Tissue expression and genomic sequences of Rat N-acetyltransferases rNat1, rNat2, rNat3, and functional characterization of a novel rNat3*2 genetic variant

Toxicological Sciences

Volumn 99, Issue 2, 2007, Pages 413-421

  Walraven, Jason M ^a   Barker, David F ^a   Doll, Mark A ^a   Hein, David W ^a  

^a University of Louisville School of Medicine   (United States)

Author keywords

Expression; N acetyltransferase; Rat; rNat3; Tissue specific

Indexed keywords

ACYLTRANSFERASE; ARYLAMINE ACETYLTRANSFERASE; MESSENGER RNA; PROTEIN NAT1; PROTEIN NAT3; ISOENZYME; N ACETYLTRANSFERASE 1; N-ACETYLTRANSFERASE 1; UNCLASSIFIED DRUG;

ACETYLATION; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; COLON; CONTROLLED STUDY; DUODENUM; ENZYME ACTIVITY; GENE EXPRESSION; GENE SEQUENCE; GENETIC VARIABILITY; ILEUM; JEJUNUM; LIVER; LUNG; MALE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PHENOTYPE; PROSTATE; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; QUANTITATIVE ANALYSIS; RAT; RECOMBINANT GENE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SINGLE NUCLEOTIDE POLYMORPHISM; SPLEEN; STRAIN DIFFERENCE; TISSUE SPECIFICITY; ANIMAL; ANTIBODY SPECIFICITY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; FISCHER 344 RAT; GENETICS; METABOLISM; MOLECULAR GENETICS;

RATTUS;

ANIMALS; ARYLAMINE N-ACETYLTRANSFERASE; BASE SEQUENCE; ENZYME STABILITY; ISOENZYMES; MALE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; ORGAN SPECIFICITY; RATS; RATS, INBRED F344; VARIATION (GENETICS);

EID: 38449091987     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfm159     Document Type: Article

References (35)

1. Barker, D. F., Husain, A., Neale, J. R., Martini, B. D., Zhang, X., Doll, M. A., States, J. C., and Hein, D. W. (2006). Functional properties of an alternative, tissue-specific promoter for human arylamine N-acetyltransferase 1. Pharmacogenet. Genomics 16, 515-525.
2. Boukouvala, S., and Fakis, G. (2005). Arylamine N-acetyltransferases: What we learn from genes and genomes. Drug Metab. Rev. 37, 511-564.
3. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
4. Canzian, F. (1997). Phylogenetics of the laboratory rat Rattus norvegicus. Genome Res. 7, 262-267.
5. Chung, C. T., Niemela, S. L., and Miller, R. H. (1989). One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution. Proc. Natl. Sci. U.S.A. 86, 2172-2175.
6. Doll, M. A., and Hein, D. W. (1995). Cloning, sequencing, and expression of NAT1 and NAT2 encoding genes from rapid and slow acetylator inbred rats. Pharmacogenetics 5, 247-251.
7. Drummond, G. S., Kelker, H. C., and Weber, W. W. (1980). N-acetylation of drugs. Observations on the properties of partially purified N-acetyltransferase from peripheral blood of rabbit. Biochem. J. 187, 157-162.
8. Ebisawa, T., Sasaki, Y., and Deguchi, T. (1995). Complementary DNAs for two arylamine N-acetyltransferases with identical 5′ non-coding regions from rat pineal gland. Eur. J. Biochem. 228, 129-137.
9. Flecknell, P. (1996). Anaesthesia and analgesia for rodents and rabbits. In Handbook of Rodent and Rabbit Medicine (K. Laber-Laird, M. M. Swindle, and P. Flecknell, Eds.), pp. 225-227. Elsevier Science, New York.
10. Gollamudi, R., Muniraju, B., and Schreiber, E. C. (1980). N-acetyltransferases of rat liver and blood: Substrate specificities. Enzyme 25, 309-315.
11. Hanna, P. E. (1996). Metabolic activation and detoxification of arylamines. Curr. Med. Chem. 3, 195-210.
12. Hein, D. W. (1988). Acetylator genotype and arylamine-induced carcinogenesis. Biochim. Biophys. Acta 948, 37-66.
13. Hein, D. W., Doll, M. A., Fretland, A. J., Leff, M. A., Webb, S. J., Xiao, G. H., Devanaboyina, U. S., Nangju, N. A., and Feng, Y. (2000). Molecular genetics and epidemiology of the NAT1 and NAT2 acetylation polymorphisms. Cancer Epidemiol. Biomarkers Prev. 9, 29-42.
14. Hein, D. W., Doll, M. A., Nerland, D. E., and Fretland, A. J. (2006). Tissue distribution of N-acetyltransferase 1 and 2 catalyzing the N-acetyltation of 4-aminobiphenyl and O-acetylation of N-hydroxy-4-aminobiphenyl in the congenic rapid and slow acetylator Syrian hamster. Mol. Carcinog. 45, 230-238.
15. Hein, D. W., Fretland, A. J., and Doll, M. A. (2006). Effects of single nucleotide polymorphisms in human N-acetyltransferase 2 on metabolic activation (O-acetylation) of hetereocyclic amine carcinogens. Int. J. Cancer 119, 1208-1211.
16. Hein, D. W., Kirlin, W. G., Ferguson, R. J., Thompson, L. K., and Ogolla, F. (1986). Identification and inheritance of inbred hamster N-acetyltransferase isozymes in peripheral blood. J. Pharmacol. Exp. Ther. 239, 823-828.
17. Husain, A., Zhang, X., Doll, M. A., States, J. C., Barker, D. F., and Hein, D. W. (2007). Identification of N-acetyltransferase 2 (NAT2) transcription start sites and quantification of NAT2-specific mRNA in human tissues. Drug. Metab. Dispos. 35, 721-727.
18. Jacob, H. J. (1999). Functional genomics and rat models. Genome Res. 9, 1013-1016.
19. Kent, W. J. (2002). BLAT-the BLAST-like alignment tool. Genome Res. 12, 656-664.
20. Krebs, H. A., and Henseleit, K. (1932). Untersuchungen über die harnstoffbildung im tierkorper. Hoppe-Seylers Z. Physiol. Chem. 210, 33-66.
21. Land, S. J., Jones, R. F., and King, C. M. (1996). Genetic analysis of two rat acetyltransferases. Carcinogenesis 17, 1121-1126.
22. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
23. Lazar, J., Moreno, C., Jacob, H. J., and Kwitek, A. E. (2005). Impact of genomics on research in the rat. Genome Res. 15, 1717-1728.
24. Lindsay, R. M., and Baty, J. D. (1988). Inter-individual variation of human blood N-acetyltransferase activity in vitro. Biochem. Pharmacol. 37, 3915-3921.
25. Loehle, J. A., Cornish, V., Wakefield, L., Doll, M. A., Neale, J. R., Zang, Y., Sim, E., and Hein, D. W. (2006). N-acetyltransferase (Nat) 1 and 2 expression in Nat2 knockout mice. J. Pharmacol. Exp. Ther. 319, 724-728.
26. Mattano, S. S., and Weber, W. W. (1987). Kinetics of arylamine Nacetyltransferase in tissues from rapid and slow acetylator mice. Carcinogenesis 8, 133-137.
27. Payton, M., Mushtaq, A., Yu, T.-W., Wu, L.-J., Sinclair, J., and Sim, E. (2001). Eubacterial arylamine N-acetyltransferase identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine, and aspartate residues. Microbiology 147, 1137-1147.
28. Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., and Ferrin, T. E. (2004). UCSF Chimera - A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612.
29. Rat Genome Sequence Project Consortium. (2004). Genome sequence of the Brown Norway rat yields insights into mammalian evolution. Nature 428, 439-521.
30. Sali, A., and Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
31. Sippl, M. J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362.
32. Sugamori, K. S., Brenneman, D., Wong, S., Gaedigk, A., Yu, V., Abramovici, H., Rozmahel, R., and Grant, D. M. (2007). Effect of arylamine acetyltransferase Nat3 gene knockout on N-acetylation in the mouse. Drug Metab. Dispos. 35, 1064-1070.
33. Sugamori, K. S., Wong, S., Gaedigk, A., Yu, V., Abramovici, H., Rozmahel, R., and Grant, D. M. (2003). Generation and functional characterization of arylamine N-acetyltransferase Nat1/Nat2 doubleknockout mice. Mol. Pharmacol. 64, 170-179.
34. Walraven, J. M., Doll, M. A., and Hein, D. W. (2006). Identification and characterization of functional rat arylamine N-acetyltransferase 3: Comparisons with rat arylamine N-acetyltransferases 1 and 2. J. Pharmacol. Exp. Ther. 319, 369-375.
35. Zang, Y., Zhao, S., Doll, M. A., States, J. C., and Hein, D. W. (2004). The T341C (Ile114Thr) polymorphism of N-acetyltransferase 2 yields slow acetylator phenotype by enhanced protein degradation. Pharmacogenetics 14, 717-723.