Disease relevance of ADH7

• A polymerase chain reaction and direct sequencing of the ADH7 gene were carried out in 50 controls and 50 patients with probable multiple system atrophy (MSA) [1].
• retSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines [2].
• The effect of gastritis on human gastric alcohol dehydrogenase activity and ethanol metabolism [3].
• Here, we report the isolation, from a cDNA library prepared from uterine mRNA collected at the estrous stage and from a rat mammary adenocarcinoma cell line, of a cDNA that encodes a novel retinol dehydrogenase [4].
• Influence of age, sex, and Helicobacter pylori infection before and after eradication on gastric alcohol dehydrogenase activity [5].

Psychiatry related information on ADH7

• Gastric alcohol dehydrogenase activity in man: influence of gender, age, alcohol consumption and smoking in a caucasian population [6].

High impact information on ADH7

• Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy [7].
• Thus, aspirin may increase the bioavailability of ingested ethanol in humans, possibly by reducing ethanol oxidation by gastric alcohol dehydrogenase [8].
• Here we demonstrate that PPARgamma, turns on retinoic acid synthesis by inducing the expression of retinol and retinal metabolizing enzymes such as retinol dehydrogenase 10 and retinaldehyde dehydrogenase type 2 (RALDH2) [9].
• The contribution of gastric alcohol dehydrogenase to the first-pass metabolism of ethanol and alcohol-drug interactions is discussed [10].
• Effects of cimetidine on gastric alcohol dehydrogenase activity and blood ethanol levels [11].

Biological context of ADH7

• A nearly full-length cDNA for ADH7 was isolated from a human stomach cDNA library, and a 5' genomic clone containing exons 1 and 2 was isolated from a human genomic library [12].
• The ADH7 gene encoding human Class IV (sigma) alcohol dehydrogenase (ADH) was cloned from a Caucasian genomic DNA library and characterized [13].
• Fluorescence in situ hybridization analysis showed that ADH7 is located on human chromosome 4q23-q24, close to the ADH cluster locus (4q21-q25) [13].
• The deduced amino acid sequence shows 59-70% identities with the other human ADH classes, demonstrating that the stomach enzyme represents a distinct structure, constituting class IV, coded by a separate gene, ADH7 [14].
• We observed nominally significant pairwise linkage disequilibrium, in some populations, between the ADH7 site and some Class I ADH sites, at moderate values and at a molecular distance as great as 100 kb [15].

Anatomical context of ADH7

• Like microsomal RoDH, the recombinant enzyme recognized as substrate retinol bound to cellular retinol-binding protein, had higher activity with NADP rather than NAD, was stimulated by ethanol or phosphatidylcholine, was not inhibited by 4-methylpyrazole, was inhibited by phenylarsine oxide and carbenoxolone and localized to microsomes [16].
• The enzymatic properties of recombinant bovine prRDH closely match those previously reported for RDH activity in crude bovine rod outer segment preparations [17].
• We therefore determined the topology of mouse retinol dehydrogenase type 1 (Rdh1) and cis-retinoid androgen dehydrogenase type 1 (Crad1) in the endoplasmic reticulum of intact mammalian cells [18].
• RoDH2 cDNA was subcloned into expression vectors and transiently transfected into CHOP and COS-1 cells [19].
• Identification of the oxidative 3alpha-hydroxysteroid dehydrogenase activity of rat Leydig cells as type II retinol dehydrogenase [19].

Associations of ADH7 with chemical compounds

• Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro [20].
• BACKGROUND: Of the seven known human alcohol dehydrogenase (ADH) genes, the non-liver expressed ADH7 gene codes for the enzyme with the highest maximal activity for ethanol [21].
• A recent study in a Japanese subject found a point mutation in the codon for amino acid 287 of the ADH7 gene (which encodes sigma-ADH), changing the amino acid from glycine to valine [22].
• Retinoic acid regulation of one member of the human class I alcohol dehydrogenase (ADH) gene family was demonstrated, suggesting that the retinol dehydrogenase function of ADH may play a regulatory role in the biosynthetic pathway for retinoic acid [23].
• Cell culture studies support a role for RoDH-4 as a retinol dehydrogenase and for AKR1B1 as a retinaldehyde reductase in vivo [24].

Regulatory relationships of ADH7

• The tumor suppressor adenomatous polyposis coli and caudal related homeodomain protein regulate expression of retinol dehydrogenase L [25].

Other interactions of ADH7

• Thus, the previously observed epistatic effect of ADH7 cannot be explained by its linkage disequilibrium with a causative factor in ADH1B [21].
• Differential activity of the promoter for the human alcohol dehydrogenase (retinol dehydrogenase) gene ADH3 in neural tube of transgenic mouse embryos [26].
• Our results show an association between a certain ADH4 (formerly known as ADH7 in humans) allele and PD [27].
• Protein structures were verified by amino acid analysis and mass spectrometry, retinoid binding properties were evaluated by UV-visible and fluorescence spectroscopy and substrate carrier functions were assayed for recombinant 11-cis-retinol dehydrogenase (rRDH5) [28].
• Identification of RDH10, an All-trans Retinol Dehydrogenase, in Retinal Muller Cells [29].

Analytical, diagnostic and therapeutic context of ADH7

• We report here the isolation and sequence determination of a novel human ADH gene (ADH7) [30].
• Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH [13].
• Therefore, in a pilot study, we used the denaturing high performance liquid chromatography (DHPLC) method to screen 49 oesophageal cancer cases for SNPs in the ADH7 gene [31].
• Sequence analysis of cloned PCR products identified retinol dehydrogenase type II (RoDH2) as the prevalent species in purified Leydig cells [19].
• Sex and age differences in gastric alcohol dehydrogenase activity in relation to abnormalities of gastric histology and Helicobacter pylori infection were determined in 63 patients (32 men and 31 women) undergoing upper endoscopy for gastrointestinal symptoms [32].

References