The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

UGT1A7  -  UDP glucuronosyltransferase 1 family,...

Homo sapiens

Synonyms: GNT1, UDP-glucuronosyltransferase 1-7, UDP-glucuronosyltransferase 1-G, UDP-glucuronosyltransferase 1A7, UDPGT, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of UGT1A7

 

Psychiatry related information on UGT1A7

  • CONCLUSIONS: UGT1A7 polymorphisms may have a significant modifying effect on colorectal cancer risk, which may interact with environmental factors, cigarette smoking and alcohol drinking in colorectal carcinogenesis [6].
 

High impact information on UGT1A7

 

Chemical compound and disease context of UGT1A7

 

Biological context of UGT1A7

  • In summary, our results suggest gastrointestinally distributed UGT1A10 is important for detoxifying estrogens/phytoestrogens and aromatic acids with complementary activity by UGT1A7, -1A8, -1A3, and/or -1A1 evidently dependent upon phosphorylation [12].
  • We identified a novel reduced-function TATA box SNP of the UGT1A7 gene that catalyzes irinotecan metabolite detoxification [13].
  • A novel -57 T--> G SNP with a gene frequency of 0.39 in healthy blood donors was identified in the putative TATA box of the UGT1A7 gene, reducing promoter activity to 30% [13].
  • In conclusion, the data suggest that the presence of variant UGT1A6 and UGT1A7 genotypes with expected reduced enzyme activities, might enhance susceptibility to CRC [14].
  • Although several genetic polymorphisms are reported for UGT1A1 and UGT1A7 that affect the SN-38 glucuronidation activities, no such polymorphisms have been identified for UGT1A9 [15].
 

Anatomical context of UGT1A7

 

Associations of UGT1A7 with chemical compounds

 

Regulatory relationships of UGT1A7

  • METHODS: Genomic DNA from the blood of 59 patients with hepatocellular carcinoma and 70 control subjects without evidence of cancer was analyzed by UGT1A7- and UGT1A9-specific PCR, sequencing analysis, and temperature gradient gel electrophoresis [3].
  • These data provide evidence for an important stimulatory role of HNF1 in promoting UGT1A7 gene expression in rat liver [25].
 

Other interactions of UGT1A7

  • In addition, both UGT1A9 and UGT1A7 preferentially formed BPD-7R-Gluc [26].
  • UGT1A8 was found to be closely related to gastric UGT1A7 with a 93.8% identity of first exon sequences [27].
  • In rabbits, cDNAs encoding proteins homologous to human UGT1A4, UGT1A6, and UGT1A7 have previously been identified [28].
  • Its association with variants of the UGT1A1 promoter and UGT1A7 gene may influence irinotecan metabolism [13].
  • CONCLUSION: The UGT1A7 polymorphisms together with IL-1 beta were associated with the presence of HCC in Japanese HCV-infected patients [29].
 

Analytical, diagnostic and therapeutic context of UGT1A7

  • METHODS: UGT1A7 expression in normal orolaryngeal tissue was determined by semiquantitative reverse transcription-polymerase chain reaction (PCR) [7].
  • We have evaluated whether UGT1A7 allelic variations are associated with colon cancer and whether UGT1A7 genotype modified associations among meat intake, exposure to HCAs and PAHs, and colon cancer in a population-based case-control study of African Americans (197 cases and 202 controls) and whites (203 cases and 210 controls) [30].
  • All the patients had received irinotecan-containing chemotherapy and were evaluated to see whether the variant UGT1A7 genotype would increase the likelihood of severe toxicity of irinotecan consisting of grade 4 leukopenia and/or grade 3 or more diarrhea [31].
  • Quantitative immunoblotting revealed a parallel between the MPA UGT activity and the content of UGT1A7-like immunoreactivity (18.7 and 7.3 microg/mg for duodenum and colon, respectively) [32].
  • PCR and Western blots confirmed the presence and expression of UGT1 in liver [33].

References

  1. Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus. Strassburg, C.P., Strassburg, A., Nguyen, N., Li, Q., Manns, M.P., Tukey, R.H. Biochem. J. (1999) [Pubmed]
  2. Polymorphisms of uridine-diphosphoglucuronosyltransferase 1A7 gene in Taiwan Chinese. Huang, M.J., Yang, S.S., Lin, M.S., Huang, C.S. World J. Gastroenterol. (2005) [Pubmed]
  3. Genetic link of hepatocellular carcinoma with polymorphisms of the UDP-glucuronosyltransferase UGT1A7 gene. Vogel, A., Kneip, S., Barut, A., Ehmer, U., Tukey, R.H., Manns, M.P., Strassburg, C.P. Gastroenterology (2001) [Pubmed]
  4. UGT1A7 and UGT1A9 polymorphisms predict response and toxicity in colorectal cancer patients treated with capecitabine/irinotecan. Carlini, L.E., Meropol, N.J., Bever, J., Andria, M.L., Hill, T., Gold, P., Rogatko, A., Wang, H., Blanchard, R.L. Clin. Cancer Res. (2005) [Pubmed]
  5. UDP-glucuronosyltransferase 1A7 genetic polymorphisms are associated with hepatocellular carcinoma risk and onset age. Tseng, C.S., Tang, K.S., Lo, H.W., Ker, C.G., Teng, H.C., Huang, C.S. Am. J. Gastroenterol. (2005) [Pubmed]
  6. Genetic polymorphisms of the uridine diphosphate glucuronosyltransferase 1A7 and colorectal cancer risk in relation to cigarette smoking and alcohol drinking in a Chinese population. Chen, K., Jin, M., Zhu, Y., Jiang, Q., Yu, W., Ma, X., Yao, K. J. Gastroenterol. Hepatol. (2006) [Pubmed]
  7. Tobacco carcinogen-detoxifying enzyme UGT1A7 and its association with orolaryngeal cancer risk. Zheng, Z., Park, J.Y., Guillemette, C., Schantz, S.P., Lazarus, P. J. Natl. Cancer Inst. (2001) [Pubmed]
  8. UDP glucuronosyltransferase (UGT1A7) gene polymorphisms increase the risk of chronic pancreatitis and pancreatic cancer. Ockenga, J., Vogel, A., Teich, N., Keim, V., Manns, M.P., Strassburg, C.P. Gastroenterology (2003) [Pubmed]
  9. Comprehensive analysis of UGT1A polymorphisms predictive for pharmacokinetics and treatment outcome in patients with non-small-cell lung cancer treated with irinotecan and cisplatin. Han, J.Y., Lim, H.S., Shin, E.S., Yoo, Y.K., Park, Y.H., Lee, J.E., Jang, I.J., Lee, D.H., Lee, J.S. J. Clin. Oncol. (2006) [Pubmed]
  10. Molecular analysis of patients of Sardinian descent with Crigler-Najjar syndrome type I. Rosatelli, M.C., Meloni, A., Faa, V., Saba, L., Crisponi, G., Clemente, M.G., Meloni, G., Piga, M.T., Cao, A. J. Med. Genet. (1997) [Pubmed]
  11. Regulation of the human bilirubin UDP-glucuronosyltransferase gene. Brierley, C.H., Senafi, S.B., Clarke, D., Hsu, M.H., Johnson, E.F., Burchell, B. Adv. Enzyme Regul. (1996) [Pubmed]
  12. Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteroidal anti-inflammatory drugs, depends upon phosphorylation. Basu, N.K., Kubota, S., Meselhy, M.R., Ciotti, M., Chowdhury, B., Hartori, M., Owens, I.S. J. Biol. Chem. (2004) [Pubmed]
  13. Identification and characterization of a functional TATA box polymorphism of the UDP glucuronosyltransferase 1A7 gene. Lankisch, T.O., Vogel, A., Eilermann, S., Fiebeler, A., Krone, B., Barut, A., Manns, M.P., Strassburg, C.P. Mol. Pharmacol. (2005) [Pubmed]
  14. Genetic polymorphisms in UDP-glucuronosyltransferases and glutathione S-transferases and colorectal cancer risk. van der Logt, E.M., Bergevoet, S.M., Roelofs, H.M., van Hooijdonk, Z., te Morsche, R.H., Wobbes, T., de Kok, J.B., Nagengast, F.M., Peters, W.H. Carcinogenesis (2004) [Pubmed]
  15. Functional characterization of human UDP-glucuronosyltransferase 1A9 variant, D256N, found in Japanese cancer patients. Jinno, H., Saeki, M., Saito, Y., Tanaka-Kagawa, T., Hanioka, N., Sai, K., Kaniwa, N., Ando, M., Shirao, K., Minami, H., Ohtsu, A., Yoshida, T., Saijo, N., Ozawa, S., Sawada, J. J. Pharmacol. Exp. Ther. (2003) [Pubmed]
  16. Polymorphic expression of the UDP-glucuronosyltransferase UGT1A gene locus in human gastric epithelium. Strassburg, C.P., Nguyen, N., Manns, M.P., Tukey, R.H. Mol. Pharmacol. (1998) [Pubmed]
  17. Amino acid residue ILE211 is essential for the enzymatic activity of human UDP-glucuronosyltransferase 1A10 (UGT1A10). Martineau, I., Tchernof, A., Bélanger, A. Drug Metab. Dispos. (2004) [Pubmed]
  18. Glucuronidation: an important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues. Zheng, Z., Fang, J.L., Lazarus, P. Drug Metab. Dispos. (2002) [Pubmed]
  19. Regulation of UDP glucuronosyltransferases in the gastrointestinal tract. Gregory, P.A., Lewinsky, R.H., Gardner-Stephen, D.A., Mackenzie, P.I. Toxicol. Appl. Pharmacol. (2004) [Pubmed]
  20. Characterization of rabbit UDP-glucuronosyltransferase UGT1A7: tertiary amine glucuronidation is catalyzed by UGT1A7 and UGT1A4. Bruck, M., Li, Q., Lamb, J.G., Tukey, R.H. Arch. Biochem. Biophys. (1997) [Pubmed]
  21. UDP-glucuronosyltransferase 1A6: structural, functional, and regulatory aspects. Bock, K.W., Köhle, C. Meth. Enzymol. (2005) [Pubmed]
  22. Novel functional polymorphisms in the UGT1A7 and UGT1A9 glucuronidating enzymes in Caucasian and African-American subjects and their impact on the metabolism of 7-ethyl-10-hydroxycamptothecin and flavopiridol anticancer drugs. Villeneuve, L., Girard, H., Fortier, L.C., Gagné, J.F., Guillemette, C. J. Pharmacol. Exp. Ther. (2003) [Pubmed]
  23. Glucuronidation of 1-hydroxypyrene by human liver microsomes and human UDP-glucuronosyltransferases UGT1A6, UGT1A7, and UGT1A9: development of a high-sensitivity glucuronidation assay for human tissue. Luukkanen, L., Mikkola, J., Forsman, T., Taavitsainen, P., Taskinen, J., Elovaara, E. Drug Metab. Dispos. (2001) [Pubmed]
  24. Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity. Basu, N.K., Kovarova, M., Garza, A., Kubota, S., Saha, T., Mitra, P.S., Banerjee, R., Rivera, J., Owens, I.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  25. Involvement of hepatocyte nuclear factor 1 in the regulation of the UDP-glucuronosyltransferase 1A7 (UGT1A7) gene in rat hepatocytes. Metz, R.P., Auyeung, D.J., Kessler, F.K., Ritter, J.K. Mol. Pharmacol. (2000) [Pubmed]
  26. Characterization of benzo(a)pyrene-trans-7,8-dihydrodiol glucuronidation by human tissue microsomes and overexpressed UDP-glucuronosyltransferase enzymes. Fang, J.L., Beland, F.A., Doerge, D.R., Wiener, D., Guillemette, C., Marques, M.M., Lazarus, P. Cancer Res. (2002) [Pubmed]
  27. Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8. Strassburg, C.P., Manns, M.P., Tukey, R.H. J. Biol. Chem. (1998) [Pubmed]
  28. Characterization of the UDP-glucuronosyltransferase 1A locus in lagomorphs: evidence for duplication of the UGT1A6 gene. Li, Q., Lamb, G., Tukey, R.H. Mol. Pharmacol. (2000) [Pubmed]
  29. UDP-glucuronosyltransferase 1A7 genetic polymorphisms are associated with hepatocellular carcinoma in japanese patients with hepatitis C virus infection. Wang, Y., Kato, N., Hoshida, Y., Otsuka, M., Taniguchi, H., Moriyama, M., Shiina, S., Kawabe, T., Ito, Y.M., Omata, M. Clin. Cancer Res. (2004) [Pubmed]
  30. Joint effects between UDP-glucuronosyltransferase 1A7 genotype and dietary carcinogen exposure on risk of colon cancer. Butler, L.M., Duguay, Y., Millikan, R.C., Sinha, R., Gagné, J.F., Sandler, R.S., Guillemette, C. Cancer Epidemiol. Biomarkers Prev. (2005) [Pubmed]
  31. Genetic polymorphisms of the UDP-glucuronosyltransferase 1A7 gene and irinotecan toxicity in Japanese cancer patients. Ando, M., Ando, Y., Sekido, Y., Ando, M., Shimokata, K., Hasegawa, Y. Jpn. J. Cancer Res. (2002) [Pubmed]
  32. Characterization of rat intestinal microsomal UDP-glucuronosyltransferase activity toward mycophenolic acid. Miles, K.K., Kessler, F.K., Smith, P.C., Ritter, J.K. Drug Metab. Dispos. (2006) [Pubmed]
  33. Therapeutic lentivirus-mediated neonatal in vivo gene therapy in hyperbilirubinemic Gunn rats. Nguyen, T.H., Bellodi-Privato, M., Aubert, D., Pichard, V., Myara, A., Trono, D., Ferry, N. Mol. Ther. (2005) [Pubmed]
 
WikiGenes - Universities