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Gene Review

CRYZ  -  crystallin, zeta (quinone reductase)

Bos taurus

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Disease relevance of CRYZ


High impact information on CRYZ

  • Chaperone-like activity of alpha-crystallin. The effect of NADPH on its interaction with zeta-crystallin [2].
  • Complex formation between alpha-crystallin and non-native zeta-crystallin was demonstrated in the presence of either cibacron blue 3GA or NADPH [2].
  • NADH and dextran sulfate did not affect this characteristic of bovine zeta-crystallin and the enzyme showed no binding affinity for the heparin-Ultragel A4R [3].
  • Superoxide anions were formed during reduction of TNT by zeta-crystallin, though negligible enzyme activity or protein content for superoxide dismutase, a superoxide scavenging enzyme, was found in the lens [1].
  • The absorbing species in these animals is most likely NAD(P)H, which has an absorption maximum at approximately 345 nm and is associated with zeta-crystallin [4].

Biological context of CRYZ

  • Therefore, we speculate that zeta-crystallin may act as a transcriptional enhancer (outer lens cortex), possibly binding to Z-DNA regulatory elements within lens crystallin genes [5].

Associations of CRYZ with chemical compounds

  • The pattern of zeta-crystallin probe-DNA reactivity correlates with the loss of anti-B-DNA antibody staining and decreased eosin-protein staining [6].

Analytical, diagnostic and therapeutic context of CRYZ


  1. Zeta-crystallin catalyzes the reductive activation of 2,4,6-trinitrotoluene to generate reactive oxygen species: a proposed mechanism for the induction of cataracts. Kumagai, Y., Wakayama, T., Lib, S., Shinohara, A., Iwamatsu, A., Sun, G., Shimojo, N. FEBS Lett. (2000) [Pubmed]
  2. Chaperone-like activity of alpha-crystallin. The effect of NADPH on its interaction with zeta-crystallin. Rao, P.V., Horwitz, J., Zigler, J.S. J. Biol. Chem. (1994) [Pubmed]
  3. Guinea pig and bovine zeta-crystallins have distinct functional characteristics highlighting replacements in otherwise similar structures. Rao, P.V., Gonzalez, P., Persson, B., Jörnvall, H., Garland, D., Zigler, J.S. Biochemistry (1997) [Pubmed]
  4. Transmission spectra of light to the mammalian retina. Dillon, J., Zheng, L., Merriam, J.C., Gaillard, E.R. Photochem. Photobiol. (2000) [Pubmed]
  5. Binding properties of bovine ocular lens zeta-crystallin to right-handed B-DNA, left-handed Z-DNA, and single-stranded DNA. Gagna, C.E., Chen, J.H., Kuo, H.R., Lambert, W.C. Cell Biol. Int. (1998) [Pubmed]
  6. Novel use of bovine zeta-crystallin as a conformational DNA probe to characterize a phase transition zone and terminally differentiating fiber cells in the adult canine ocular lens. Gagna, C.E., Kuo, H.R., Agostino, N., Rizzo, D., Isquith, I.R., Mathew, J., Mohammed, J., Hoo, S., Lambert, W.C. Arch. Histol. Cytol. (2001) [Pubmed]
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