Disease relevance of CRYZ

• Sequence data from peptides obtained by digestion with lysylendopeptidase Achromobacter protease I (API) revealed that TNT reductase is identical to zeta-crystallin [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 [1].

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

• Circular dichroism spectroscopy of zeta-crystallin in the presence and absence of NADPH or cibacron blue indicated that nucleotide binding was accompanied by a change in the protein's aromatic amino acid environment but that the secondary structure was unaffected [2].
• The enzyme-linked immunosorbent assay (ELISA) was used to quantitate the binding of bovine zeta-crystallin to purified high molecular weight double-stranded (ds-) and single-stranded (ss-) DNA (bovine and synthetic DNA) [5].

References