Gene-environment interactions in esophageal cancer

Critical Reviews in Clinical Laboratory Sciences

Volumn 52, Issue 5, 2015, Pages 211-231

  Matejcic, Marco ^a,b   Parker, M Iqbal ^a,b  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^b UNIVERSITY OF CAPE TOWN   (South Africa)

Author keywords

cytochrome P450; epoxide hydrolase; Esophageal cancer; genetic and environmental risk factors; glutathione S transferase; N acetyltransferase; sulfotransferase; UDP glucuronosyltransferase

Indexed keywords

ACYLTRANSFERASE; CARCINOGEN; CYTOCHROME P450; CYTOCHROME P450 1A1; CYTOCHROME P450 2E1; CYTOCHROME P450 3A; DNA; EPOXIDE HYDROLASE; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE M1; GLUTATHIONE TRANSFERASE M3; GLUTATHIONE TRANSFERASE P1; GLUTATHIONE TRANSFERASE T1; GLUTATHIONE TRANSFERASE T2; NORADRENALIN TRANSPORTER; NORADRENALIN TRANSPORTER 2; SULFOTRANSFERASE; SULFOTRANSFERASE 1A1; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

BIOSYNTHESIS; CARCINOGENESIS; DETOXIFICATION; ENVIRONMENTAL FACTOR; ESOPHAGUS CANCER; GENETIC ASSOCIATION; GENETIC POLYMORPHISM; GENETIC RISK; GENETIC SUSCEPTIBILITY; GENOTYPE ENVIRONMENT INTERACTION; HUMAN; METABOLISM; MORTALITY; PRIORITY JOURNAL; REVIEW; RISK FACTOR; ADENOCARCINOMA; CARCINOMA, SQUAMOUS CELL; CHEMICALLY INDUCED; ENZYMOLOGY; ESOPHAGEAL NEOPLASMS; FOOD CONTAMINATION; GENETICS; METABOLIC ACTIVATION; TOXICOKINETICS;

ACTIVATION, METABOLIC; ADENOCARCINOMA; CARCINOGENS, ENVIRONMENTAL; CARCINOMA, SQUAMOUS CELL; ESOPHAGEAL NEOPLASMS; FOOD CONTAMINATION; GENE-ENVIRONMENT INTERACTION; HUMANS; POLYMORPHISM, GENETIC; RISK FACTORS; TOXICOKINETICS; XENOBIOTICS;

EID: 84941733695     PISSN: 10408363     EISSN: 1549781X     Source Type: Journal    
DOI: 10.3109/10408363.2015.1020358     Document Type: Review

References (229)

1. Parkin DM, Bray F, Ferlay J, Pisani P. Global cancer statistics, 2002. CA Cancer J Clin 2005;55:74-108.
2. Mudan SM, Kang JY. Epidemiology and clinical presentation in esophageal cancer. In: Rankin SC, ed. Carcinoma of the Esophagus. Cambridge: Cambridge University Press, 2007:1-13.
3. van Blankenstein M, Looman CW, Hop WC, Bytzer P. The incidence of adenocarcinoma and squamous cell carcinoma of the esophagus: Barrett's esophagus makes a difference. Am J Gastroenterol 2005;100:766-74.
4. Steevens J, Schouten LJ, Goldbohm RA, van den Brandt PA. Alcohol consumption, cigarette smoking and risk of subtypes of oesophageal and gastric cancer: a prospective cohort study. Gut 2010;59:39-48.
5. Kamangar F, Chow WH, Abnet CC, Dawsey SM. Environmental causes of esophageal cancer. Gastroenterol Clin North Am 2009; 38:27-57.
6. Singh MS, Michael M. Role of xenobiotic metabolic enzymes in cancer epidemiology. Methods Mol Biol 2009;472:243-64.
7. Liska DJ. The detoxification enzyme systems. Altern Med Rev 1998;3:187-98.
8. Ingelman-Sundberg M, Sim SC, Gomez A, Rodriguez-Antona C. Influence of cytochrome P450 polymorphisms on drug therapies: pharmacogenetic, pharmacoepigenetic and clinical aspects. Pharmacol Ther 2007;116:496-526.
9. Nakajima T, Wang RS, Nimura Y, et al. Expression of cytochrome P450s and glutathione S-transferases in human esophagus with squamous-cell carcinomas. Carcinogenesis 1996;17:1477-81.
10. den Dunnen JT, Antonarakis SE. Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion. Hum Mutat 2000;15:7-12.
11. Garte S, Boffetta P, Caporaso N, Vineis P. Metabolic gene allele nomenclature. Cancer Epidemiol Biomarkers Prev 2001;10: 1305-6.
12. Gonzalez FJ, Gelboin HV. Role of human cytochromes 450 in the metabolic activation of chemical carcinogens and toxins. Drug Metab Rev 1994;26:165-83.
13. Lechevrel M, Casson AG, Wolf CR, et al. Characterization of cytochrome P450 expression in human oesophageal mucosa. Carcinogenesis 1999;20:243-8.
14. Murray M. Altered CYP expression and function in response to dietary factors: potential roles in disease pathogenesis. Curr Drug Metab 2006;7:67-81.
15. Wong PS, Eiserich JP, Reddy S, et al. Inactivation of glutathione S-transferases by nitric oxide-derived oxidants: exploring a role for tyrosine nitration. Arch Biochem Biophys 2001;394:216-28.
16. Pascussi JM, Gerbal-Chaloin S, Duret C, et al. The tangle of nuclear receptors that controls xenobiotic metabolism and transport: crosstalk and consequences. Annu Rev Pharmacol Toxicol 2008;48:1-32.
17. Lamba JK. Pharmacogenetics of the constitutive androstane receptor. Pharmacogenomics 2008;9:71-83.
18. Ding X, Kaminsky LS. Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. Annu Rev Pharmacol Toxicol 2003;43:149-73.
19. Shimada T, Gillam EM, Sutter TR, et al. Oxidation of xenobiotics by recombinant human cytochrome P450 1B1. Drug Metab Dispos 1997;25:617-22.
20. Kim JH, Sherman ME, Curriero FC, et al. Expression of cytochromes P450 1A1 and 1B1 in human lung from smokers, non-smokers, and ex-smokers. Toxicol Appl Pharmacol 2004;199: 210-19.
21. Hildebrand CE, Gonzalez FJ, McBride OW, Nebert DW. Assignment of the human 2,3,7,8-tetrachlorodibenzo-p-dioxininducible cytochrome P1-450 gene to chromosome 15. Nucleic Acids Res 1985;13:2009-16.
22. Crofts F, Taioli E, Trachman J, et al. Functional significance of different human CYP1A1 genotypes. Carcinogenesis 1994;15: 2961-3.
23. Landi MT, Bertazzi PA, Shields PG, et al. Association between CYP1A1 genotype, mRNA expression and enzymatic activity in humans. Pharmacogenetics 1994;4:242-6.
24. Hirvonen A, Husgafvel-Pursiainen K, Karjalainen A, et al. Pointmutational MspI and Ile-Val polymorphisms closely linked in the CYP1A1 gene: lack of association with susceptibility to lung cancer in a Finnish study population. Cancer Epidemiol Biomarkers Prev 1992;1:485-9.
25. Hayashi S, Watanabe J, Nakachi K, Kawajiri K. Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P450IA1 gene. J Biochem 1991;110:407-11.
26. Taioli E, Crofts F, Trachman J, et al. Radical differences in CYP1A1 genotype and function. Toxicol Lett 1995;77:357-62.
27. Yousef AM, Bulatova NR, Newman W, et al. Allele and genotype frequencies of the polymorphic cytochrome P450 genes (CYP1A1, CYP3A4, CYP3A5, CYP2C9 and CYP2C19) in the Jordanian population. Mol Biol Rep 2012;39:9423-33.
28. Chen Z, Li Z, Niu X, et al. The effect of CYP1A1 polymorphisms on the risk of lung cancer: a global meta-analysis based on 71 case-control studies. Mutagenesis 2011;26:437-46.
29. Zhan P, Wang Q, Qian Q, et al. CYP1A1 Msp1 and exon7 gene polymorphisms and lung cancer risk: an updated meta-analysis and review. J Exp Clin Cancer Res 2011;30:99. doi: 10.1186/1756-9966-30-99.
30. Ji YN, Wang Q, Suo LJ. CYP1A1 Ile462Val polymorphism contributes to lung cancer susceptibility among lung squamous carcinoma and smokers: a meta-analysis. PLoS One 2012;7(8): e43397. doi: 10.1371/journal.pone.0043397. Epub 2012 Aug 28.
31. Wu MT, Lee JM, Wu DC, et al. Genetic polymorphisms of cytochrome P4501A1 and oesophageal squamous-cell carcinoma in Taiwan. Br J Cancer 2002;87:529-32.
32. Bhat GA, Shah IA, Makhdoomi MA, et al. CYP1A1 and CYP2E1 genotypes and risk of esophageal squamous cell carcinoma in a high-incidence region, Kashmir. Tumour Biol 2014;35:5323-30.
33. Malik MA, Upadhyay R, Mittal RD, et al. Association of xenobiotic metabolizing enzymes genetic polymorphisms with esophageal cancer in Kashmir Valley and influence of environmental factors. Nutr Cancer 2010;62:734-42.
34. Jain M, Kumar S, Ghoshal UC, Mittal B. CYP1A1 Msp1 T/C polymorphism in esophageal cancer: no association and risk modulation. Oncol Res 2007;16:437-43.
35. Roth MJ, Abnet CC, Johnson LL, et al. Polymorphic variation of Cyp1A1 is associated with the risk of gastric cardia cancer: a prospective case-cohort study of cytochrome P-450 1A1 and GST enzymes. Cancer Causes Control 2004;15:1077-83.
36. Wang Z, Tang L, Sun G, et al. Etiological study of esophageal squamous cell carcinoma in an endemic region: a populationbased case control study in Huaian, China. BMC Cancer 2006;6: 287.
37. Morita S, Yano M, Shiozaki H, et al. CYP1A1, CYP2E1 and GSTM1 polymorphisms are not associated with susceptibility to squamous-cell carcinoma of the esophagus. Int J Cancer 1997;71: 192-5.
38. Casson AG, Zheng Z, Chiasson D, et al. Associations between genetic polymorphisms of Phase I and II metabolizing enzymes, p53 and susceptibility to esophageal adenocarcinoma. Cancer Detect Prev 2003;27:139-46.
39. Wideroff L, Vaughan TL, Farin FM, et al. GST, NAT1, CYP1A1 polymorphisms and risk of esophageal and gastric adenocarcinomas. Cancer Detect Prev 2007;31:233-6.
40. Shen FF, Zhou FY, Xue QS, et al. Association between CYP1A1 polymorphisms and esophageal cancer: a meta-analysis. Mol Biol Rep 2013;40:6035-42.
41. Shimada T, Yamazaki H, Mimura M, et al. Interindividual variations in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens, and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians. J Pharmacol Exp Ther 1994;270:414-23.
42. Kessova I, Cederbaum AI. CYP2E1: biochemistry, toxicology, regulation and function in ethanol-induced liver injury. Curr Mol Med 2003;3:509-18.
43. Bolt HM, Roos PH, Thier R. The cytochrome P-450 isoenzyme CYP2E1 in the biological processing of industrial chemicals: consequences for occupational and environmental medicine. Int Arch Occup Environ Health 2003;76:174-85.
44. Yin H, Anders MW, Korzekwa KR, et al. Designing safer chemicals: predicting the rates of metabolism of halogenated alkanes. Proc Natl Acad Sci USA 1995;92:11076-80.
45. Umeno M, McBride OW, Yang CS, et al. Human ethanolinducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry 1988;27:9006-13.
46. Hayashi S, Watanabe J, Kawajiri K. Genetic polymorphism in the 5′-flanking region changes the transcriptional regulation of the human cytochrome P450 2E1 gene. J Biochem 1991;110: 559-65.
47. Watanabe J, Hayashi S, Kawajiri K. Different regulation and expression of the human CYP2E1 gene due to the RsaI polymorphism in the 5′-flanking region. J Biochem 1994;116: 321-6.
48. Liu S, Park JY, Schantz SP, et al. Elucidation of CYP2E1 5′ regulatory RsaI/Pstl allelic variants and their role in risk for oral cancer. Oral Oncol 2001;37:437-45.
49. Stephens EA, Taylor JA, Kaplan N, et al. Ethnic variation in the CYP2E1 gene: polymorphism analysis of 695 African-Americans, European-Americans and Taiwanese. Pharmacogenetics 1994;4: 185-92.
50. Chelule PK, Pegoraro RJ, Gqaleni N, Dutton MF. The frequency of cytochrome P450 2E1 polymorphisms in Black South Africans. Dis Markers 2006;22:351-4.
51. Marchand LL, Wilkinson GR, Wilkens LR. Genetic and dietary predictors of CYP2E1 activity: a phenotyping study in Hawaii Japanese using chlorzoxazone. Cancer Epidemiol Biomarkers Prev 1999;8:495-500.
52. Millonig G, Wang Y, Homann N, et al. Ethanol-mediated carcinogenesis in the human esophagus implicates CYP2E1 induction and the generation of carcinogenic DNA-lesions. Int J Cancer 2011;128:533-40.
53. Uematsu F, Ikawa S, Kikuchi H, et al. Restriction fragment length polymorphism of the human CYP2E1 (cytochrome P450IIE1) gene and susceptibility to lung cancer: possible relevance to low smoking exposure. Pharmacogenetics 1994;4:58-63.
54. Garte S, Gaspari L, Alexandrie AK, et al. Metabolic gene polymorphism frequencies in control populations. Cancer Epidemiol Biomarkers Prev 2001;10:1239-48.
55. Hu Y, Oscarson M, Johansson I, et al. Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol 1997;51:370-6.
56. Uchimoto T, Itoga S, Nezu M, et al. Role of the genetic polymorphisms in the 5′-flanking region for transcriptional regulation of the human CYP2E1 gene. Alcohol Clin Exp Res 2007;31:S36-42.
57. McCarver DG, Byun R, Hines RN, et al. A genetic polymorphism in the regulatory sequences of human CYP2E1: association with increased chlorzoxazone hydroxylation in the presence of obesity and ethanol intake. Toxicol Appl Pharmacol 1998;152: 276-81.
58. Fritsche EPittman GS, Bell DA. Localization, sequence analysis, and ethnic distribution of a 96-bp insertion in the promoter of the human CYP2E1 gene. Mutat Res 2000;432:1-5.
59. Wang Y, Yang H, Li L, et al. Association between CYP2E1 genetic polymorphisms and lung cancer risk: a meta-analysis. Eur J Cancer 2010;46:758-64.
60. Feng J, Pan X, Yu J, et al. Functional PstI/RsaI polymorphism in CYP2E1 is associated with the development, progression and poor outcome of gastric cancer. PLoS One 2012;7:e44478.
61. Jiang O, Zhou R, Wu D, et al. CYP2E1 polymorphisms and colorectal cancer risk: a HuGE systematic review and metaanalysis. Tumour Biol 2013;34:1215-24.
62. Tang K, Li Y, Zhang Z, et al. The PstI/RsaI and DraI polymorphisms of CYP2E1 and head and neck cancer risk: a meta-analysis based on 21 case-control studies. BMC Cancer 2010;10:575.
63. Lin DX, Tang YM, Peng Q, et al. Susceptibility to esophageal cancer and genetic polymorphisms in glutathione S-transferases T1, P1, and M1 and cytochrome P450 2E1. Cancer Epidemiol Biomarkers Prev 1998;7:1013-18.
64. Tan W, Song N, Wang GQ, et al. Impact of genetic polymorphisms in cytochrome P450 2E1 and glutathione S-transferases M1, T1, and P1 on susceptibility to esophageal cancer among high-risk individuals in China. Cancer Epidemiol Biomarkers Prev 2000;9: 551-6.
65. Itoga S, Nomura F, Makino Y, et al. Tandem repeat polymorphism of the CYP2E1 gene: an association study with esophageal cancer and lung cancer. Alcohol Clin Exp Res 2002;26: 15S-9S.
66. Rossini A, Rapozo DC, Soares Lima SC, et al. Polymorphisms of GSTP1 and GSTT1, but not of CYP2A6, CYP2E1 or GSTM1, modify the risk for esophageal cancer in a western population. Carcinogenesis 2007;28:2537-42.
67. Li D, Dandara C, Parker MI. Association of cytochrome P450 2E1 genetic polymorphisms with squamous cell carcinoma of the oesophagus. Clin Chem Lab Med 2005;43:370-5.
68. Niu Y, Yuan H, Leng W, et al. CYP2E1 Rsa1/Pst1 polymorphism and esophageal cancer risk: a meta-analysis based on 1088 cases and 2,238 controls. Med Oncol 2011;28:182-7.
69. Westlind A, Löfberg L, Tindberg N, et al. Interindividual differences in hepatic expression of CYP3A4: relationship to genetic polymorphism in the 5′-upstream regulatory region. Biochem Biophys Res Commun 1999;259:201-5.
70. Canaparo R, Finnström N, Serpe L, et al. Expression of CYP3A isoforms and P-glycoprotein in human stomach, jejunum and ileum. Clin Exp Pharmacol Physiol 2007;34:1138-44.
71. Gellner K, Eiselt R, Hustert E, et al. Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics 2001;11:111-21.
72. Huang W, Lin YS, McConn II DJ, et al. Evidence of significant contribution from CYP3A5 to hepatic drug metabolism. Drug Metab Dispos 2004;32:1434-45.
73. Kuehl P, Zhang J, Lin Y, et al. Sequence diversity in CYP3A promoters and characterization of the genetic basis of polymorphic CYP3A5 expression. Nat Genet 2001;27:383-91.
74. Lamba JK, Lin YS, Schuetz EG, Thummel KE. Genetic contribution to variable human CYP3A-mediated metabolism. Adv Drug Deliv Rev 2002;54:1271-94.
75. Roy JN, Lajoie J, Zijenah LS, et al. CYP3A5 genetic polymorphisms in different ethnic populations. Drug Metab Dispos 2005;33: 884-7.
76. Dandara C, Ballo R, Parker MI. CYP3A5 genotypes and risk of oesophageal cancer in two South African populations. Cancer Lett 2005;225:275-82.
77. Wang BS, Liu Z, Xu WX, Sun SL. CYP3A5∗3 polymorphism and cancer risk: a meta-analysis and meta-regression. Tumour Biol 2013;34:2357-66.
78. Dandara C, Li DP, Walther G, Parker MI. Gene-environment interaction: the role of SULT1A1 and CYP3A5 polymorphisms as risk modifiers for squamous cell carcinoma of the oesophagus. Carcinogenesis 2006;27:791-7.
79. Hyland PL, Freedman ND, Hu N, et al. Genetic variants in sex hormone metabolic pathway genes and risk of esophageal squamous cell carcinoma. Carcinogenesis 2013;34:1062-8.
80. Morisseau C, Hammock BD. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu Rev Pharmacol Toxicol 2005;45:311-33.
81. Seidegård J, Ekström G. The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics. Environ Health Perpect 1997;105:791-9.
82. Petruzzelli S, Camus AM, Carrozzi L, et al. Long-lasting effects of tobacco smoking on pulmonary drug-metabolizing enzymes: a case-control study on lung cancer patients. Cancer Res 1988;48: 4695-700.
83. Enayetallah AE, French RA, Thibodeau MS, Grant DF. Distribution of soluble epoxide hydrolase and of cytochrome P450 2C8, 2C9, and 2J2 in human tissues. J Histochem Cytochem 2004;52:447-54.
84. Hartsfield Jr JK, Sutcliffe MJ, Everett ET, et al. Assignment of microsomal epoxide hydrolase (EPHX1) to human chromosome 1q42.1 by in situ hybridization. Cytogenet Cell Genet 1998;83: 44-5.
85. Hassett C, Aicher L, Sidhu JS, Omiecinski CJ. Human microsomal epoxide hydrolase: genetic polymorphism and functional expression in vitro of amino acid variants. Hum Mol Genet 1994;3: 421-8.
86. Kiyohara C, Yoshimasu K, Takayama K, Nakanishi Y. EPHX1 polymorphisms and the risk of lung cancer: a HuGE review. Epidemiology 2006;17:89-99.
87. Gebhardt GS, Peters WH, Hillermann R, et al. Maternal and fetal single nucleotide polymorphisms in the epoxide hydrolase and gluthatione S-transferase P1 genes are not associated with preeclampsia in the coloured population of the Western Cape, South Africa. J Obstet Gynaecol 2004;24:866-72.
88. Li X, Hu Z, Qu X, et al. Putative EPHX1 enzyme activity is related with risk of lung and upper aerodigestive tract cancers: a comprehensive meta-analysis. PLoS One 2011;6:e14749.
89. Ihsan R, Chattopadhyay I, Phukan R, et al. Role of epoxide hydrolase 1 gene polymorphisms in esophageal cancer in a high-risk area in India. J Gastroenterol Hepatol 2010;25: 1456-62.
90. Jain M, Tilak AR, Upadhyay R, et al. Microsomal epoxide hydrolase (EPHX1), slow (exon 3, 113His) and fast (exon 4, 139Arg) alleles confer susceptibility to squamous cell esophageal cancer. Toxicol Appl Pharmacol 2008;230:247-51.
91. Lin YC, Wu DC, Lee JM, et al. The association between microsomal epoxide hydrolase genotypes and esophageal squamous-cell-carcinoma in Taiwan: interaction between areca chewing and smoking. Cancer Lett 2006;237:281-8.
92. Dura P, Bregitha CV, Te Morsche RH, et al. EPHX1 polymorphisms do not modify esophageal carcinoma susceptibility in Dutch Caucasians. Oncol Rep 2012;27:1710-16.
93. Casson AG, Zheng Z, Porter GA, Guernsey DL. Genetic polymorphisms of microsomal epoxide hydroxylase and glutathione S-transferases M1, T1 and P1, interactions with smoking, and risk for esophageal (Barrett) adenocarcinoma. Cancer Detect Prev 2006;30:423-31.
94. Zhao W, Luo J, Cai X. Association between microsomal epoxide hydrolase 1 polymorphisms and susceptibility to esophageal cancer: a meta-analysis. Tumour Biol 2013;34:2383-8.
95. Hayes JD, Flanagan JU, Jowsey IR. Glutathione transferases. Annu Rev Pharmacol Toxicol 2005;45:51-88.
96. Landi S. Mammalian class theta GST and differential susceptibility to carcinogens: a review. Mutat Res 2000;463:247-83.
97. Rowe JD, Nieves E, Listowsky I. Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequencespecific antisera. Biochem J 1997;325:481-6.
98. Srám RJ. Effect of glutathione S-transferase M1 polymorphisms on biomarkers of exposure and effects. Environ Health Perspect 1998;106:231-9.
99. Pearson WR, Vorachek WR, Xu SJ, et al. Identification of classmuglutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am J Hum Genet 1993;53:220-33.
100. Bolt HM, Thier R. Relevance of the deletion polymorphisms of the glutathione S-transferases GSTT1 and GSTM1 in pharmacology and toxicology. Curr Drug Metab 2006;7:613-28.
101. Brockmöller J, Gross D, Kerb R, et al. Correlation between transstilbene oxide-glutathione conjugation activity and the deletion mutation in the glutathione S-transferase class mu gene detected by polymerase chain reaction. Biochem Pharmacol 1992;43: 647-50.
102. McCarroll SA, Hadnott TN, Perry GH, et al.; International HapMap Consortium. Common deletion polymorphisms in the human genome. Nat Genet 2006;38:86-92.
103. Adams CH, Werely CJ, Victor TC, et al. Allele frequencies for glutathione S-transferase and N-acetyltransferase 2 differ in African population groups and may be associated with oesophageal cancer or tuberculosis incidence. Clin Chem Lab Med 2003; 41:600-5.
104. Liu X, Li Z, Zhang Z, et al. Meta-analysis of GSTM1 null genotype and lung cancer risk in Asians. Med Sci Monit 2014;20: 1239-45.
105. Meng X, Liu Y, Liu B. Glutathione S-transferase M1 null genotype meta-analysis on gastric cancer risk. Diagn Pathol 2014; 9:122. doi: 10.1186/1746-1596-9-122.
106. Song K, Yi J, Shen X, Cai Y. Genetic polymorphisms of glutathione S-transferase genes GSTM1, GSTT1 and risk of hepatocellular carcinoma. PLoS One 2012;7:e48924.
107. Teng Z, Wang L, Zhang J, et al. Glutathione S-transferase M1 polymorphism and colorectal cancer risk in Chinese population. Tumour Biol 2014;35:2117-21.
108. Wei B, Xu Z, Zhou Y, et al. Association of GSTM1 null allele with prostate cancer risk: evidence from 36 case-control studies. PLoS One 2012;7:e46982.
109. Zhang ZJ, Hao K, Shi R, et al. Glutathione S-transferase M1 (GSTM1) and glutathione S-transferase T1 (GSTT1) null polymorphisms, smoking, and their interaction in oral cancer: a HuGE review and meta-analysis. Am J Epidemiol 2011;173: 847-57.
110. Gao CM, Takezaki T, Wu JZ, et al. Glutathione-S-transferases M1 (GSTM1) and GSTT1 genotype, smoking, consumption of alcohol and tea and risk of esophageal and stomach cancers: a case-control study of a high-incidence area in Jiangsu Province, China. Cancer Lett 2002;188:95-102.
111. Yokoyama A, Kato H, Yokoyama T, et al. Genetic polymorphisms of alcohol and aldehyde dehydrogenases and glutathione S-transferase M1 and drinking, smoking, and diet in Japanese men with esophageal squamous cell carcinoma. Carcinogenesis 2002;23:1851-9.
112. Djansugurova LB, Perfilyeva AV, Zhunusova GS, et al. The determination of genetic markers of age-related cancer pathologies in populations from Kazakhstan. Front Genet 2013;4:70. doi: 10.3389/fgene.2013.00070.
113. Sharma A, Das BC, Sehgal A, et al. GSTM1 and GSTT1 polymorphism and susceptibility to esophageal cancer in high-and low-risk regions of India. Tumour Biol 2013;34:3249-57.
114. Jain M, Kumar S, Rastogi N, et al. GSTT1, GSTM1 and GSTP1 genetic polymorphisms and interaction with tobacco, alcohol and occupational exposure in esophageal cancer patients from North India. Cancer Lett 2006;242:60-7.
115. Moaven O, Raziee HR, Sima HR, et al. Interaction between glutathione-S-transferase M1, T1 and P1 polymorphisms and smoking, and increased susceptibility to esophageal squamous cell carcinoma. Cancer Epidemiol 2010;34:285-90.
116. Dura P, Salomon J, Te Morsche RH, et al. No role for glutathione S-transferase genotypes in Caucasian esophageal squamous cell or adenocarcinoma etiology: an European case-control study. BMC Gastroenterol 2013;13:97.
117. Zendehdel K, Bahmanyar S, McCarthy S, et al. Genetic polymorphisms of glutathione S-transferase genes GSTP1, GSTM1, and GSTT1 and risk of esophageal and gastric cardia cancers. Cancer Causes Control 2009;20:2031-8.
118. Li D, Dandara C, Parker MI. The 341C/T polymorphism in the GSTP1 gene is associated with increased risk of oesophageal cancer. BMC Genet 2010;11:47.
119. Zhuo WL, Zhang YS, Wang Y, et al. Association studies of CYP1A1 and GSTM1 polymorphisms with esophageal cancer risk: evidence-based meta-analyses. Arch Med Res 2009;40:169-79.
120. Anttila S, Luostarinen L, Hirvonen A, et al. Pulmonary expression of glutathione S-transferase M3 in lung cancer patients: association with GSTM1 polymorphism, smoking, and asbestos exposure. Cancer Res 1995;55:3305-9.
121. Inskip A, Elexperu-Camiruaga J, Buxton N, et al. Identification of polymorphism at the glutathione S-transferase, GSTM3 locus: evidence for linkage with GSTM1∗A. Biochem J 1995;312:713-16.
122. Nakajima T, Elovaara E, Anttila S, et al. Expression and polymorphism of glutathione S-transferase in human lungs: risk factors in smoking-related lung cancer. Carcinogenesis 1995;16: 707-11.
123. Teixeira D, Vargens D, Príncipe A, et al. High prevalence of the GSTM3∗A/B polymorphism in sub-Sarahan African populations. Braz J Med Biol Res 2010;43:677-80.
124. Xu Y, Wang J, Dong W. GSTM3 A/B polymorphism and risk for head and neck cancer: a meta-analysis. PLoS One 2014;9: e83851.
125. Sikdar N, Paul RR, Roy B. Glutathione S-transferase M3 (A/A) genotype as a risk factor for oral cancer and leukoplakia among Indian tobacco smokers. Int J Cancer 2004;109:95-101.
126. Jain M, Kumar S, Lal P, et al. Role of GSTM3 polymorphism in the risk of developing esophageal cancer. Cancer Epidemiol Biomarkers Prev 2007;16:178-81.
127. Sherratt PJ, Manson MM, Thomson AM, et al. Increased bioactivation of dihaloalkanes in rat liver due to induction of class theta glutathione S-transferase T1-1. Biochem J 1998;335: 619-30.
128. Coggan M, Whitbread L, Whittington A, Board P. Structure and organization of the human theta-class glutathione S-transferase and D-dopachrome tautomerase gene complex. Biochem J 1998; 334:617-23.
129. Sprenger R, Schlagenhaufer R, Kerb R, et al. Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics 2000;10: 557-65.
130. Löf A, Johanson G, Rannug A, Warholm M. Glutathione transferase T1 phenotype affects the toxicokinetics of inhaled methyl chloride in human volunteers. Pharmacogenetics 2000;10: 645-53.
131. Yang Q, Du J, Yao X. Significant association of Glutathione S-transferase T1 null genotype with prostate cancer risk: a metaanalysis of 26,393 subjects. PLoS One 2013;8:e53700.
132. He HR, Zhang XX, Sun JY, et al. Glutathione S-transferase gene polymorphisms and susceptibility to chronic myeloid leukemia. Tumour Biol 2014;35:6119-25.
133. Ma W, Zhuang L, Han B, Tang B. Association between glutathione S-transferase T1 null genotype and gastric cancer risk: a meta-analysis of 48 studies. PLoS One 2013;8:e60833.
134. Matejcic M, Li D, Prescott NJ, et al. Association of a deletion of GSTT2B with an altered risk of oesophageal squamous cell carcinoma in a South African population: a case-control study. PLoS One 2011;6:e29366.
135. Cai Y, Wang J. Significant association of glutathione S-transferase T1 null genotype with esophageal cancer risk: a meta-analysis. Mol Biol Rep 2013;40:2397-403.
136. Hurst R, Bao Y, Jemth P, et al. Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases. Biochem J 1998;332:97-100.
137. Marnett LJ. Oxy radicals, lipid peroxidation and DNA damage. Toxicology 2002;181-182:219-22.
138. Zhao Y, Marotta M, Eichler EE, et al. Linkage disequilibrium between two high-frequency deletion polymorphisms: implications for association studies involving the glutathione-S transferase (GST) genes. PLoS Genetics 2009;5:e1000472.
139. Jang SG, Kim IJ, Kang HC, et al. GSTT2 promoter polymorphisms and colorectal cancer risk. BMC Cancer 2007;7:16.
140. Zienolddiny S, Campa D, Lind H, et al. A comprehensive analysis of phase I and phase II metabolism gene polymorphisms and risk of non-small cell lung cancer in smokers. Carcinogenesis 2008;29: 1164-9.
141. Fields WR, Morrow CS, Doss AJ, et al. Overexpression of stably transfected human glutathione S-transferase P1-1 protects against DNA damage by benzo[a]pyrene diol-epoxide in human T47D cells. Mol Pharmacol 1998;54:298-304.
142. Berhane K, Widersten M, Engstrom M, et al. Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc Natl Acad Sci USA 1994; 91:1480-4.
143. Morrow CS, Cowan KH, Goldsmith ME. Structure of the human genomic glutathione S-transferase-pi gene. Gene 1989; 75:3-11.
144. Ali-Osman F, Akande O, Antoun G, et al. Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J Biol Chem 1997;272:10004-12.
145. Watson MA, Stewart RK, Smith GB, et al. Human glutathione Stransferase P1 polymorphisms: relationship to lung tissue enzyme activity and population frequency distribution. Carcinogenesis 1998;19:275-80.
146. Ryberg D, Skaug V, Hewer A, et al. Genotypes of glutathione transferase M1 and P1 and their significance for lung DNA adduct levels and cancer risk. Carcinogenesis 1997;18:1285-9.
147. Harries LW, Stubbins MJ, Forman D, et al. Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer. Cacinogenesis 1997;18:641-4.
148. Huang SX, Wu FX, Luo M, et al. The glutathione S-transferase P1 341C>T polymorphism and cancer risk: a meta-analysis of 28 case-control studies. PLoS One 2013;8:e56722.
149. Cai L, Mu LN, Lu H, et al. Dietary selenium intake and genetic polymorphisms of the GSTP1 and p53 genes on the risk of esophageal squamous cell carcinoma. Cancer Epidemiol Biomarkers Prev 2006;15:294-300.
150. Lee JM, Lee YC, Yang SY, et al. Genetic polymorphisms of p53 and GSTP1, but not NAT2, are associated with susceptibility to squamous-cell carcinoma of the esophagus. Int J Cancer 2000;89: 458-64.
151. Morita S, Yano M, Tsujinaka T, et al. Association between genetic polymorphisms of glutathione S-transferase P1 and N-acetyltransferase 2 and susceptibility to squamous-cell carcinoma of the esophagus. Int J Cancer 1998;79:517-20.
152. Zhao Y, Wang F, Shan S, et al. Genetic polymorphism of p53, but not GSTP1, is association with susceptibility to esophageal cancer risk - a meta-analysis. Int J Med Sci 2010;7:300-8.
153. Hein DW. Molecular genetics and function of NAT1 and NAT2: role in aromatic amine metabolism and carcinogenesis. Mutat Res 2002;506-7:65-77.
154. Hickman D, Risch A, Buckle V, et al. Chromosomal localization of human genes for arylamine N-acetyltransferase. Biochem J 1994;297:441-5.
155. Hein DW, Doll MA, Rustan TD, et al. Metabolic activation and deactivation of arylamine carcinogens by recombinant human NAT1 and polymorphic NAT2 acetyltransferases. Carcinogenesis 1993;14:1633-8.
156. Barker DF, Husain A, Neale JR, et al. Functional properties of an alternative, tissue-specific promoter for human arylamine N-acetyltransferase 1. Pharmacogenet Genomics 2006;16:515-25.
157. Husain A, Zhang X, Doll MA, et al. Identification of N-acetyltransferase 2 (NAT2) transcription start sites and quantitation of NAT2-specific mRNA in human tissues. Drug Metab Dispos 2007;35:721-7.
158. Zang Y, Doll MA, Zhao S, et al. Functional characterization of single-nucleotide polymorphisms and haplotypes of human N-acetyltransferase 2. Carcinogenesis 2007;28:1665-71.
159. Fretland AJ, Doll MA, Zhu Y, et al. Effect of nucleotide substitutions in N-acetyltransferase-1 on N-acetylation (deactivation) and O-acetylation (activation) of arylamine carcinogens: implications for cancer predisposition. Cancer Detect Prev 2002; 26:10-14.
160. Djordjevic N, Carrillo JA, Ueda N, et al. N-Acetyltransferase-2 (NAT2) gene polymorphisms and enzyme activity in Serbs: unprecedented high prevalence of rapid acetylators in a White population. J Clin Pharmacol 2011;51:994-1003.
161. Zhu Y, States JC, Wang Y, Hein DW. Functional effects of genetic polymorphisms in the N-acetyltransferase 1 coding and 3′ untranslated regions. Birth Defects Res A Clin Mol Teratol 2011; 91:77-84.
162. Butcher NJ, Ilett KF, Minchin RF. Substrate-dependent regulation of human arylamine N-acetyltransferase-1 in cultured cells. Mol Pharmacol 2000;57:468-73.
163. Hein DW. N-Acetyltransferase genetics and their role in predisposition to aromatic and heterocyclic amine-induced carcinogenesis. Toxicol Lett 2000;112-3:349-56.
164. Minchin RF. Acetylation of p-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells. Biochem J 1995;307:1-3.
165. Minchin RF, Hanna PE, Dupret JM, et al. Arylamine N-acetyltransferase I. Int J Biochem Cell Biol 2007; 39:1999-2005.
166. Wang D, Para MF, Koletar SL, Sadee W. Human N-acetyltransferase 1 ∗10 and ∗11 alleles increase protein expression through distinct mechanisms and associate with sulfamethoxazole-induced hypersensitivity. Pharmacogenet Genomics 2011;21:652-64.
167. Cascorbi I, Roots I, Brockmöller J. Association of NAT1 and NAT2 polymorphisms to urinary bladder cancer: significantly reduced risk in subjects with NAT1∗10. Cancer Res 2001;61: 5051-6.
168. Loktionov A, Moore W, Spencer SP, et al. Differences in Nacetylation genotypes between Caucasians and Black South Africans: implications for cancer prevention. Cancer Detect Prev 2002;26:15-22.
169. Dhaini HR, Levy GN. Arylamine N-acetyltransferase 1 (NAT1) genotypes in a Lebanese population. Pharmacogenetics 2000;10: 79-83.
170. Butcher NJ, Minchin RF. Arylamine N-acetyltransferase 1: a novel drug target in cancer development. Pharmacol Rev 2012;64: 147-65.
171. Matejcic M, Vogelsang M, Wang Y, Parker MI. NAT1 and NAT2 genetic polymorphisms and environmental exposure as risk factors for oesophageal squamous cell carcinoma: a case-control study. BMC Cancer 2015;15:150. doi: 10.1186/s12885-015-1105-4.
172. Boukouvala S, Sim E. Structural analysis of the genes for human arylamine N-acetyltransferases and characterisation of alternative transcripts. Basic Clin Pharmacol Toxicol 2005;96: 343-51.
173. Gross M, Kruisselbrink T, Anderson K, et al. Distribution and concordance of N-acetyltransferase genotype and phenotype in an American population. Cancer Epidemiol Biomarkers Prev 1999;8: 683-92.
174. Delomenie C, Sica L, Grant DM, et al. Genotyping of the polymorphic N-acetyltransferase (NAT2∗) gene locus in two native African populations. Pharmacogenetics 1996;6:177-85.
175. Hein DW, Fretland AJ, Doll MA. Effects of single nucleotide polymorphisms in human N-acetyltransferase 2 on metabolic activation (O-acetylation) of heterocyclic amine carcinogens. Int J Cancer 2006;119:1208-11.
176. Sabbagh A, Darlu P, Crouau-Roy B, Poloni ES. Arylamine N-acetyltransferase 2 (NAT2) genetic diversity and traditional subsistence: a worldwide population survey. PLoS One 2011;6: e18507.
177. Dandara C, Masimirembwa CM, Magimba A, et al. Arylamine N-acetyltransferase (NAT2) genotypes in Africans: the identification of a new allele with nucleotide changes 481C4T and 590G4A. Pharmacogenetics 2003;13:55-8.
178. Ebeshi BU, Bolaji OO, Masimirembwa CM. Arylamine N-acetyltransferase 2 (NAT2) single nucleotide polymorphisms' frequencies in Nigerian populations. Afr J Pharmacy Pharmacol Res 2011;1:001-6.
179. Sanderson S, Salanti G, Higgins J. Joint effects of the N-acetyltransferase 1 and 2 (NAT1 and NAT2) genes and smoking on bladder carcinogenesis: a literature-based systematic HuGE review and evidence synthesis. Am J Epidemiol 2007; 166:741-51.
180. Nöthlings U, Yamamoto JF, Wilkens LR, et al. Meat and heterocyclic amine intake, smoking, NAT1 and NAT2 polymorphisms, and colorectal cancer risk in the multiethnic cohort study. Cancer Epidemiol Biomarkers Prev 2009;18:2098-106.
181. Malik MA, Upadhyay R, Modi DR, et al. Association of NAT2 gene polymorphisms with susceptibility to esophageal and gastric cancers in the Kashmir Valley. Arch Med Res 2009;40: 416-23.
182. Jain M, Kumar S, Lal P, et al. Association of genetic polymorphisms of N-acetyltransferase 2 and susceptibility to esophageal cancer in north Indian population. Cancer Invest 2007;25:340-6.
183. Glatt H, Boeing H, Engelke CE, et al. Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. Mutat Res 2001;482:27-40.
184. Gamage N, Barnett A, Hempel N, et al. Human sulfotransferases and their role in chemical metabolism. Toxicol Sci 2006;90:5-22.
185. Lindsay J, Wang LL, Li Y, Zhou SF. Structure, function and polymorphism of human cytosolic sulfotransferases. Curr Drug Metab 2008;9:99-105.
186. Raftogianis RB, Wood TC, Weinshilboum RM. Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations. Biochem Pharmacol 1999;58:605-16.
187. Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem Biol Interact 2000;129:141-70.
188. Adjei AA, Weinshilboum RM. Catecholestrogen sulfation: possible role in carcinogenesis. Biochem Biophys Res Commun 2002; 292:402-8.
189. Coughtrie MW. Sulfation through the looking glass - recent advances in sulfotransferase research for the curious. Pharmacogenomics J 2002;2:297-308.
190. Dooley TP, Huang ZM. Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16. Biochem Biophys Res Commun 1996;228:134-40.
191. Nagar S, Walther S, Blanchard RL. Sulfotransferase (SULT) 1A1 polymorphic variants ∗1, ∗2, and ∗3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation. Mol Pharmacol 2006;69:2084-92.
192. Carlini EJ, Raftogianis RB, Wood TC, et al. Sulfation pharmacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian, Chinese and African-American subjects. Pharmacogenetics 2001;11:57-68.
193. Kotnis A, Kannan S, Sarin R, Mulherkar R. Case-control study and meta-analysis of SULT1A1 Arg213His polymorphism for gene, ethnicity and environment interaction for cancer risk. Br J Cancer 2008;99:1340-7.
194. Li K, Ren YW, Wan Y, et al. SULT1A1 Arg213His polymorphism and susceptibility of environment-related cancers: a meta analysis of 5,915 cases and 7,900 controls. Mol Biol Rep 2012;39: 2597-605.
195. Wu MT, Wang YT, Ho CK, et al. SULT1A1 polymorphism and esophageal cancer in males. Int J Cancer 2003;103:101-4.
196. Bock KW, Köhle C. UDP-glucuronosyltransferase 1A6: structural, functional, and regulatory aspects. Methods Enzymol 2005;400: 57-75.
197. Daly AK. Pharmacogenetics of the major polymorphic metabolizing enzymes. Fundam Clin Pharmacol 2003;17:27-41.
198. Mackenzie PI, Bock KW, Burchell B, et al. Nomenclature update for the mammalian UDP glycosyltransferase (UGT) gene superfamily. Pharmacogenet Genomics 2005;15:677-85.
199. Burchell B, Lockley DJ, Staines A, et al. Substrate specificity of human hepatic udp-glucuronosyltransferases. Methods Enzymol 2005;400:46-57.
200. Strassburg CP, Strassburg A, Nguyen N, et al. Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus. Biochem J 1999; 338:489-98.
201. Gong QH, Cho JW, Huang T, et al. Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics 2001;11:357-68.
202. Miners JO, McKinnon RA, Mackenzie PI. Genetic polymorphisms of UDP-glucuronosyltransferases and their functional significance. Toxicology 2002;181-2:453-6.
203. Bajro MH, Josifovski T, Panovski M, et al. Promoter length polymorphism in UGT1A1 and the risk of sporadic colorectal cancer. Cancer Genet 2012;205:163-7.
204. Guillemette C, Millikan RC, Newman B, Housman DE. Genetic polymorphisms in uridine diphospho-glucuronosyltransferase 1A1 and association with breast cancer among African Americans. Cancer Res 2000;60:950-6.
205. Adegoke OJ, Shu XO, Gao YT, et al. Genetic polymorphisms in uridine diphospho-glucuronosyltransferase 1A1 (UGT1A1) and risk of breast cancer. Breast Cancer Res Treat 2004;85:239-45.
206. Han SX, Wang L, Wu DQ. The association between UGT1A7 polymorphism and cancer risk: a meta-analysis. Cancer Epidemiol 2012;36:e201-6.
207. Lacko M, Roelofs HM, Te Morsche RH, et al. Genetic polymorphism in the conjugating enzyme UGT1A1 and the risk of head and neck cancer. Int J Cancer 2010;127:2815-21.
208. Chan AT, Tranah GJ, Giovannucci EL, et al. Genetic variants in the UGT1A6 enzyme, aspirin use, and the risk of colorectal adenoma. J Natl Cancer Inst 2005;97:457-60.
209. Angstadt AY, Hartman TJ, Lesko SM, et al. The effect of UGT1A and UGT2B polymorphisms on colorectal cancer risk: haplotype associations and gene-environment interactions. Genes Chromosomes Cancer 2014;53:454-66.
210. Dura P, Salomon J, Te Morsche RH, et al. High enzyme activity UGT1A1 or low activity UGT1A8 and UGT2B4 genotypes increase esophageal cancer risk. Int J Oncol 2012;40: 1789-96.
211. Tanaka M, Fukui M, Tomiyasu K, et al. Low serum bilirubin concentration is associated with coronary artery calcification (CAC). Atherosclerosis 2009;206:287-91.
212. Hindorff LA, Sethupathy P, Junkins HA, et al. Potential etiologic and functional implications of genome-wide association loci for human diseases and traits. Proc Natl Acad Sci USA 2009;106: 9362-7.
213. Cui R, Kamatani Y, Takahashi A, et al. Functional variants in ADH1B and ALDH2 coupled with alcohol and smoking synergistically enhance esophageal cancer risk. Gastroenterology 2009; 137:1768-75.
214. Wu C, Hu Z, He Z, et al. Genome-wide association study identifies three new susceptibility loci for esophageal squamous-cell carcinoma in Chinese populations. Nat Genet 2011;43:679-84.
215. Wu C, Kraft P, Zhai K, et al. Genome-wide association analyses of esophageal squamous cell carcinoma in Chinese identify multiple susceptibility loci and gene-environment interactions. Nat Genet 2012;44:1090-7; corrected after print 27 August 2014.
216. McKay JD, Truong T, Gaborieau V, et al. A genome-wide association study of upper aerodigestive tract cancers conducted within the INHANCE consortium. PLoS Genet 2011;7:e1001333.
217. Teo YY, Small KS, Kwiatkowski DP. Methodological challenges of genome-wide association analysis in Africa. Nat Rev Genet 2010;11:149-60.
218. McEvoy BP, Powell JE, Goddard ME, Visscher PM. Human population dispersal "Out of Africa" estimated from linkage disequilibrium and allele frequencies of SNPs. Genome Res 2011; 21:821-9.
219. Manolio TA, Collins FS, Cox NJ, et al. Finding the missing heritability of complex diseases. Nature 2009;461:747-53.
220. Matimba A, Del-Favero J, Van Broeckhoven C, Masimirembwa C. Novel variants of major drug-metabolising enzyme genes in diverse African populations and their predicted functional effects. Hum Genomics 2009;3:169-90.
221. Zhang L, Jiang Y, Wu Q, et al. Gene-environment interactions on the risk of esophageal cancer among Asian populations with the G48A polymorphism in the alcohol dehydrogenase-2 gene: a meta-analysis. Tumour Biol 2014;35:4705-17.
222. Lewis SJ, Smith GD. Alcohol, ALDH2, and esophageal cancer: a meta-analysis which illustrates the potentials and limitations of a Mendelian randomization approach. Cancer Epidemiol Biomarkers Prev 2005;14:1967-71.
223. Brooks PJ, Enoch MA, Goldman D, et al. The alcohol flushing response: an unrecognized risk factor for esophageal cancer from alcohol consumption. PLoS Med 2009;6:e50.
224. Ginsberg G, Smolenski S, Neafsey P, et al. The influence of genetic polymorphisms on population variability in six xenobiotic metabolizing enzymes. J Toxicol Environ Health B Crit Rev 2009; 12:307-33.
225. Shimada T. Xenobiotic-metabolizing enzymes involved in activation and detoxification of carcinogenic polycyclic aromatic hydrocarbons. Drug Metab Pharmacokinet 2006;21: 257-76.
226. García-Martín E. Interethnic and intraethnic variability of NAT2 single nucleotide polymorphisms. Curr Drug Metab 2008;9: 487-97.
227. Reich DE, Goldstein DB. Detecting association in a case-control study while allowing for population stratification. Genet Epidemiol 2001;20:4-16.
228. Wu C, Kraft P, Zhai K, et al. Corrigendum: genome-wide association analyses of esophageal squamous cell carcinoma in Chinese identify multiple susceptibility loci and gene environment interactions. Nat Genet 2014;44:1040-1.
229. Wang LD, Zhou FY, Li XM, et al. Corrigendum: genome-wide association study of esophageal squamous cell carcinoma in Chinese subjects identifies susceptibility loci at PLCE1 and C20orf54. Nat Genet 2010;42:759-63; published online 9 September 2012; corrected after print 27 August 2014.