Disease relevance of CRYZ

• zeta-Crystallin is a lens protein that has been associated with autosomal dominant congenital cataracts in guinea pigs and thus is a candidate for human congenital cataracts [1].
• Expression of human NAD(P)H: quinone oxidoreductase (DT-diaphorase) in Chinese hamster ovary cells: effect on the toxicity of antitumor quinones [2].
• Association between NAD(P)H: quinone oxidoreductase 1 (NQ01) inactivating C609T polymorphism and adenocarcinoma of the upper gastrointestinal tract [3].
• 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 [4].
• We conducted a hospital-based case-control study of 814 lung cancer patients and 1123 controls to examine the association of the NAD(P)H: quinone oxidoreductase 1 (NQO1) gene polymorphism with lung cancer susceptibility [5].

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 1.11.1.7) and pyridine nucleotide quinone oxidoreductase (EC 1.6.99.2), 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

• A point mutation in the mRNA of NADP(H): quinone oxidoreductase 1 (NQO1, DT-diaphorase) is believed to be responsible for reduced enzyme activity in the adenocarcinoma BE cell line [10].

Biological context of CRYZ

• Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms [1].
• We report here the isolation and characterization of the human zeta-crystallin gene (CRYZ) and its processed pseudogene [11].
• A significant interaction was also found between the -180C>G SNP, a marker of oxidative stress (NAD[P]H quinone oxidoreductase mRNA) and homeostasis model assessment of insulin resistance [12].
• METHODS: A total of 263 healthy volunteers were genotyped for CYP2C9*2, CYP2C9*3, CYP2C9*4, and CYP2C9*5 alleles, as well as for the nicotinamide adenine dinucleotide phosphate, reduced, quinone oxidoreductase 1 genetic polymorphism (NQO1*2) [13].
• Jun and Fos regulation of NAD(P)H: quinone oxidoreductase gene expression [14].

Anatomical context of CRYZ

• Co-refolding zeta-crystallin from its denatured state in 2.5 M urea with either calf eye lens alpha-crystallin or recombinant human alpha B-crystallin could significantly enhance its reactivation yield. alpha B-crystallin was found to be more efficient than alpha A-crystallin in chaperoning the refolding of zeta-crystallin [15].
• We have assigned the zeta-crystallin gene (CRYZ) to human chromosome 1 using a Southern panel of 17 human-mouse somatic cell hybrids and regionally localized it to 1p22-p31 by fluorescence in situ hybridization [1].
• NAD(P)H: quinone oxidoreductase 1 expression in kidney podocytes [16].
• Turkey liver cytosol also had quinone oxidoreductase (QOR) activity [17].
• The human dioxin-inducible NAD(P)H: quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4 [18].

Associations of CRYZ with chemical compounds

• It has been shown to have a novel NADPH: quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals [19].
• Inhibition of quinone oxidoreductase enzymatic activity with dicumarol prior to quinone treatment resulted in increased transcript levels [20].
• Treatment with oltipraz increased GST and NQR activities by approximately 21% and 11%, respectively [21].
• The four Cys ligands for the structural zinc are conserved except in zeta-crystallin, the sorbitol dehydrogenases, and two bacterial enzymes [22].
• Consistent with this, NADPH was able to substantially protect zeta-crystallin against aspirin, whereas PQ did not provide any protection [23].

Physical interactions of CRYZ

• Inhibition kinetics suggested that salicylic acid interacted with zeta-crystallin via a binding site that was distinct from that of NADPH [24].

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

• Organization of the human zeta-crystallin/quinone reductase gene (CRYZ) [11].
• An association between idiopathic Parkinson's disease and polymorphisms of phase II detoxification enzymes: glutathione S-transferase M1 and quinone oxidoreductase 1 and 2 [26].
• Identification of a zeta-crystallin (quinone reductase)-like 1 gene (CRYZL1) mapped to human chromosome 21q22.1 [27].
• The related alcohol dehydrogenases and zeta-crystallin have the same gene organization split by 8 introns, but no splice points coincide between SORD and these gene types [28].
• Catalog of 320 single nucleotide polymorphisms (SNPs) in 20 quinone oxidoreductase and sulfotransferase genes [29].

Analytical, diagnostic and therapeutic context of CRYZ

• Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver [19].
• Clinical significance of a NAD(P)H: quinone oxidoreductase 1 polymorphism in patients with disseminated peritoneal cancer receiving intraperitoneal hyperthermic chemotherapy with mitomycin C [30].
• The purified zeta-crystallin has a molecular weight of 140 kDa, as determined by Superose 12 gel filtration column [31].
• The protein arrays expressed under the four conditions were very similar, and endo-1,4-beta-glucanase (detected by 2-D gels) activity along with beta-glucosidase, xylanase, and NADH/quinone oxidoreductase activities were detected [32].

References