메뉴 건너뛰기




Volumn 28, Issue 11, 2007, Pages 2412-2418

Glucuronidation of PhIP and N-OH-PhIP by UDP-glucuronosyltransferase 1A10

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 1 METHYL 6 PHENYLIMIDAZO[4,5 B]PYRIDINE; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A10; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A9; HETEROCYCLIC AMINE; LYSINE; POLYCYCLIC AROMATIC HYDROCARBON;

EID: 35549008096     PISSN: 01433334     EISSN: 14602180     Source Type: Journal    
DOI: 10.1093/carcin/bgm164     Document Type: Article
Times cited : (53)

References (28)
  • 1
    • 0023017251 scopus 로고
    • The isolation and identification of a new mutagen from fried ground beef: 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP)
    • Felton,J.S. et al. (1986) The isolation and identification of a new mutagen from fried ground beef: 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP). Carcinogenesis, 7, 1081-1086.
    • (1986) Carcinogenesis , vol.7 , pp. 1081-1086
    • Felton, J.S.1
  • 2
    • 0031657862 scopus 로고    scopus 로고
    • Carcinogenic heterocyclic amines in model systems and cooked food: A review on formation, occurrence and intake
    • Skog,K.I. et al. (1999) Carcinogenic heterocyclic amines in model systems and cooked food: A review on formation, occurrence and intake. Food Chem. Toxicol., 36, 879-896.
    • (1999) Food Chem. Toxicol , vol.36 , pp. 879-896
    • Skog, K.I.1
  • 3
    • 0025986958 scopus 로고
    • Detection of a carcinogen, 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine (PhIP), in cigarette smoke condensate
    • Manabe,S. et al. (1991) Detection of a carcinogen, 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine (PhIP), in cigarette smoke condensate. Carcinogenesis, 12, 1945-1947.
    • (1991) Carcinogenesis , vol.12 , pp. 1945-1947
    • Manabe, S.1
  • 4
    • 28444478039 scopus 로고    scopus 로고
    • Modeling human colon cancer in rodents using a food-borne carcinogen, PhIP
    • Nakagama,H. et al. (2005) Modeling human colon cancer in rodents using a food-borne carcinogen, PhIP. Cancer Sci., 96, 627-636.
    • (2005) Cancer Sci , vol.96 , pp. 627-636
    • Nakagama, H.1
  • 5
    • 0034942927 scopus 로고    scopus 로고
    • N-Glucuronidation of 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine (PhIP) and N hydroxy-PhIP by specific human UDP-glucuronosyltransferases
    • Malfatti,M.A. et al. (2001) N-Glucuronidation of 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine (PhIP) and N hydroxy-PhIP by specific human UDP-glucuronosyltransferases. Carcinogenesis, 22, 1087-1093.
    • (2001) Carcinogenesis , vol.22 , pp. 1087-1093
    • Malfatti, M.A.1
  • 6
    • 23044471764 scopus 로고    scopus 로고
    • UGT1A1 polymorphisms are important determinants of dietary detoxilication in the liver
    • Girard,H. et al. (2005) UGT1A1 polymorphisms are important determinants of dietary detoxilication in the liver. Hepatology, 42, 448-457.
    • (2005) Hepatology , vol.42 , pp. 448-457
    • Girard, H.1
  • 7
    • 33751357589 scopus 로고    scopus 로고
    • The urinary metabolite profile of the dietary carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine is predictive of colon DNA adducts after low-dose exposure to humans
    • Malfatti,M.A. et al. (2006) The urinary metabolite profile of the dietary carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine is predictive of colon DNA adducts after low-dose exposure to humans. Cancer Res., 66, 10541-10547.
    • (2006) Cancer Res , vol.66 , pp. 10541-10547
    • Malfatti, M.A.1
  • 8
    • 0025284207 scopus 로고
    • UDP-glucuronosyltransferases: A family of detoxifying enzymes
    • Tephly,T.R. et al. (1990) UDP-glucuronosyltransferases: A family of detoxifying enzymes. Trends Pharmacol. Sci., 11, 276-279.
    • (1990) Trends Pharmacol. Sci , vol.11 , pp. 276-279
    • Tephly, T.R.1
  • 9
    • 0028833732 scopus 로고
    • Gene structure at the human UGTI locus creates diversity in isozyme structure, substrate specificity, and regulation
    • Owens,I.S. et al. (1995) Gene structure at the human UGTI locus creates diversity in isozyme structure, substrate specificity, and regulation. Prog. Nucleic Acid Res. Mol. Biol., 51, 305-338.
    • (1995) Prog. Nucleic Acid Res. Mol. Biol , vol.51 , pp. 305-338
    • Owens, I.S.1
  • 10
    • 0032211978 scopus 로고    scopus 로고
    • Glucuronidation: A dual control
    • Gueraud,F. et al. (1998) Glucuronidation: A dual control. Gen. Pharmacol., 31, 683-688.
    • (1998) Gen. Pharmacol , vol.31 , pp. 683-688
    • Gueraud, F.1
  • 11
    • 0033783035 scopus 로고    scopus 로고
    • O-Glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by human UDP-glucuronosyltransferases 2B7 and 1A9
    • Ren,Q. et al. (2000) O-Glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by human UDP-glucuronosyltransferases 2B7 and 1A9. Drug Metab. Dispos., 28, 1352-1360.
    • (2000) Drug Metab. Dispos , vol.28 , pp. 1352-1360
    • Ren, Q.1
  • 12
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • Tukey,R.H. et al. (2000) Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu. Rev. Pharmacol. Toxicol. 40 581-616.
    • (2000) Annu. Rev. Pharmacol. Toxicol , vol.40 , pp. 581-616
    • Tukey, R.H.1
  • 13
    • 33645120407 scopus 로고    scopus 로고
    • Uridine diphosphoglucuronosyltranferase pharmacogenetics and cancer
    • Nagar,S. et al. (2006) Uridine diphosphoglucuronosyltranferase pharmacogenetics and cancer. Oncogene., 25, 1659-1672.
    • (2006) Oncogene , vol.25 , pp. 1659-1672
    • Nagar, S.1
  • 14
    • 0027433317 scopus 로고
    • Complementary deoxyribonucleic acid cloning and expression of a human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs
    • Jin,C.J. et al. (1993) Complementary deoxyribonucleic acid cloning and expression of a human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs. J. Pharmacol. Exp. Ther., 264, 475-479.
    • (1993) J. Pharmacol. Exp. Ther , vol.264 , pp. 475-479
    • Jin, C.J.1
  • 15
    • 0030669869 scopus 로고    scopus 로고
    • Chromosomal localization, structure, and regulation of the UGT2B17 gene, encoding a C19 steroid metabolizing enzyme
    • Beaulieu,M. et al. (1997) Chromosomal localization, structure, and regulation of the UGT2B17 gene, encoding a C19 steroid metabolizing enzyme. DNA Cell Biol., 16, 1143-1154.
    • (1997) DNA Cell Biol , vol.16 , pp. 1143-1154
    • Beaulieu, M.1
  • 16
    • 4243182634 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of N hydroxy-PhIP in vitro
    • Malfatti,M.A. et al. (2004) Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of N hydroxy-PhIP in vitro. Chem. Res. Toxicol., 17, 1137-1144.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 1137-1144
    • Malfatti, M.A.1
  • 17
    • 0033747658 scopus 로고    scopus 로고
    • Identification of urine metabolites of 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine following consumption of a single cooked chicken meal in humans
    • Kulp,K.S. et al. (2000) Identification of urine metabolites of 2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine following consumption of a single cooked chicken meal in humans. Carcinogenesis, 21 2065-2072.
    • (2000) Carcinogenesis , vol.21 , pp. 2065-2072
    • Kulp, K.S.1
  • 18
    • 1642457368 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferase 1A4: N glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL)
    • Wiener,D. et al. (2004) UDP-glucuronosyltransferase 1A4: N glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL). Drug Metab. Dispos., 32, 72-79.
    • (2004) Drug Metab. Dispos , vol.32 , pp. 72-79
    • Wiener, D.1
  • 19
    • 33646804138 scopus 로고    scopus 로고
    • 139Lys, isoform. Drug Metab. Dispos., 34, 943-949.
    • 139Lys, isoform. Drug Metab. Dispos., 34, 943-949.
  • 20
    • 33748318005 scopus 로고    scopus 로고
    • Characterization of tamoxifen and 4-hydroxytamoxifen glucuronidation by human UGT1A4 variants
    • Sun,D. et al. (2006) Characterization of tamoxifen and 4-hydroxytamoxifen glucuronidation by human UGT1A4 variants. Breast Cancer Res., 8, R50.
    • (2006) Breast Cancer Res , vol.8
    • Sun, D.1
  • 21
    • 0036532140 scopus 로고    scopus 로고
    • Characterization of benzo i a]pyrene-7,8-dihydrodiol glucuronidation by human liver microsomes and over-expressed human UDP-glucuronosytransferase enzymes
    • Fang,J.-L. et al. (2002) Characterization of benzo i a]pyrene-7,8-dihydrodiol glucuronidation by human liver microsomes and over-expressed human UDP-glucuronosytransferase enzymes. Cancer Res., 62, 1978-1986.
    • (2002) Cancer Res , vol.62 , pp. 1978-1986
    • Fang, J.-L.1
  • 22
    • 0842325733 scopus 로고    scopus 로고
    • Correlation between UDP-glucuronosyl-transferase genotypes and NNAL glucuronidation phenotype in human liver microsomes
    • Wiener,D. et al. (2004) Correlation between UDP-glucuronosyl-transferase genotypes and NNAL glucuronidation phenotype in human liver microsomes. Cancer Res., 64, 1190-1196.
    • (2004) Cancer Res , vol.64 , pp. 1190-1196
    • Wiener, D.1
  • 23
    • 0032924835 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferase activity in human liver and colon
    • Strassburg,C.P. et al. (1999) UDP-glucuronosyltransferase activity in human liver and colon. Gastroenterology, 116, 149-160.
    • (1999) Gastroenterology , vol.116 , pp. 149-160
    • Strassburg, C.P.1
  • 24
    • 0036204296 scopus 로고    scopus 로고
    • Glucuronidation: An important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues
    • Zheng,Z. et al. (2002) Glucuronidation: An important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues. Drug Metab. Dispos., 30, 397-403.
    • (2002) Drug Metab. Dispos , vol.30 , pp. 397-403
    • Zheng, Z.1
  • 25
    • 0036509528 scopus 로고    scopus 로고
    • Nuclear UDP-glucuronosyltransferases: Identification of UGT2B7 and UGT1A6 in human liver nuclear membranes
    • Radominska-Pandya,A. et al. (2002) Nuclear UDP-glucuronosyltransferases: Identification of UGT2B7 and UGT1A6 in human liver nuclear membranes. Arch Biochem. Biophys., 399, 37-48.
    • (2002) Arch Biochem. Biophys , vol.399 , pp. 37-48
    • Radominska-Pandya, A.1
  • 26
    • 0030062286 scopus 로고    scopus 로고
    • Posttranslational processing of recombinant human interferon-gamma in animal expression systems
    • James,D.C. et al. (1996) Posttranslational processing of recombinant human interferon-gamma in animal expression systems. Protein Sci., 5, 331-340.
    • (1996) Protein Sci , vol.5 , pp. 331-340
    • James, D.C.1
  • 27
    • 33744965385 scopus 로고    scopus 로고
    • Structural and functional analysis of the human Toll-like receptor 3. Role of glycosylation
    • Sun,J. et al. (2006) Structural and functional analysis of the human Toll-like receptor 3. Role of glycosylation. J. Biol. Chem., 281, 11144-11151.
    • (2006) J. Biol. Chem , vol.281 , pp. 11144-11151
    • Sun, J.1
  • 28
    • 18144393495 scopus 로고    scopus 로고
    • Phosphorylation of UDP-glucuronosyltransferase regulates substrate specificity
    • Basu,N.K. et al. (2005) Phosphorylation of UDP-glucuronosyltransferase regulates substrate specificity. Proc. Natl Acad. Sci. USA, 102, 6285-6290.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6285-6290
    • Basu, N.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.