Complexation of ytterbium to human transferrin and its uptake by K562 cells

European Journal of Biochemistry

Volumn 269, Issue 24, 2002, Pages 6082-6090

  Du, Xiu Lian ^a   Zhang, Tian Lan ^a   Yuan, Lan ^a   Zhao, Yong Yuan ^a   Li, Rong Chang ^a   Wang, Kui ^a   Yan, Siu Cheong ^b   Zhang, Li ^b   Sun, Hongzhe ^b   Qian, Zhong Ming ^c  

^a PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

^c HONG KONG POLYTECHNIC UNIVERSITY   (Hong Kong)

Author keywords

K562 cells; Recognition; Transferrin; Ytterbium

Indexed keywords

BICARBONATE; CELL RECEPTOR; DNA; FLUORESCEIN ISOTHIOCYANATE; IRON; PROPIDIUM IODIDE; RNA; TRANSFERRIN; YTTERBIUM;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL LINE; COMPLEX FORMATION; CONFORMATION; CONTROLLED STUDY; FLOW CYTOMETRY; HUMAN; HUMAN CELL; KINETICS; LASER MICROSCOPY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; SPECTROPHOTOMETRY; SPECTROSCOPY; THERMODYNAMICS; ULTRAVIOLET RADIATION;

BINDING, COMPETITIVE; CATIONS; CELL LINE; CELL MEMBRANE; FLOW CYTOMETRY; HUMANS; IRON; K562 CELLS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, CONFOCAL; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROPHOTOMETRY; THERMODYNAMICS; TRANSFERRIN; ULTRAVIOLET RAYS; YTTERBIUM;

EID: 18744411774     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03326.x     Document Type: Article

References (41)

1. 90Y in patients with Baker's cysts and persistent synovitis of the knee. Ann. Rheum. Dis. 47, 553-558.
2. Canada, R.G. (1993) Calcium receptor binding of cisplatin and terbium in human breast tumor cells after hyperthermia. Radiat. Res. 133, 170-175.
3. Wang, K., Li, R.C., Cheng, Y. & Zhu, B. (1999) Lanthanides- the future drugs? Coord. Chem. Rev. 190-192, 297-308.
4. Lazarescu, G.R. & Battista, J.J. (1997) Analysis of the radio-biology of ytterbium-169 and iodine-125 permanent brachytherapy implants. Phys. Med. Biol. 42, 1727-1736.
5. 169Yb complexes in normal and tumour cells: Influence of ligand and metabolic cell activity and stability of cellular association. Nucl. Med. Biol. 24, 349-355.
6. Evans, C.H. (1990) Biochemistry of the Lanthanides. Plenum Press, New York.
7. Cheng, Y., Huo, Q.H., Lu, J.F., Li, R.C. & Wang, K. (1999) The transport kinetics of lanthanide species in a single erythrocyte probed by confocal laser scanning microscopy. J. Biol. Inorg. Chem. 4, 447-456.
8. Shastri, B.P., Sankaram, M.B. & Easwaran, K.R. (1987) Carboxylic ionophore (lasalocid A and A23187) mediated lanthanide ion transport across phospholipid vesicles. Biochemistry 26, 4925-4930.
9. Powis, D.A., Clark, C.L. & O'Brien, K.J. (1994) Lanthanum can be transported by the sodium-calcium exchange pathway and directly triggers catecholamine release from bovine chromaffin cells. Cell Calcium 16, 377-390.
10. Cheng, Y., Liu, M.Z., Li, R.C., Wang, C., Bai, C.L. & Wang, K. (1999) Gadolinium induces domain and pore formation of human erythrocyte membrane: An atomic force microscopic study. Biochim. Biophys. Acta 1421, 249-260.
11. Jackson, G.E. & Byrne, M.J. (1996) Metal ion speciation in blood plasma: Gallium-67-citrate and MRI contrast agents. J. Nucl. Med. 37 , 379-386.
12. Taylor, D.M., Duffield, J.R., Williams, D.R., Yuele, L., Gaskin, P.W. & Unalkat, P. (1991) Binding of f-elements to the iron-transport protein transferrin. Eur. J. Solid. State. Inorg. Chem. 28, 271-274.
13. Meng, L., Ding, L., Chen, H.T., Zhao, D.Q. & Ni, J.Z. (1999) Biological effect of rare earth (I) - Content and distribution of rare earth in normal human plasma. Chem. J. Chin. University 20, 5-8.
14. Luk, K.C. (1971) Study of the nature of the metal-binding sites and estimate of the distance between the metal-binding sites in transferrin using trivalent lanthanide ions as fluorescent probes. Biochemistry 10, 2838-2843.
15. Aisen, P. (1998) Transferrin, the transferrin receptor, and the uptake of iron by cells. Metal Ions Biol. Syst. 35, 585-631.
16. Sun, H., Li, H. & Sadler, P.J. (1999) Transferrin as a metal ion mediator. Chem. Rev. 99, 2817-2842.
17. 59Fe uptake by cultured mouse myeloma cells. Cancer Res. 37, 3634-3638.
18. van Leeuwen-Stok, A.E., Schuurhuis, G.J., Drager, A.M., Visser-Platier, A.W., Teule, G.J. & Huijgens, P.C. (1996) EWect of modulation of the transferrin receptor on gallium-67 uptake and cytotoxicity in lymphoma cell lines. Br. J. Cancer 74, 619-624.
19. Roskams, A.J. & Connor, J.R. (1990) Aluminum access to the brain: A role for transferrin and its receptor. Proc. Natl Acad. Sci. USA 87, 9024-9027.
20. Zuccola, H.J. (1993) The crystal structure of monoferric human serum transferrin. PhD Thesis, Georgia Institute of Technology, Atlanta, GA.
21. Jeffrey, P.D., Bewley, M.C., MacGillivray, R.T.A., Mason, A.B., Woodworth, R.C. & Baker, E.N. (1998) Ligand-induced conformational change in transferrins: Crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry 37, 13978-13986.
22. MacGillivray, R.T.A., Moore, S.A., Chen, J., Anderson, B.F., Baker, H., Luo, Y., Bewley, M., Smith, C.A., Murphy, M.E.P., Wang, Y., Mason, A.B., Woodworth, R.C., Brayer, G.D. & Baker, E.N. (1998) Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry 37, 7919-7928.
23. 5 modified transferrin. Biochim. Biophys. Acta 1076, 252-258.
24. Bali, P.K. & Harris, W.R. (1990) Site-specific rate constants for iron removal from diferric transferrin by nitrilotris (methylene-phosphonic acid) and pyrophosphate. Arch. Biochim. Biophys. 281, 251-256.
25. Musgrove, E., Rugg, C., Tayor, I. & Hedley, D. (1984) Transferrin receptor expression during exponential and plateau phase growth of human tumour cells in culture. J. Cell Physiol. 118, 6-12.
26. Aladar, J. & Kalman, K. (1966) Chemical characterization of fluorescein isothiocyanate-protein conjugates. Biochim. Biophys. Acta 124, 166-175.
27. Zhang, L., Szeto, K.Y., Wong, W.B., Loh, T.T., Sadler, P.J. & Sun, H. (2001) Interactions of bismuth with human lactoferrin and recognition of the Bi(III)-lactoferrin complex by intestinal cells. Biochemistry 40, 13281-13287.
28. Naik, D.V., Paul, W.L., Threatte, R.M. & Schulman, S.G. (1975) Fluorometric determination of drug-protein association constants: The binding of 8-anilino-1-naphthalenesulfonate by bovine serum albumin. Anal. Chem. 47, 267-270.
29. 3+ into the N-lobe of human serum transferrin. Biochem. J. 285, 711-714.
30. 3+binding. Biochemistry 32, 3387-3395.
31. 1H-NMR spectroscopy. Eur. J. Biochem. 220, 781-787.
32. Li, H., Sadler, P.J. & Sun, H. (1996) Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin. J. Biol. Chem. 271, 9483-9489.
33. Li, H., Sun, H. & Qian, Z.M. (2002) The role of the transferrin-transferrin-receptor system in drug delivery and targeting. Trends Pharmacol. Sci. 23, 206-209.
34. Harris, W.R., Yang, B., Abdollahi, S. & Hamada, Y. (1999) Steric restrictions on the binding of large metal ions to serum transferrin. J. Inorg. Biochem. 76, 231-242.
35. 3+) at 3.4 Å resolution. Acta Crystallogr. D55, 1799-1804.
36. Kitamura, T., Gatmaitan, Z. & Arias, I.M. (1990) Serial quantitative image analysis and confocal microscopy of hepatic uptake, intracellular distribution and biliary secretion of a fluorescent bile acid analog in rat hepatocyte doublets. Hepatology 12, 1358-1364.
37. Kotze, A.F., Lueben, H.L., de Leeuw, B.J., de Boer, B.G., Verhoef, J.C. & Jungier, H.E. (1997) N-trimethyl chitosan chloride as a potential absorption enhancer across mucosal surfaces: In vitro evaluation in intestinal epithelial cells (Caco-2). Pharmaceut. Res. 14 , 1197-1202.
38. Drevets, D. & Campbell, P.A. (1991) Macrophage phagocytosis: Use of fluorescence microscopy to distinguish between extracellular and intracellular bacteria. J. Immunol. Meth. 142, 31-38.
39. Flulk, W.P., His, B.L. & Stevens, P.J. (1980) Transferrin and transferrin receptors in carcinoma of the breast. Lancet 2, 390-392.
40. Bernstein, L.R. (1998) Mechanisms of therapeutic activity for gallium. Pharmacol. Rev. 50, 665-682.
41. Harris, W.R. (1998) Binding and transport of nonferrous metals by serum transferrin. Struct. Bonding 92, 122-162.