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Complexation of ytterbium to human transferrin and its uptake by K562 cells
Du, XL; Zhang, TI; Yuan, L; Zhao, YY; Li, RC; Wang, K; Yan, SC; Zhang, L; Sun, HZ; Qian, ZM
关键词K562 cells recognition transferrin ytterbium
刊名EUROPEAN JOURNAL OF BIOCHEMISTRY
2002-12-01
DOI10.1046/j.1432-1033.2002.03326.x
269期:24页:6082-6090
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]HUMAN SERUM TRANSFERRIN ; RECOMBINANT N-LOBE ; TUMOR-CELLS ; STRUCTURAL-CHANGES ; CRYSTAL-STRUCTURE ; BINDING ; RECEPTOR ; IRON ; MICROSCOPY ; TRANSPORT
英文摘要

There is an increasing interest in the use of lanthanides in medicine. However, the mechanism of their accumulation in cells is not well understood. Lanthanide cations are similar to ferric ions with regard to transferrin binding, suggesting transferrin-receptor mediated transport is possible; however, this has not yet been confirmed. In order to clarify this mechanism, we investigated the binding of Yb3+ to apotransferrin by UV-Vis spectroscopy and stopped-flow spectrophotometry, and found that Yb3+ binds to apotransferrin at the specific iron sites in the presence of bicarbonate. The apparent binding constants of these sites showed that the affinity of Yb3+ is lower than that of Fe3+ and binding of Yb3+ in the N-lobe is kinetically favored while the C-lobe is thermodynamically favored. The first Yb3+ bound to the C-lobe quantitatively with a Yb/apotransferrin molar ratio of < 1, whereas the binding to the other site is weaker and approaches completeness by a higher molar ratio only. As demonstrated by (1) H NMR spectra, Yb3+ binding disturbed the conformation of apotransferrin in a manner similar to Fe3+ . Flow cytometric studies on the uptake of fluorescein isothiocyanate labeled Yb3+ -bound transferrin species by K562 cells showed that they bind to the cell receptors. Laser scanning confocal microscopic studies with fluorescein isothiocyanate labeled Yb3+ -bound transferrin and propidium iodide labeled DNA and RNA in cells indicated that the Yb3+ entered the cells. The Yb3+ -transferrin complex inhibited the uptake of the fluorescein labeled ferric-saturated transferrin (Fe-2 -transferrin) complex into K562 cells. The results demonstrate that the complex of Yb3+ -transferrin complex was recognized by the transferrin receptor and that the transferrin-receptor-mediated mechanism is a possible pathway for Yb3+ accumulation in cells.

语种英语
WOS记录号WOS:000179772800010
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被引频次:33[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/65992
专题北京大学药学院_化学生物学系
作者单位1.Peking Univ, Dept Biol Chem, Sch Pharmaceut Sci, Beijing 100083, Peoples R China
2.Univ Hong Kong, Dept Chem, Hong Kong, Hong Kong, Peoples R China
3.Univ Hong Kong, Open Lab Chem Biol, Hong Kong, Hong Kong, Peoples R China
4.Hong Kong Polytech Univ, Dept Appl Biol & Chem Technol, Kowloon, Hong Kong, Peoples R China
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GB/T 7714
Du, XL,Zhang, TI,Yuan, L,et al. Complexation of ytterbium to human transferrin and its uptake by K562 cells[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY,2002,269(24):6082-6090.
APA Du, XL.,Zhang, TI.,Yuan, L.,Zhao, YY.,Li, RC.,...&Qian, ZM.(2002).Complexation of ytterbium to human transferrin and its uptake by K562 cells.EUROPEAN JOURNAL OF BIOCHEMISTRY,269(24),6082-6090.
MLA Du, XL,et al."Complexation of ytterbium to human transferrin and its uptake by K562 cells".EUROPEAN JOURNAL OF BIOCHEMISTRY 269.24(2002):6082-6090.
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