A "silent" polymorphism in the MDR1 gene changes substrate specificity

Science

Volumn 315, Issue 5811, 2007, Pages 525-528

  Kimchi Sarfaty, Chava ^a,b   Oh, Jung Mi ^a,c   Kim, In Wha ^a   Sauna, Zuben E ^a   Calcagno, Anna Maria ^a   Ambudkar, Suresh V ^a   Gottesman, Michael M ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^c Seoul National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN P; MESSENGER RNA; MULTIDRUG RESISTANCE PROTEIN 1; PROTEIN;

DRUG RESISTANCE; GENE EXPRESSION; POLYMORPHISM; PROTEIN; RNA;

ARTICLE; CODON; ENZYME SPECIFICITY; GENE; GENETIC POLYMORPHISM; HUMAN; MDR1 GENE; MEMBRANE STRUCTURE; MULTIDRUG RESISTANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SILENCER ELEMENT; SINGLE NUCLEOTIDE POLYMORPHISM;

ANIMALS; CELL LINE; CELL MEMBRANE; CERCOPITHECUS AETHIOPS; CODON; CYCLOSPORINE; GENES, MDR; HAPLOTYPES; HELA CELLS; HUMANS; MUTAGENESIS, SITE-DIRECTED; P-GLYCOPROTEIN; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RHODAMINE 123; RNA, MESSENGER; SIROLIMUS; SUBSTRATE SPECIFICITY; TRANSFECTION; VERAPAMIL;

EID: 33846504706     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1135308     Document Type: Article

References (31)

1. M. M. Gottesman, T. Fojo, S. E. Bates, Nat. Rev. Cancer 2, 48 (2002).
2. C. Cordon-Cardo et al., J. Histochem. Cytochem. 38, 1277 (1990).
3. S. Hoffmeyer et al., Proc. Natl. Acad. Sci. U.S.A. 97, 3473 (2000).
4. S. Drescher et al., Br. J. Clin. Pharmacol. 53, 526 (2002).
5. M. Goto et al., Pharmacogenetics 12, 451 (2002).
6. S. V. Ambudkar, C. Kimchi-Sarfaty, E. Z. Sauna, M. M. Gottesman, Oncogene 22, 7468 (2003).
7. H. N. Salama, Z. Yang, T. Bui, R. J. Y. Ho, J. Pharm. Sci. 95, 2293 (2006).
8. K. Tang et al., Pharmacogenetics 12, 437 (2002).
9. M. Horinouchi et al., Pharm. Res. 19, 1581 (2002).
10. L. X. Shen, J. P. Basilion, V. P. Stanton Jr., Proc. Natl. Acad. Sci. U.SA 96, 7871 (1999).
11. L. Frittitta et al., Diabetes 50, 1952 (2001).
12. M. D. Perloff, L. L. von Moltke, E. Stormer, R. I. Shader, D. J. Greenblatt, Br. J. Pharmacol. 134, 1601 (2001).
13. J. J. Gribar, M. Ramachandra, C. A. Hrycyna, S. Dey, S. V. Ambudkar, J. Membr. Biol. 173, 203 (2000).
14. See supporting material on Science Online.
15. C. Kimchi-Sarfaty, J. J. Gribar, M. M. Gottesman, Mol. Pharmacol. 62, 1 (2002).
16. H. T. Thi Tran et al., Mol. Genet. Metab. 85, 213 (2005).
17. D. Wang, A. D. Johnson, A. C. Papp, D. L. Kroetz, W. Sadee, Pharmacogenet. Genomics 15, 693 (2005).
18. A. Ruth, W. D. Stein, E. Rose, I. B. Roninson, Biochemistry 40, 4332 (2001).
19. T. W. Loo, D. M. Clarke, J. Biol. Chem. 273, 14671 (1998).
20. I. Z. Siemion, P. J. Siemion, Biosystems 33, 139 (1994).
21. S. Brunak, J. Engelbrecht, Proteins 25, 237 (1996).
22. A. A. Adzhubei, I. A. Adzhubei, I. A. Krasheninnikov, S. Neidle, FEBS Lett. 399, 78 (1996).
23. S. K. Gupta, S. Majumdar, T. K. Bhattacharya, T. C. Ghosh, Biochem. Biophys. Res. Commun. 269, 692 (2000).
24. P. Cortazzo et al., Biochem. Biophys. Res. Commun. 293, S37 (2002).
25. A. A. Komar, T. Lesnik, C. Reiss, FEBS Lett. 462, 387 (1999).
26. T. Xie, D. Ding, FEBS Lett. 434, 93 (1998).
27. P. M. Sharp, W. H. Li, Nucleic Acids Res. 15, 1281 (1987).
28. F. Supek, K. Vlahovicek, BMC Bioinformatics 6, 182 (2005).
29. V. Anthony, W. R. Skach, Curr. Protein Pept. Sci. 3, 485 (2002).
30. L. Bercovitch, P. Terry, J. Am. Acad. Dermatol. 51, 513 (2004).
31. We thank W. Stein for fruitful discussions; R. Kincaid for a discussion that led to the idea that substitution of rare codons could affect folding of complex transmembrane proteins; G. Leiman for valuable editorial assistance; P. FitzGerald, who assisted us with codon usage rates; and S. Garfield for help with confocal images. Supported by the National Institute of General Medical Sciences Pharmacology Research Associate (PRAT) program (A.M.C.) and by the Intramural Research Program of the Center for Cancer Research, National Cancer Institute.