Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/17880
Title: Complexation of ytterbium to human transferrin and its uptake by K562 cells
Authors: Du, XL
Zhang, TL
Yuan, L
Zhao, YY
Li, RC
Wang, K
Yan, SC
Zhang, L
Sun, H
Qian, ZM
Keywords: K562 cells
Recognition
Transferrin
Ytterbium
Issue Date: 2002
Publisher: Wiley-Blackwell
Source: European journal of biochemistry, 2002, v. 269, no. 24, p. 6082-6090 How to cite?
Journal: European journal of biochemistry 
Abstract: 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 1H 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 (Fe2-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.
URI: http://hdl.handle.net/10397/17880
ISSN: 0014-2956
EISSN: 1432-1033
DOI: 10.1046/j.1432-1033.2002.03326.x
Appears in Collections:Journal/Magazine Article

Access
View full-text via PolyU eLinks SFX Query
Show full item record

SCOPUSTM   
Citations

31
Last Week
0
Last month
0
Citations as of Dec 3, 2017

WEB OF SCIENCETM
Citations

32
Last Week
0
Last month
1
Citations as of Dec 9, 2017

Page view(s)

52
Last Week
1
Last month
Checked on Dec 10, 2017

Google ScholarTM

Check

Altmetric



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.