Further studies on the 37 kD liver protein-acetaldehyde adduct that formsin Vivo during chronic alcohol ingestion
Open Access
- 1 November 1989
- journal article
- research article
- Published by Ovid Technologies (Wolters Kluwer Health) in Hepatology
- Vol. 10 (5), 807-814
- https://doi.org/10.1002/hep.1840100510
Abstract
We have previously reported the detection of a 37 kD liver protein-acetaldehyde adduct in rats fed alcohol chronically with the AIN'76 diet. It was surprising that only one liver protein-acetaldehyde adduct was found. In this report, we have tried to detect additional protein-acetaldehyde adducts by electroimmunotransblot with rabbit anti-hemocyanin-acetaldehyde adduct IgG and to further characterize the 37 kD liver protein-acetaldehyde adduct. Sensitivity of electroimmunotransblot increased 10-to 20-fold when alkaline phosphatase-linked antibody was used in place of horseradish peroxidase, but only one protein-acetaldehyde adduct band was detected in liver. Feeding rats the Lieber-DeCarli alcohol diet also did not produce more protein-acetaldehyde adduct bands in electroimmunotransblot. Addition of cyanamide, an aldehyde dehydrogenase inhibitor, to the AIN'76 alcohol diet greatly increased the intensity of the 37-kD protein-acetaldehyde adduct band on electroimmunotransblot but did not produce other bands. The 37 kD protein-acetaldehyde adduct decayed in vivo with a half-life of 4 days when alcohol was removed from the diet. The 37 kD protein-acetaldehyde adduct in liver is cytosolic. Its interaction with anti-hemocyanin-acetaldehyde adduct IgG was blocked by polylysine-acetaldehyde adduct and polytyrosine-acetaldehyde adduct. It could be removed by immunosorption with anti-hemocyanin-acetaldehyde adduct IgG-bound immunoresin. When immunoblotted with anti-alcohol dehydrogenase and anti-aldehyde dehydrogenase antibodies, the alcohol dehydrogenase and aldehyde dehydrogenase bands in liver of alcoholfed rats showed identical intensities before and after immunosorption. These data indicate that: (i) the 37 kD protein-acetaldehyde adduct is neither alcohol dehydrogenase nor aldehyde dehydrogenase; (ii) its interaction with anti-hemocyanin-acetaldehyde adduct IgG is by way of acetaldehyde adducts of ϵ- and/or α-amino groups; (iii) its formation and decay in liver in vivo are likely to depend on acetaldehyde concentration.This publication has 18 references indexed in Scilit:
- Formation of acetaldehyde adducts with ethanol-inducible P450IIE1 in vivoBiochemical and Biophysical Research Communications, 1988
- Detection of a protein-acetaldehyde adduct in the liver of rats fed alcohol chronically.JCI Insight, 1988
- Antibodies against acetaldehyde-modified protein epitopes in human alcoholicsHepatology, 1987
- The Interaction of Acetaldehyde With TubulinaAnnals of the New York Academy of Sciences, 1987
- Monoclonal and polyclonal antibodies against acetaldehyde-containing epitopes in acetaldehyde-protein adducts.Proceedings of the National Academy of Sciences of the United States of America, 1986
- Acetaldehyde adducts with proteins: Binding of [14C]acetaldehyde to serum albuminArchives of Biochemistry and Biophysics, 1983
- Binding of acetaldehyde to rat liver microsomes: Enhancement after chronic alcohol consumptionBiochemical and Biophysical Research Communications, 1981
- Acetaldehyde adducts with hemoglobin.JCI Insight, 1981
- Report of the American Institute of Nutrition Ad Hoc Committee on Standards for Nutritional StudiesJournal of Nutrition, 1977
- Fatty Liver in the Rat after Prolonged Intake of Ethanol with a Nutritionally Adequate New Liquid DietJournal of Nutrition, 1967