAuley, A. (1970) Comparison of the dimerisation of the iron(III)-nitrilotriacetate and -bis-picolinate complexes, J. Chem. Soc. A, 2847-2850.
28. Grossmann, J. G., Mason, A. B., Wood worth, R. C., Neu, M., Lindley, P. F. & Hasnain, F. (1993) Asp ligand provides the trigger for closure of transferrin molecules - Direct evidence from X-ray scattering studies of site-specific mutants of the N-terminal half-molecule of human transferrin, J. Mol. Biol. 231, 554-558.
29. Harris, W. R., Carrano, C. J., Cooper, S. R., Sofen, S. R., Avdeef, A. E., McArdle, J. V. & Raymond, K. N. (1979) Coordination chemistry of microbial iron transport compounds -19- stability constants and electrochemical behavior of ferric enterobactin and model complexes. J. Am. Chem. Soc. 101, 6097-6104.
30. Kretchmar, S. A. & Raymond, K. N. (1986) Biphasic kinetics and temperature dependence of iron removal from transferrin by 3.4-LICAMS, J. Am. Chem. Soc. 108, 6212-6218.
31. Kretchmar-Nguyen, S. A., Craig, A. & Raymond, K. N. (1993) Transferrin - The role of conformational changes in iron removal by chelators. J. Am. Chem. Soc. 115, 6758-6764.
32. Legrand, D., Mazurier, J., Aubert, J. P., Loucheux-Lefebvre, M. H., Montreuil, J. & Spik, G. (1986) Evidence for interactions between the 30 kDa N- and 50 kDa C-terminal triptic fragments of human lactotransferrin, Biochem, J. 236, 839-844.
33. MacGillivray, R. T. A., Mendez, E., Sinha, S. K., Linebeck-Zins, J. & Brew, K. (1983) The primary structure of human serum transferrin, J. Biol. Chem. 258, 3543-3553.
34. Makey, D. G. & Seal, U. S. (1976) The detection of four molecular forms of Human transferrin during the iron-binding process, Biochim. Biophys. Acta 453, 250-256.
35. Martell, A. E. & Smith, R. M. S. (1989) Critical stability constants, vol. 1, Plenum Press, New York.
36. Mead, P. E. & Tweedie, J. W. (1990) cDNA and protein sequence of bovine lactoferrin, Nucleic Acids Res. 18, 7167.
37. Metz-Boutigue, M. H., Jolles, M., Mazurier, J., Schoentgen, F., Legrand, D. & Spik, G. (1984) Human lactoferrin: amino acid sequence and structural comparison with other transferrins, Eur. J. Biochem. 145, 659-676.
38. Montreuil, J., Tonnelat, J. & Mullet, S. (1960) Préparation et propriétés de la lactosidérophiline du lait de femme. Biochim. Biophys. 45, 413-421.
39. Morin, M. & Scharff, J. P. (1973) Etude des chélates mixtes des ions ferriques avec les acides nitrilotriacétique, sulfo-5-salicylique et pyrocathecholdisulfonique-3,5, Anal. Chim. Acta 66, 113-121.
40. Pakdaman, R. & El Hage Chahine, J. M. (1996) A mechanism for iron uptake by transferrin, Eur. J. Biochem. 236, 922-931.
41. Pakdaman, R. & El Hage Chahine, J. M. (1997) Transferrin - the interaction of lactoferrin with hydrogen carbonate, Eur. J. Biochem. 249, 149-155.
42. Petitjean, M. (1996) Three-dimensional pattern recognition from molecular distance minimization, J. Chem. Inf. Comput. Sci. 36, 1038-1049.
43. Smith, C. A., Anderson, B. F., Baker, M. H. & Baker, E. N. (1992) Metal substitution in transferrins: the crystal structure of human copperlactoferrin at 2.1 Å resolution, Biochemistry 31, 4527-4533.
44. Zuccola, H. J. (1992) The crystal structure of monoferric human serum transferrin, Ph.D. Thesis, Georgia Institute of Technology, Ann Arbor, USA.