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Tunicamycin Depresses P-Glycoprotein Glycosylation Without an Effect on Its Membrane Localization and Drug Efflux Activity in L1210 Cells

Institute of Molecular Physiology and Genetics, Centre of Excellence of the Slovak Research and Development Agency “BIOMEMBRANES2008”, Slovak Academy of Sciences, Vlárska 5, Bratislava 83334, Slovakia
Cancer Research Institute, Slovak Academy of Sciences, Vlárska 7, Bratislava 83391, Slovakia
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2011, 12(11), 7772-7784;
Received: 25 September 2011 / Revised: 20 October 2011 / Accepted: 3 November 2011 / Published: 10 November 2011
(This article belongs to the Special Issue Membrane Transport)
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P-glycoprotein (P-gp), also known as ABCB1, is a member of the ABC transporter family of proteins. P-gp is an ATP-dependent drug efflux pump that is localized to the plasma membrane of mammalian cells and confers multidrug resistance in neoplastic cells. P-gp is a 140-kDa polypeptide that is glycosylated to a final molecular weight of 170 kDa. Our experimental model used two variants of L1210 cells in which overexpression of P-gp was achieved: either by adaptation of parental cells (S) to vincristine (R) or by transfection with the human gene encoding P-gp (T). R and T cells were found to differ from S cells in transglycosylation reactions in our recent studies. The effects of tunicamycin on glycosylation, drug efflux activity and cellular localization of P-gp in R and T cells were examined in the present study. Treatment with tunicamycin caused less concentration-dependent cellular damage to R and T cells compared with S cells. Tunicamycin inhibited P-gp N-glycosylation in both of the P-gp-positive cells. However, tunicamycin treatment did not alter either the P-gp cellular localization to the plasma membrane or the P-gp transport activity. The present paper brings evidence that independently on the mode of P-gp expression (selection with drugs or transfection with a gene encoding P-gp) in L1210 cells, tunicamycin induces inhibition of N-glycosylation of this protein, without altering its function as plasma membrane drug efflux pump. View Full-Text
Keywords: P-gp (MDR1); tunicamycin; N-glycosylation; L1210 P-gp (MDR1); tunicamycin; N-glycosylation; L1210
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Šereš, M.; Cholujová, D.; Bubenčíkova, T.; Breier, A.; Sulová, Z. Tunicamycin Depresses P-Glycoprotein Glycosylation Without an Effect on Its Membrane Localization and Drug Efflux Activity in L1210 Cells. Int. J. Mol. Sci. 2011, 12, 7772-7784.

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