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Int. J. Mol. Sci. 2011, 12(11), 7772-7784; doi:10.3390/ijms12117772

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

1,*  and 1,*
1 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 2 Cancer Research Institute, Slovak Academy of Sciences, Vlárska 7, Bratislava 83391, Slovakia
* Authors to whom correspondence should be addressed.
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.
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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