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Chemical Compound Review

N-hydroxy-PHIP     N-(9-methyl-3-phenyl-5,7,9...

Synonyms: N-Hydroxy phip, AGN-PC-0053MZ, CCRIS 4107, AG-D-52243, CHEMBL1743302, ...
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Disease relevance of CCRIS 4107

  • This divergent behavior of PhIP and N-hydroxy-PhIP in Salmonella may also be a key to the understanding of several 'unusual' properties of PhIP in mammalian cells and organisms [1].

High impact information on CCRIS 4107

  • The presence of the glucuronide conjugate of N-hydroxy-PhIP in the urine of pups and the lack of detectable conjugate or N-hydroxylamine itself in breast milk suggest that PhIP from breast milk undergoes metabolic activation via N-hydroxylation in 5-day-old rat pups [2].
  • The current study examines the expression and catalytic activity of NAT toward the N-hydroxy-HCAs 2-hydroxyamino-1-methyl-6-phenylimidazo[4,5-b]pyridine (N-hydroxy-PhIP) and 2-hydroxy-amino-3-methylimidazo[4,5-f]quinoline (N-hydroxy-IQ) in the human mammary gland [3].
  • The formation of DNA adducts and metabolites from colon slices exposed to N-hydroxy-PhIP but not PhIP implies that there is insufficient P450 activity in the rat colon to activate PhIP to hydroxylated metabolites, suggesting that the rat colon is a site of Phase II metabolism for PhIP and that the liver is the primary source for hydroxylation [4].
  • In addition, liver microsomes, unlike intestinal microsomes, were able to convert PhIP to the proximate mutagen N-hydroxy-PhIP [5].
  • These results indicate that UGT1A-mediated glucuronidation of PhIP and N-hydroxy-PhIP is an important pathway for PhIP detoxification, and demonstrate the importance of tissue-specific metabolism [6].

Biological context of CCRIS 4107

  • Only N-hydroxy-PhIP (at 10 and 50 microM), however, was cytotoxic as assessed by the MTT cell survival assay (which measures the capacity of mitochondria to metabolize a tetrazolium salt) [7].
  • The plasmids were treated in vitro with 0, 5, 10, or 40 microM N-hydroxy-IQ or N-hydroxy-PhIP in the presence of a 10-fold molar excess of acetic anhydride to generate the N-acetoxy derivatives in situ [8].
  • To examine if PhIP and its reactive metabolite N-hydroxy-PhIP inhibit apoptosis in human mammary epithelial MCF-10A cells, confluent cultures deprived of serum and growth factors were incubated for 24 h with either compound [9].
  • Following N-hydroxylation, N-acetyltransferases catalyze the O-acetylation (activation) of N-hydroxy-PhIP to an electrophile causing DNA damage [10].
  • N-hydroxy-PhIP O-sulfotransferase activities did not vary with acetylator genotype [11].

Anatomical context of CCRIS 4107


Associations of CCRIS 4107 with other chemical compounds


Gene context of CCRIS 4107


Analytical, diagnostic and therapeutic context of CCRIS 4107


  1. Azido- and nitro-PhIP, relatives of the heterocyclic arylamine and food mutagen PhIP--mechanism of their mutagenicity in Salmonella. Wild, D., Watkins, B.E., Vanderlaan, M. Carcinogenesis (1991) [Pubmed]
  2. Metabolism of the food-derived carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by lactating Fischer 344 rats and their nursing pups. Davis, C.D., Ghoshal, A., Schut, H.A., Snyderwine, E.G. J. Natl. Cancer Inst. (1994) [Pubmed]
  3. N-acetyltransferase expression and metabolic activation of the food-derived heterocyclic amines in the human mammary gland. Sadrieh, N., Davis, C.D., Snyderwine, E.G. Cancer Res. (1996) [Pubmed]
  4. The capability of rat colon tissue slices to metabolize the cooked-food carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine. Malfatti, M.A., Connors, M.S., Mauthe, R.J., Felton, J.S. Cancer Res. (1996) [Pubmed]
  5. 2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine is a potent mutagen in the mouse small intestine. Brooks, R.A., Gooderham, N.J., Zhao, K., Edwards, R.J., Howard, L.A., Boobis, A.R., Winton, D.J. Cancer Res. (1994) [Pubmed]
  6. The impact of glucuronidation on the bioactivation and DNA adduction of the cooked-food carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine in vivo. Malfatti, M.A., Ubick, E.A., Felton, J.S. Carcinogenesis (2005) [Pubmed]
  7. Cytotoxicity, DNA adduct formation and DNA repair induced by 2-hydroxyamino-3-methylimidazo[4,5-f]quinoline and 2-hydroxyamino-1-methyl-6-phenylimidazo[4,5-b]pyridine in cultured human mammary epithelial cells. Fan, L., Schut, H.A., Snyderwine, E.G. Carcinogenesis (1995) [Pubmed]
  8. Inhibition of plasmid reporter gene expression in CHO cells by DNA adducts of 2-amino-3-methylimidazo[4,5-f]quinoline and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine. Fan, L., Snyderwine, E.G. Mol. Carcinog. (1994) [Pubmed]
  9. Inhibition of cell death in human mammary epithelial cells by the cooked meat-derived carcinogen 2-amino-1-methyl-6-phenylimidazo[4, 5-b]pyridine. Venugopal, M., Agarwal, R., Callaway, A., Schut, H.A., Snyderwine, E.G. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  10. Oral administration of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) yields PhIP-DNA adducts but not tumors in male Syrian hamsters congenic at the N-acetyltransferase 2 (NAT2) locus. Fretland, A.J., Devanaboyina, U.S., Feng, Y., Leff, M.A., Xiao, G.H., Webb, S.J., Hein, D.W. Toxicol. Sci. (2001) [Pubmed]
  11. Metabolic activation of 2-hydroxyamino-1-methyl-6-phenylimidazo[4,5-b]pyridine in Syrian hamsters congenic at the N-acetyltransferase 2 (NAT2) locus. Fretland, A.J., Devanaboyina, U.S., Doll, M.A., Zhao, S., Xiao, G.H., Hein, D.W. Toxicol. Sci. (2003) [Pubmed]
  12. Metabolism of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in mice. Buonarati, M.H., Roper, M., Morris, C.J., Happe, J.A., Knize, M.G., Felton, J.S. Carcinogenesis (1992) [Pubmed]
  13. Possible mechanisms for PhIP-DNA adduct formation in the mammary gland of female Sprague-Dawley rats. Ghoshal, A., Davis, C.D., Schut, H.A., Snyderwine, E.G. Carcinogenesis (1995) [Pubmed]
  14. Enzymatic phase II activation of the N-hydroxylamines of IQ, MeIQx and PhIP by various organs of monkeys and rats. Davis, C.D., Schut, H.A., Snyderwine, E.G. Carcinogenesis (1993) [Pubmed]
  15. Metabolism of the food-derived mutagen/carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in nonhuman primates. Snyderwine, E.G., Buonarati, M.H., Felton, J.S., Turteltaub, K.W. Carcinogenesis (1993) [Pubmed]
  16. Protective effect of N-acetylcysteine against heterocyclic amine-induced cardiotoxicity in cultured myocytes and in rats. Davis, C.D., Snyderwine, E.G. Food Chem. Toxicol. (1995) [Pubmed]
  17. Resveratrol modulates human mammary epithelial cell O-acetyltransferase, sulfotransferase, and kinase activation of the heterocyclic amine carcinogen N-hydroxy-PhIP. Dubuisson, J.G., Dyess, D.L., Gaubatz, J.W. Cancer Lett. (2002) [Pubmed]
  18. Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of N-hydroxy-PhIP in vitro. Malfatti, M.A., Felton, J.S. Chem. Res. Toxicol. (2004) [Pubmed]
  19. Heterologous expression of human N-acetyltransferases 1 and 2 and sulfotransferase 1A1 in Salmonella typhimurium for mutagenicity testing of heterocyclic amines. Muckel, E., Frandsen, H., Glatt, H.R. Food Chem. Toxicol. (2002) [Pubmed]
  20. Functional characterization of nucleotide polymorphisms in the coding region of N-acetyltransferase 1. Fretland, A.J., Doll, M.A., Leff, M.A., Hein, D.W. Pharmacogenetics (2001) [Pubmed]
  21. Expression of cytochromes P450 and glutathione S-transferases in human prostate, and the potential for activation of heterocyclic amine carcinogens via acetyl-coA-, PAPS- and ATP-dependent pathways. Di Paolo, O.A., Teitel, C.H., Nowell, S., Coles, B.F., Kadlubar, F.F. Int. J. Cancer (2005) [Pubmed]
  22. 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., Felton, J.S. Carcinogenesis (2001) [Pubmed]
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