Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/24116
Title: Apotransferrin is internalized and distributed in the same way as holotransferrin in K562 cells
Authors: Du, XL
Wang, K
Ke, Y
Yuan, L
Li, RC
Chang, CZ
Ho, KP
Qian, ZM
Issue Date: 2004
Source: Journal of cellular physiology, 2004, v. 201, no. 1, p. 45-54 How to cite?
Journal: Journal of Cellular Physiology 
Abstract: Transferrin (Tf), a naturally existing protein, has received considerable attention in the area of drug targeting since it is biodegradable, non-toxic, and non-immunogenic. The efficient cellular uptake of Tf shows it has potential in the delivery of anti-cancer drugs, proteins, and therapeutic genes into proliferating malignant cells that overexpress transferrin receptor (TfR). In human serum, about 30% of Tf exists in the iron-saturated form (Fe 2-Tf) and the remainder exists as apotransferrin (apo-Tf). Understanding the uptake of apo-Tf by cells will provide key insights into studies on Tf-mediated drug delivery. In the present study, we investigated visually the transport of apo-Tf into K562 cells and its intracellular localization by laser-scanning confocal microscopy (LSCM) and flow cytometry analysis (FCA). It was found that, like Fe2-Tf, apo-Tf can be taken up into the cells. The process is time- and temperature-dependent, competitively inhibited by Fe2-Tf, and significantly abolished by pronase pretreatment. Visual evidence showed that the transport of apo-Tf into K562 cells is a TfR-mediated process. Furthermore, the investigations using optical-slicing technique demonstrated that the distribution of apo-Tf is similar to that of Fe2-Tf, both appearing in the perinuclear region in ball-in-bowl shape.
URI: http://hdl.handle.net/10397/24116
ISSN: 0021-9541
DOI: 10.1002/jcp.20051
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