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Volumn 76, Issue 3, 2008, Pages 404-415

Characterisation of novel defective thiopurine S-methyltransferase allelic variants

Author keywords

Heterologous expression; HPLC; Molecular modeling; Thiopurine drugs; TPMT genetic polymorphism

Indexed keywords

AZATHIOPRINE; MERCAPTOPURINE; THIOPURINE METHYLTRANSFERASE; TIOGUANINE;

EID: 46649107499     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.05.009     Document Type: Article
Times cited : (54)

References (43)
  • 1
  • 2
    • 0026758498 scopus 로고
    • The clinical pharmacology of 6-mercaptopurine
    • Lennard L. The clinical pharmacology of 6-mercaptopurine. Eur J Clin Pharmacol 43 (1992) 329-339
    • (1992) Eur J Clin Pharmacol , vol.43 , pp. 329-339
    • Lennard, L.1
  • 4
    • 2942532516 scopus 로고    scopus 로고
    • Translating pharmacogenetics and pharmacogenomics into drug development for clinical pediatrics and beyond
    • Leeder J.S. Translating pharmacogenetics and pharmacogenomics into drug development for clinical pediatrics and beyond. Drug Discov Today 9 (2004) 567-573
    • (2004) Drug Discov Today , vol.9 , pp. 567-573
    • Leeder, J.S.1
  • 5
    • 0035871560 scopus 로고    scopus 로고
    • Preponderance of thiopurine S-methyltransferase deficiency and heterozygosity among patients intolerant to mercaptopurine or azathioprine
    • Evans W.E., Hon Y.Y., Bomgaars L., Coutre S., Holdsworth M., Janco R., et al. Preponderance of thiopurine S-methyltransferase deficiency and heterozygosity among patients intolerant to mercaptopurine or azathioprine. J Clin Oncol 19 (2001) 2293-2301
    • (2001) J Clin Oncol , vol.19 , pp. 2293-2301
    • Evans, W.E.1    Hon, Y.Y.2    Bomgaars, L.3    Coutre, S.4    Holdsworth, M.5    Janco, R.6
  • 6
    • 0018822866 scopus 로고
    • Mercaptopurine pharmacogenetics: monogenic inheritance of erythrocyte thiopurine methyltransferase activity
    • Weinshilboum R.M., and Sladek S.L. Mercaptopurine pharmacogenetics: monogenic inheritance of erythrocyte thiopurine methyltransferase activity. Am J Hum Genet 32 (1980) 651-662
    • (1980) Am J Hum Genet , vol.32 , pp. 651-662
    • Weinshilboum, R.M.1    Sladek, S.L.2
  • 7
    • 0030934850 scopus 로고    scopus 로고
    • Molecular diagnosis of thiopurine S-methyltransferase deficiency: genetic basis for azathioprine and mercaptopurine intolerance
    • Yates C.R., Krynetski E.Y., Loennechen T., Fessing M.Y., Tai H.L., Pui C.H., et al. Molecular diagnosis of thiopurine S-methyltransferase deficiency: genetic basis for azathioprine and mercaptopurine intolerance. Ann Intern Med 126 (1997) 608-614
    • (1997) Ann Intern Med , vol.126 , pp. 608-614
    • Yates, C.R.1    Krynetski, E.Y.2    Loennechen, T.3    Fessing, M.Y.4    Tai, H.L.5    Pui, C.H.6
  • 8
    • 3242762099 scopus 로고    scopus 로고
    • Comprehensive analysis of thiopurine S-methyltransferase phenotype-genotype correlation in a large population of German-Caucasians and identification of novel TPMT variants
    • Schaeffeler E., Fischer C., Brockmeier D., Wernet D., Moerike K., Eichelbaum M., et al. Comprehensive analysis of thiopurine S-methyltransferase phenotype-genotype correlation in a large population of German-Caucasians and identification of novel TPMT variants. Pharmacogenetics 14 (2004) 407-417
    • (2004) Pharmacogenetics , vol.14 , pp. 407-417
    • Schaeffeler, E.1    Fischer, C.2    Brockmeier, D.3    Wernet, D.4    Moerike, K.5    Eichelbaum, M.6
  • 9
    • 33750581390 scopus 로고    scopus 로고
    • Three novel thiopurine S-methyltransferase allelic variants (TPMT*20, *21, *22)-association with decreased enzyme function
    • Schaeffeler E., Eichelbaum M., Reinisch W., Zanger U.M., and Schwab M. Three novel thiopurine S-methyltransferase allelic variants (TPMT*20, *21, *22)-association with decreased enzyme function. Hum Mutat 27 (2006) 976
    • (2006) Hum Mutat , vol.27 , pp. 976
    • Schaeffeler, E.1    Eichelbaum, M.2    Reinisch, W.3    Zanger, U.M.4    Schwab, M.5
  • 10
    • 0005454374 scopus 로고    scopus 로고
    • Genotypic and phenotypic analysis of the polymorphic thiopurine S-methyltransferase gene (TPMT) in a European population
    • Spire-Vayron de la Moureyre C., Debuysere H., Mastain B., Vinner E., Marez D., Lo Guidice J.M., et al. Genotypic and phenotypic analysis of the polymorphic thiopurine S-methyltransferase gene (TPMT) in a European population. Br J Pharmacol 125 (1998) 879-887
    • (1998) Br J Pharmacol , vol.125 , pp. 879-887
    • Spire-Vayron de la Moureyre, C.1    Debuysere, H.2    Mastain, B.3    Vinner, E.4    Marez, D.5    Lo Guidice, J.M.6
  • 12
    • 15944394455 scopus 로고    scopus 로고
    • Thiopurine methyltransferase (TPMT) heterozygosity and enzyme activity as predictive tests for the development of azathioprine-related adverse events
    • Heckmann J.M., Lambson E.M., Little F., and Owen E.P. Thiopurine methyltransferase (TPMT) heterozygosity and enzyme activity as predictive tests for the development of azathioprine-related adverse events. J Neurol Sci 231 (2005) 71-80
    • (2005) J Neurol Sci , vol.231 , pp. 71-80
    • Heckmann, J.M.1    Lambson, E.M.2    Little, F.3    Owen, E.P.4
  • 15
    • 0028913757 scopus 로고
    • Thiopurine methyltransferase pharmacogenetics. Cloning of human liver cDNA and a processed pseudogene on human chromosome 18q21.1
    • Lee D., Szumlanski C., Houtman J., Honchel R., Rojas K., Overhauser J., et al. Thiopurine methyltransferase pharmacogenetics. Cloning of human liver cDNA and a processed pseudogene on human chromosome 18q21.1. Drug Metab Dispos 23 (1995) 398-405
    • (1995) Drug Metab Dispos , vol.23 , pp. 398-405
    • Lee, D.1    Szumlanski, C.2    Houtman, J.3    Honchel, R.4    Rojas, K.5    Overhauser, J.6
  • 16
    • 33847360477 scopus 로고    scopus 로고
    • Structural basis of allele variation of human thiopurine-S-methyltransferase
    • Wu H., Horton J.R., Battaile K., Allali-Hassani A., Martin F., Zeng H., et al. Structural basis of allele variation of human thiopurine-S-methyltransferase. Proteins 67 (2007) 198-208
    • (2007) Proteins , vol.67 , pp. 198-208
    • Wu, H.1    Horton, J.R.2    Battaile, K.3    Allali-Hassani, A.4    Martin, F.5    Zeng, H.6
  • 17
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G., Willett P., Glen R.C., Leach A.R., and Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267 (1997) 727-748
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 18
    • 84988115618 scopus 로고
    • Validation of the general purpose Tripos 5.2 force field
    • Clark M., Cramer III R.D., and Van Opdenbosch N. Validation of the general purpose Tripos 5.2 force field. J Comp Chem 10 (1989) 982-1012
    • (1989) J Comp Chem , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer III, R.D.2    Van Opdenbosch, N.3
  • 20
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D., St Jean A., Woods R.A., and Schiestl R.H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20 (1992) 1425
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 22
    • 0033837392 scopus 로고    scopus 로고
    • Thiopurine methyltransferase polymorphic tandem repeat: genotype-phenotype correlation analysis
    • Yan L., Zhang S., Eiff B., Szumlanski C.L., Powers M., O'Brien J.F., et al. Thiopurine methyltransferase polymorphic tandem repeat: genotype-phenotype correlation analysis. Clin Pharmacol Ther 68 (2000) 210-219
    • (2000) Clin Pharmacol Ther , vol.68 , pp. 210-219
    • Yan, L.1    Zhang, S.2    Eiff, B.3    Szumlanski, C.L.4    Powers, M.5    O'Brien, J.F.6
  • 23
    • 0025234587 scopus 로고
    • pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson D.E., Becktel W.J., and Dahlquist F.W. pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29 (1990) 2403-2408
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 24
    • 0035937261 scopus 로고    scopus 로고
    • Core and surface mutations affect folding kinetics, stability and cooperativity in IL-1 beta: does alteration in buried water play a role?
    • Covalt Jr. J.C., Roy M., and Jennings P.A. Core and surface mutations affect folding kinetics, stability and cooperativity in IL-1 beta: does alteration in buried water play a role?. J Mol Biol 307 (2001) 657-669
    • (2001) J Mol Biol , vol.307 , pp. 657-669
    • Covalt Jr., J.C.1    Roy, M.2    Jennings, P.A.3
  • 25
    • 0033828949 scopus 로고    scopus 로고
    • Genetic polymorphism of thiopurine S-methyltransferase: molecular mechanisms and clinical importance
    • Krynetski E.Y., and Evans W.E. Genetic polymorphism of thiopurine S-methyltransferase: molecular mechanisms and clinical importance. Pharmacology 61 (2000) 136-146
    • (2000) Pharmacology , vol.61 , pp. 136-146
    • Krynetski, E.Y.1    Evans, W.E.2
  • 26
    • 0029919807 scopus 로고    scopus 로고
    • Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians
    • Tai H.L., Krynetski E.Y., Yates C.R., Loennechen T., Fessing M.Y., Krynetskaia N.F., et al. Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians. Am J Hum Genet 58 (1996) 694-702
    • (1996) Am J Hum Genet , vol.58 , pp. 694-702
    • Tai, H.L.1    Krynetski, E.Y.2    Yates, C.R.3    Loennechen, T.4    Fessing, M.Y.5    Krynetskaia, N.F.6
  • 27
    • 0030986251 scopus 로고    scopus 로고
    • Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity
    • Tai H.L., Krynetski E.Y., Schuetz E.G., Yanishevski Y., and Evans W.E. Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity. Proc Natl Acad Sci USA 94 (1997) 6444-6449
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6444-6449
    • Tai, H.L.1    Krynetski, E.Y.2    Schuetz, E.G.3    Yanishevski, Y.4    Evans, W.E.5
  • 28
    • 0034710950 scopus 로고    scopus 로고
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble
    • Pan H., Lee J.C., and Hilser V.J. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. Proc Natl Acad Sci USA 97 (2000) 12020-12025
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12020-12025
    • Pan, H.1    Lee, J.C.2    Hilser, V.J.3
  • 29
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: tolerance to amino acid substitutions
    • Bowie J.U., Reidhaar-Olson J.F., Lim W.A., and Sauer R.T. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science 247 (1990) 1306-1310
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 30
    • 0026766573 scopus 로고
    • Structural and energetic consequences of disruptive mutations in a protein core
    • Lim W.A., Farruggio D.C., and Sauer R.T. Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 3 (1992) 4324-4333
    • (1992) Biochemistry , vol.3 , pp. 4324-4333
    • Lim, W.A.1    Farruggio, D.C.2    Sauer, R.T.3
  • 31
    • 27444443859 scopus 로고    scopus 로고
    • Thiopurine S-methyltransferase pharmacogenetics: variant allele functional and comparative genomics
    • Salavaggione O.E., Wang L., Wiepert M., Yee V.C., and Weinshilboum R.M. Thiopurine S-methyltransferase pharmacogenetics: variant allele functional and comparative genomics. Pharmacogenet Genomics 15 (2005) 801-815
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 801-815
    • Salavaggione, O.E.1    Wang, L.2    Wiepert, M.3    Yee, V.C.4    Weinshilboum, R.M.5
  • 32
    • 0032693405 scopus 로고    scopus 로고
    • Enhanced proteasomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C
    • Tai H.L., Fessing M.Y., Bonten E.J., Yanishevsky Y., d'Azzo A., Krynetski E.Y., et al. Enhanced proteasomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C. Pharmacogenetics 9 (1999) 641-650
    • (1999) Pharmacogenetics , vol.9 , pp. 641-650
    • Tai, H.L.1    Fessing, M.Y.2    Bonten, E.J.3    Yanishevsky, Y.4    d'Azzo, A.5    Krynetski, E.Y.6
  • 33
    • 34247094129 scopus 로고    scopus 로고
    • Three novel single nucleotide polymorphisms of the human thiopurine S-methyltransferase gene in Japanese individuals
    • Sasaki T., Goto E., Konno Y., Hiratsuka M., and Mizugaki M. Three novel single nucleotide polymorphisms of the human thiopurine S-methyltransferase gene in Japanese individuals. Drug Metab Pharmacokinet 21 (2006) 332-336
    • (2006) Drug Metab Pharmacokinet , vol.21 , pp. 332-336
    • Sasaki, T.1    Goto, E.2    Konno, Y.3    Hiratsuka, M.4    Mizugaki, M.5
  • 34
    • 0030048791 scopus 로고    scopus 로고
    • Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism
    • Szumlanski C., Otterness D., Her C., Lee D., Brandriff B., Kelsell D., et al. Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism. DNA Cell Biol 15 (1996) 17-30
    • (1996) DNA Cell Biol , vol.15 , pp. 17-30
    • Szumlanski, C.1    Otterness, D.2    Her, C.3    Lee, D.4    Brandriff, B.5    Kelsell, D.6
  • 35
    • 0031880735 scopus 로고    scopus 로고
    • Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis
    • Spire-Vayron de la Moureyre C., Debuysère H., Sabbagh N., Marez D., Vinner E., Chevalier E.D., et al. Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis. Hum Mutat 12 (1998) 177-185
    • (1998) Hum Mutat , vol.12 , pp. 177-185
    • Spire-Vayron de la Moureyre, C.1    Debuysère, H.2    Sabbagh, N.3    Marez, D.4    Vinner, E.5    Chevalier, E.D.6
  • 37
    • 0034093057 scopus 로고    scopus 로고
    • Genotypic analysis of thiopurine S-methyltransferase in patients with Crohn's disease and severe myelosuppression during azathioprine therapy
    • Colombel J.F., Ferrari N., Debuysere H., Marteau P., Gendre J.P., Bonaz B., et al. Genotypic analysis of thiopurine S-methyltransferase in patients with Crohn's disease and severe myelosuppression during azathioprine therapy. Gastroenterology 118 (2000) 1025-1030
    • (2000) Gastroenterology , vol.118 , pp. 1025-1030
    • Colombel, J.F.1    Ferrari, N.2    Debuysere, H.3    Marteau, P.4    Gendre, J.P.5    Bonaz, B.6
  • 38
    • 11844274653 scopus 로고    scopus 로고
    • Identification and functional analysis of two rare allelic variants of the thiopurine S-methyltransferase gene, TPMT*16 and TPMT*19
    • Hamdan-Khalil R., Gala J.L., Allorge D., Lo-Guidice J.M., Horsmans Y., Houdret N., et al. Identification and functional analysis of two rare allelic variants of the thiopurine S-methyltransferase gene, TPMT*16 and TPMT*19. Biochem Pharmacol 69 (2005) 525-529
    • (2005) Biochem Pharmacol , vol.69 , pp. 525-529
    • Hamdan-Khalil, R.1    Gala, J.L.2    Allorge, D.3    Lo-Guidice, J.M.4    Horsmans, Y.5    Houdret, N.6
  • 39
    • 34648851345 scopus 로고    scopus 로고
    • Explaining TPMT genotype/phenotype discrepancy by haplotyping of TPMT*3A and identification of a novel sequence variant, TPMT*23
    • Lindqvist M., Skoglund K., Karlgren A., Söderkvist P., Peterson C., Kidhall I., et al. Explaining TPMT genotype/phenotype discrepancy by haplotyping of TPMT*3A and identification of a novel sequence variant, TPMT*23. Pharmacogenet Genomics 17 (2007) 891-895
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 891-895
    • Lindqvist, M.1    Skoglund, K.2    Karlgren, A.3    Söderkvist, P.4    Peterson, C.5    Kidhall, I.6
  • 41
    • 0032030953 scopus 로고    scopus 로고
    • Human thiopurine methyltransferase pharmacogenetics. Kindred with a terminal exon splice junction mutation that results in loss of activity
    • Otterness D.M., Szumlanski C.L., Wood T.C., and Weinshilboum R.M. Human thiopurine methyltransferase pharmacogenetics. Kindred with a terminal exon splice junction mutation that results in loss of activity. J Clin Invest 101 (1998) 1036-1044
    • (1998) J Clin Invest , vol.101 , pp. 1036-1044
    • Otterness, D.M.1    Szumlanski, C.L.2    Wood, T.C.3    Weinshilboum, R.M.4
  • 42
    • 0038103074 scopus 로고    scopus 로고
    • A novel TPMT missense mutation associated with TPMT deficiency in a 5-year-old boy with ALL
    • Schaeffeler E., Stanulla M., Greil J., Schrappe M., Eichelbaum M., Zanger U.M., et al. A novel TPMT missense mutation associated with TPMT deficiency in a 5-year-old boy with ALL. Leukemia 17 (2003) 1422-1424
    • (2003) Leukemia , vol.17 , pp. 1422-1424
    • Schaeffeler, E.1    Stanulla, M.2    Greil, J.3    Schrappe, M.4    Eichelbaum, M.5    Zanger, U.M.6
  • 43
    • 1942435574 scopus 로고    scopus 로고
    • Identification of two novel sequence variants affecting thiopurine methyltransferase enzyme activity
    • Lindqvist M., Haglund S., Almer S., Peterson C., Taipalensu J., Hertervig E., et al. Identification of two novel sequence variants affecting thiopurine methyltransferase enzyme activity. Pharmacogenetics 14 (2004) 261-265
    • (2004) Pharmacogenetics , vol.14 , pp. 261-265
    • Lindqvist, M.1    Haglund, S.2    Almer, S.3    Peterson, C.4    Taipalensu, J.5    Hertervig, E.6


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