Disease relevance of ADH1C

• In human hepatoma cell lines and differentiated primary and secondary chick fibroblasts, no ADH activity was demonstrable; such cells were not inhibited by 100 mM ethanol additions and DNA synthesis rates were similar to untreated cultures [1].

High impact information on ADH1C

• The superposition of these two regions aligns an intron from the maize alcohol dehydrogenase gene four nucleotides from an intron in the chicken pyruvate kinase gene [2].
• We have found some sequence homology between a segment of pyruvate kinase and the structurally homologous mononucleotide binding fold of alcohol dehydrogenase [2].
• cDNA sequence and catalytic properties of a chick embryo alcohol dehydrogenase that oxidizes retinol and 3beta,5alpha-hydroxysteroids [3].
• A recent finding of a novel class of retinol-active alcohol dehydrogenase (ADH) in frog prompted analysis of this activity in other vertebrate forms [4].
• N-terminal acetylation in a third protein family of vertebrate alcohol dehydrogenase/retinal reductase found through a 'proteomics' approach in enzyme characterization [4].

Biological context of ADH1C

• The nucleotide sequence of one of the two unique cDNA clones, DGH1, had high similarity to the Human class I alcohol dehydrogenase (ADH) gamma subunit and represented the carboxy-terminus of the protein from amino acid 190-374 [5].
• Gene activation of alcohol dehydrogenase in Japanese quail and chicken-quail hybrid embryos [6].
• Point mutations mimicking phoshorylation decrease chaperone activity of Hsp25 measured by reduction of dithiothreitol induced aggregation of alpha-lactalbumin, but increase the chaperone activity of Hsp25 measured by heat induced aggregation of alcohol dehydrogenase [7].

Anatomical context of ADH1C

• Hepatocytes treated with 4-methylpyrazole, an inhibitor of ADH, were partially protected from ethanol effects [1].

Associations of ADH1C with chemical compounds

• Similarly, two different yeast glucose-6-phosphate dehydrogenases and a minor variant of a human alcohol dehydrogenase were found to be acetylated [8].
• The major ethanol-active form of chicken liver alcohol dehydrogenase was characterized [9].
• Induction of ADH by estradiol treatment occurred only in this tissue [5].
• The cytosolic LPA was associated both with carotene-cleavage activity and alcohol dehydrogenase (NAD(P)+) (EC 1.1.1.71) activity [10].
• Pyrazole is a potent inhibitor of alcohol dehydrogenase [11].

Analytical, diagnostic and therapeutic context of ADH1C

• SDS/PAGE and Western blot analysis of the proteins indicated that the level of a 38-kDa protein that cross-reacted with antibodies prepared against the chicken ADH was increased 5-7-fold by hormone treatment [5].
• Alcohol dehydrogenase activity increased during the period studied in both ethanol and control groups, however, ethanol significantly inhibited the enzymatic activity [12].

References