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Gene Review

CRYZ  -  crystallin, zeta (quinone reductase)

Homo sapiens

Synonyms: NADPH:quinone reductase, Quinone oxidoreductase, Zeta-crystallin
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Disease relevance of CRYZ


High impact information on CRYZ

  • This light-dependent oxidation was inhibited completely by SHAM, an inhibitor of quinone oxidoreductase, and 75% by 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB), which inhibits electron transfer from plastoquinone to the cytochrome b6f complex [6].
  • The metabolic system for such use of H2O2 involves the enzymes, peroxidase (EC and pyridine nucleotide quinone oxidoreductase (EC, which are present in the dormant seed prior to imbibition of water [7].
  • We therefore studied the regulation in B cells of NAD(P)H: quinone oxidoreductase (NQO1) as a typical model phase II enzyme and its role in modulating DEPX-enhanced IgE responses [8].
  • Concentrations required for doubling the NADPH-dependent quinone oxidoreductase response are increased from 1.8 microm in wild-type to >10 microm in rat Aor transgenic fibroblasts [9].
  • We demonstrate that induction of NADPH-dependent quinone oxidoreductase activity by 15d-PGJ2 is markedly attenuated in mouse embryonic fibroblasts that overexpress rAor [9].

Chemical compound and disease context of CRYZ


Biological context of CRYZ


Anatomical context of CRYZ


Associations of CRYZ with chemical compounds


Physical interactions of CRYZ


Regulatory relationships of CRYZ

  • Camel lens zeta-crystallin/NADH:quinone oxidoreductase activity was inhibited by Cibacron blue 3GA (CB) with 9.10-phenanthrenequinone (PQ) as an electron acceptor and NADPH as an electron donor in a time-independent and concentration dependent manner [25].

Other interactions of CRYZ


Analytical, diagnostic and therapeutic context of CRYZ


  1. Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms. Heinzmann, C., Kojis, T.L., Gonzalez, P., Rao, P.V., Zigler, J.S., Polymeropoulos, M.H., Klisak, I., Sparkes, R.S., Mohandas, T., Bateman, J.B. Genomics (1994) [Pubmed]
  2. Expression of human NAD(P)H: quinone oxidoreductase (DT-diaphorase) in Chinese hamster ovary cells: effect on the toxicity of antitumor quinones. Gustafson, D.L., Beall, H.D., Bolton, E.M., Ross, D., Waldren, C.A. Mol. Pharmacol. (1996) [Pubmed]
  3. Association between NAD(P)H: quinone oxidoreductase 1 (NQ01) inactivating C609T polymorphism and adenocarcinoma of the upper gastrointestinal tract. Sarbia, M., Bitzer, M., Siegel, D., Ross, D., Schulz, W.A., Zotz, R.B., Kiel, S., Geddert, H., Kandemir, Y., Walter, A., Willers, R., Gabbert, H.E. Int. J. Cancer (2003) [Pubmed]
  4. Association of NAD(P)H: quinone oxidoreductase 1 (NQO1) C609T polymorphism with esophageal squamous cell carcinoma in a German Caucasian and a northern Chinese population. Zhang, J., Schulz, W.A., Li, Y., Wang, R., Zotz, R., Wen, D., Siegel, D., Ross, D., Gabbert, H.E., Sarbia, M. Carcinogenesis (2003) [Pubmed]
  5. The NAD(P)H:quinone oxidoreductase 1 gene polymorphism and lung cancer: differential susceptibility based on smoking behavior. Xu, L.L., Wain, J.C., Miller, D.P., Thurston, S.W., Su, L., Lynch, T.J., Christiani, D.C. Cancer Epidemiol. Biomarkers Prev. (2001) [Pubmed]
  6. Association of glycolate oxidation with photosynthetic electron transport in plant and algal chloroplasts. Goyal, A., Tolbert, N.E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  7. Breaking of seed dormancy by catalase inhibition. Hendricks, S.B., Taylorson, R.B. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  8. Phase II enzymes induction blocks the enhanced IgE production in B cells by diesel exhaust particles. Wan, J., Diaz-Sanchez, D. J. Immunol. (2006) [Pubmed]
  9. Nrf2-mediated induction of cytoprotective enzymes by 15-deoxy-Delta12,14-prostaglandin J2 is attenuated by alkenal/one oxidoreductase. Yu, X., Egner, P.A., Wakabayashi, J., Wakabayashi, N., Yamamoto, M., Kensler, T.W. J. Biol. Chem. (2006) [Pubmed]
  10. Presence of a heterozygous substitution and its relationship to DT-diaphorase activity. Kuehl, B.L., Paterson, J.W., Peacock, J.W., Paterson, M.C., Rauth, A.M. Br. J. Cancer (1995) [Pubmed]
  11. Organization of the human zeta-crystallin/quinone reductase gene (CRYZ). Gonzalez, P., Rao, P.V., Zigler, J.S. Genomics (1994) [Pubmed]
  12. A promoter genotype and oxidative stress potentially link resistin to human insulin resistance. Smith, S.R., Bai, F., Charbonneau, C., Janderová, L., Argyropoulos, G. Diabetes (2003) [Pubmed]
  13. Pharmacogenetics of acenocoumarol pharmacodynamics. Morin, S., Bodin, L., Loriot, M.A., Thijssen, H.H., Robert, A., Strabach, S., Verstuyft, C., Tregouet, D.A., Dubert, L., Laurent-Puig, P., Funck-Brentano, C., Jaillon, P., Beaune, P.H., Becquemont, L. Clin. Pharmacol. Ther. (2004) [Pubmed]
  14. Jun and Fos regulation of NAD(P)H: quinone oxidoreductase gene expression. Jaiswal, A.K. Pharmacogenetics (1994) [Pubmed]
  15. Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation. Goenka, S., Raman, B., Ramakrishna, T., Rao, C.M. Biochem. J. (2001) [Pubmed]
  16. NAD(P)H: quinone oxidoreductase 1 expression in kidney podocytes. Zappa, F., Ward, T., Pedrinis, E., Butler, J., McGown, A. J. Histochem. Cytochem. (2003) [Pubmed]
  17. Biochemical basis for the extreme sensitivity of turkeys to aflatoxin B(1). Klein, P.J., Buckner, R., Kelly, J., Coulombe, R.A. Toxicol. Appl. Pharmacol. (2000) [Pubmed]
  18. The human dioxin-inducible NAD(P)H: quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4. Shaw, P.M., Reiss, A., Adesnik, M., Nebert, D.W., Schembri, J., Jaiswal, A.K. Eur. J. Biochem. (1991) [Pubmed]
  19. Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver. Gonzalez, P., Rao, P.V., Zigler, J.S. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  20. Quinone oxidoreductase message levels are differentially regulated in parasitic and non-parasitic plants exposed to allelopathic quinones. Matvienko, M., Wojtowicz, A., Wrobel, R., Jamison, D., Goldwasser, Y., Yoder, J.I. Plant J. (2001) [Pubmed]
  21. Protection of retinal pigment epithelial cells from oxidative damage by oltipraz, a cancer chemopreventive agent. Nelson, K.C., Armstrong, J.S., Moriarty, S., Cai, J., Wu, M.W., Sternberg, P., Jones, D.P. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  22. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. Sun, H.W., Plapp, B.V. J. Mol. Evol. (1992) [Pubmed]
  23. Inhibition of camel lens zeta-crystallin by aspirin and aspirin-like analgesics. Bazzi, M.D., Rabbani, N., Duhaiman, A.S. Int. J. Biochem. Cell Biol. (2002) [Pubmed]
  24. Zeta-crystallin displays strong selectivity for salicylic acid over aspirin. Bazzi, M.D. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  25. Inhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase activity by Cibacron blue. Duhaiman, A.S. J. Enzym. Inhib. (1996) [Pubmed]
  26. An association between idiopathic Parkinson's disease and polymorphisms of phase II detoxification enzymes: glutathione S-transferase M1 and quinone oxidoreductase 1 and 2. Harada, S., Fujii, C., Hayashi, A., Ohkoshi, N. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  27. Identification of a zeta-crystallin (quinone reductase)-like 1 gene (CRYZL1) mapped to human chromosome 21q22.1. Kim, M.Y., Lee, H.K., Park, J.S., Park, S.H., Kwon, H.B., Soh, J. Genomics (1999) [Pubmed]
  28. Structural organization of the human sorbitol dehydrogenase gene (SORD). Iwata, T., Popescu, N.C., Zimonjic, D.B., Karlsson, C., Höög, J.O., Vaca, G., Rodriguez, I.R., Carper, D. Genomics (1995) [Pubmed]
  29. Catalog of 320 single nucleotide polymorphisms (SNPs) in 20 quinone oxidoreductase and sulfotransferase genes. Iida, A., Sekine, A., Saito, S., Kitamura, Y., Kitamoto, T., Osawa, S., Mishima, C., Nakamura, Y. J. Hum. Genet. (2001) [Pubmed]
  30. Clinical significance of a NAD(P)H: quinone oxidoreductase 1 polymorphism in patients with disseminated peritoneal cancer receiving intraperitoneal hyperthermic chemotherapy with mitomycin C. Fleming, R.A., Drees, J., Loggie, B.W., Russell, G.B., Geisinger, K.R., Morris, R.T., Sachs, D., McQuellon, R.P. Pharmacogenetics (2002) [Pubmed]
  31. Purification and characterization of zeta-crystallin from the camel lens. Duhaiman, A.S., Rabbani, N., AlJafari, A.A., Alhomida, A.S. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  32. Culture conditions affecting biodegradation components of the brown-rot fungus Gloeophyllum trabeum. Varela, E., Mester, T., Tien, M. Arch. Microbiol. (2003) [Pubmed]
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