Cosuppression refers to the phenomenon in which silencing among dispersed homologous genes occurs. Here we demonstrate that two nonhomologous reciprocal fusion genes, white-Alcohol dehydrogenase (w-Adh) and Adh-w, exhibit cosuppression using the endogenous Adh sequence as an intermediary. Deletion of the endogenous Adh gene eliminates the interaction, while reintroduction of an 8.6 kb Adh fragm...

Abstract Many hangover cure products containing natural ingredients that are also effective against alcohol-related liver damage or improve function have recently become available. In addition to curing damage, antioxidants, anti-inflammatory agents, and blood ethanol reduction aids emerging as relief targets reduce symptoms. We investigated the ameliorating effect of WON-21 herbal medicinal by...

Chronic alcohol intake leads to alcoholic cardiomyopathy characterized by cardiac hypertrophy and contractile dysfunction possibly related to the toxicity of the ethanol metabolite acetaldehyde. This study examined the impact of augmented acetaldehyde exposure on myocardial function, geometry, and insulin signaling via cardiac-specific overexpression of alcohol dehydrogenase (ADH). ADH transgen...

We present results showing that several species in the plant genus Leavenworthia, in the Brassica family, have three alcohol dehydrogenase loci, unlike Arabidopsis thaliana, which has only a single classical (class P) alcohol dehydrogenase locus. Based on a portion of the sequence, the alcohol dehydrogenase loci of Leavenworthia show about 92%-93% amino acid sequence identity to that of the A. ...

Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD(+) pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein fr...

The primary enzymes involved in alcohol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Both enzymes occur in several forms that are encoded by different genes; moreover, there are variants (i.e., alleles) of some of these genes that encode enzymes with different characteristics and which have different ethnic distributions. Which ADH or ALDH alleles a person carri...

A gene (Adhr(r)) which controls the activity of alcohol dehydrogenase in the scutellum of maize has been found. This gene is not allelic to the Adh(1) locus, which specifies the charge of the enzyme molecule and hence its migration rate. The two genes are linked and located about 17 crossover units apart. The Adh(r)(N) allele specifies equal activities of both the Adh(1)(S) and Adh(1)(F) produc...

A potent new enzyme-antibody conjugate system for amplifying cytotoxicity was tested in a well-defined model of hapten [2,4,6-trinitrophenyl (TNP)]-substituted tumor cells (HEp2) and purified anti-hapten antibody. Brief treatment of TNP-HEp2 cells with low concentrations (0.05 to 0.74 micrograms/ml) of antihapten antibody-alcohol dehydrogenase conjugate (Ab-ADH) followed by culture in complemen...

OBJECTIVE Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in esophageal cancer cells. Moreover the total activity of ADH as well as the activity of class IV ADH isoenzyme is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is reflected in the sera and could thus be helpful for diagnostics of esophageal cancer. ...

One cell strain with stable tolerance to allyl alcohol (AA(r)) was selected from 6 x 10(8) suspension cultured Nicotiana plumbaginifolia Viviani cells. The selected strain contained one-half the alcohol dehydrogenase (ADH) activity of the wild type (NP) due to the loss of two of three bands of ADH activity seen on starch gels following electrophoresis of wild-type cell extracts. Anaerobic condi...