P-glycoproteins: mediators of multidrug resistance |
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| Institution: | 1. McGill University, Montreal, QC, Canada;2. University of Michigan, Ann Arbor, MI, United States;3. Zhejiang University, Hangzhou, China;1. Department of Physics, Arab-American University, Jenin, Palestine;2. Group of Physics, Faculty of Engineering, Atilim University, 06836 Ankara, Turkey;1. Unidad Académica de Física, Universidad Autónoma de Zacatecas, Calzada Solidaridad esquina con Paseo La Bufa S/N, C.P. 98060, Zacatecas, Zac., Mexico;2. Unidad Académica de Ingeniería, Universidad Autónoma de Zacatecas, Ramón López Velarde 801, C.P. 98000, Zacatecas, Zac., Mexico;3. Centro de Investigación en Ciencias, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, CP 62209, Cuernavaca, Morelos, Mexico;1. Electron Optica, Palo Alto, CA, United States of America;2. Physics Department, Stanford University, Stanford, CA, United States of America;3. Universitaet Wien, Vienna, Austria;4. Delong Instruments, Brno, Czech Republic;1. Department of Electrical Engineering and Computer Science, University of Michigan, Ann Arbor, MI 48109, USA;2. Department of Electrical and Computer Engineering, McGill University, Montreal, QC H3A 0E9, Canada;3. Raytheon BBN Technologies, Cambridge, MA 02138, USA |
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| Abstract: | Multidrug resistance represents a major obstacle to successful chemotherapy of metastatic disease. Elevated levels in cancer cells if the product of the multidrug resistance gene, P-glycoprotein or the multidrug transporter, have been associated with the development of simultaneous resistance to a great variety of amphiphilic cytotoxic drugs. P-glycoproteins is an integral plasma membrane protein which contains 12 putative transmembrane regions and two ATP binding sites. It confers multidrug resistance by functioning as an energy-dependent drug efflux pump. Here we describe recent studies on the biosynthesis, structure, function, and mechanism of action of P-glycoprotein which have provided insights into the complexity of this multifunctional transport system and revealed an additional chloride channel activity. The physiological role of P-glycoprotein, however, still remains to be elucidated. |
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