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Gene Review

Cryz  -  crystallin, zeta (quinone reductase)

Rattus norvegicus

Synonyms: NADPH:quinone reductase, Quinone oxidoreductase, Zeta-crystallin
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Anatomical context of Cryz


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Analytical, diagnostic and therapeutic context of Cryz

  • Western blot analysis using antibodies raised against zeta-crystallin peptides demonstrated the presence of substantial amounts of this protein in human liver homogenates [17].


  1. Nicotinamide adenine dinucleotide (phosphate): quinone oxidoreductase (DT-diaphorase) as a target for bioreductive antitumor quinones: quinone cytotoxicity and selectivity in human lung and breast cancer cell lines. Beall, H.D., Murphy, A.M., Siegel, D., Hargreaves, R.H., Butler, J., Ross, D. Mol. Pharmacol. (1995) [Pubmed]
  2. Role of deadenylation and AUF1 binding in the pH-responsive stabilization of glutaminase mRNA. Schroeder, J.M., Ibrahim, H., Taylor, L., Curthoys, N.P. Am. J. Physiol. Renal Physiol. (2006) [Pubmed]
  3. Requirement for iron for the production of hydroxyl radicals by rat liver quinone reductase. Dicker, E., Cederbaum, A.I. J. Pharmacol. Exp. Ther. (1993) [Pubmed]
  4. Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver. Kelly, V.P., Ellis, E.M., Manson, M.M., Chanas, S.A., Moffat, G.J., McLeod, R., Judah, D.J., Neal, G.E., Hayes, J.D. Cancer Res. (2000) [Pubmed]
  5. Regulation of carbonyl-reducing enzymes in rat liver by chemoprotectors. Ellis, E.M., Judah, D.J., Neal, G.E., O'Connor, T., Hayes, J.D. Cancer Res. (1996) [Pubmed]
  6. pH-responsive stabilization of glutamate dehydrogenase mRNA in LLC-PK1-F+ cells. Schroeder, J.M., Liu, W., Curthoys, N.P. Am. J. Physiol. Renal Physiol. (2003) [Pubmed]
  7. A novel 4 S [3H]beta-naphthoflavone-binding protein in liver cytosol of female Sprague-Dawley rats treated with aryl hydrocarbon receptor agonists. Brauze, D., Malejka-Giganti, D. Biochem. J. (2000) [Pubmed]
  8. Hormonal influences of detoxication in the rat ovary on enzymes in comparison with the liver. Becedas, L., Bengtson Ahlberg, M. Biochem. Pharmacol. (1995) [Pubmed]
  9. Toxicogenomics of resveratrol in rat liver. Hebbar, V., Shen, G., Hu, R., Kim, B.R., Chen, C., Korytko, P.J., Crowell, J.A., Levine, B.S., Kong, A.N. Life Sci. (2005) [Pubmed]
  10. NAD(P)H: quinone oxidoreductase (DT-diaphorase) in chick embryo liver. Comparison to activity in rat and guinea pig liver and differences in co-induction with 7-ethoxyresorufin deethylase by 2,3,7,8-tetrachlorodibenzo-p-dioxin. Spencer, C.B., Rifkind, A.B. Biochem. Pharmacol. (1990) [Pubmed]
  11. Extremely high levels of NADPH in guinea pig lens: correlation with zeta-crystallin concentration. Rao, P.V., Zigler, J.S. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  12. Cytosol-mediated reduction of resorufin: a method for measuring quinone oxidoreductase. Nims, R.W., Prough, R.A., Lubet, R.A. Arch. Biochem. Biophys. (1984) [Pubmed]
  13. Coenzyme Q cytoprotective mechanisms for mitochondrial complex I cytopathies involves NAD(P)H: quinone oxidoreductase 1(NQO1). Chan, T.S., Teng, S., Wilson, J.X., Galati, G., Khan, S., O'Brien, P.J. Free Radic. Res. (2002) [Pubmed]
  14. Primaquine alters antioxidant enzyme profiles in rat liver and kidney. Magwere, T., Naik, Y.S., Hasler, J.A. Free Radic. Res. (1997) [Pubmed]
  15. Site-directed mutagenesis of rat liver NAD(P)H: quinone oxidoreductase: roles of lysine 76 and cysteine 179. Ma, Q., Cui, K., Wang, R.W., Lu, A.Y., Yang, C.S. Arch. Biochem. Biophys. (1992) [Pubmed]
  16. Subchronic dietary exposure to Aroclor 1254 in rats: accumulation of PCBs in liver, blood, and adipose tissue and its relationship to induction of various hepatic drug-metabolizing enzymes. Dragnev, K.H., Beebe, L.E., Jones, C.R., Fox, S.D., Thomas, P.E., Nims, R.W., Lubet, R.A. Toxicol. Appl. Pharmacol. (1994) [Pubmed]
  17. Purification and characterization of zeta-crystallin/quinone reductase from guinea pig liver. Rao, P.V., Zigler, J.S. Biochim. Biophys. Acta (1992) [Pubmed]
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