Title: P-Glycoprotein
Additional Names: Glycoprotein-P; P-gp; P-170; permeability glycoprotein
Literature References: Highly conserved cell-surface glycoprotein of Mr 170,000 daltons; protein product of the mammalian multidrug resistance (mdr) gene. Present in selective human tissues where it functions as an energy-dependent efflux pump. Increased expression in mammalian tumor cells is associated with multidrug resistance (MDR) to cancer chemotherapy agents. Identification and isolation from colchicine-resistant Chinese hamster ovary (CHO) cells: R. J. Juliano, V. Ling, Biochim. Biophys. Acta 455, 152 (1976). Purification from plasma membrane of CHO cells: J. R. Riordan, V. Ling, J. Biol. Chem. 254, 12701 (1979). MDR associated with P-glycoprotein in mammalian cell lines: N. Kartner et al., Science 221, 1285 (1983); N. Kartner et al., Cancer Res. 43, 4413 (1983). Deduced amino acid sequence from mouse mdr cDNA: P. Gros et al., Cell 47, 371 (1986); from human mdr1 cDNA: C.-j. Chen et al., ibid. 381. Transfection and expression of human mdr1 gene in cell culture: K. Ueda et al., Proc. Natl. Acad. Sci. USA 84, 3004 (1987). Characterization of ATPase activity: H. Hamada, T. Tsuruo, Cancer Res. 48, 4926 (1988). Detection in normal human tissues: F. Thiebaut et al., Proc. Natl. Acad. Sci. USA 84, 7735 (1987); R. N. Hitchins et al., Eur. J. Cancer Clin. Oncol. 24, 449 (1988); and in human tumor cells: D. R. Bell et al., J. Clin. Oncol. 3, 311 (1985); W. S. Dalton et al., Blood 73, 747 (1989). Review of role in MDR in human cancer: I. Pastan, M. Gottesman, N. Engl. J. Med. 316, 1388 (1987); of biochemistry of MDR: J. A. Endicott, V. Ling, Annu. Rev. Biochem. 58, 137-171 (1989); of mechanism of action: S. Ruetz, P. Gros, Trends Pharmacol. Sci. 15, 260-263 (1994).

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