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The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer

The brain being highly sensitive to the action of alcohol is potentially susceptible to its carcinogenic effects. Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the main enzymes involved in ethanol metabolism, which leads to the generation of carcinogenic acetaldehyde. Human brain...

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Autores principales: Laniewska-Dunaj, Magdalena, Jelski, Wojciech, Orywal, Karolina, Kochanowicz, Jan, Rutkowski, Robert, Szmitkowski, Maciej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671125/
https://www.ncbi.nlm.nih.gov/pubmed/23624825
http://dx.doi.org/10.1007/s11064-013-1053-9
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author Laniewska-Dunaj, Magdalena
Jelski, Wojciech
Orywal, Karolina
Kochanowicz, Jan
Rutkowski, Robert
Szmitkowski, Maciej
author_facet Laniewska-Dunaj, Magdalena
Jelski, Wojciech
Orywal, Karolina
Kochanowicz, Jan
Rutkowski, Robert
Szmitkowski, Maciej
author_sort Laniewska-Dunaj, Magdalena
collection PubMed
description The brain being highly sensitive to the action of alcohol is potentially susceptible to its carcinogenic effects. Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the main enzymes involved in ethanol metabolism, which leads to the generation of carcinogenic acetaldehyde. Human brain tissue contains various ADH isoenzymes and possess also ALDH activity. The purpose of this study was to compare the capacity for ethanol metabolism measured by ADH isoenzymes and ALDH activity in cancer tissues and healthy brain cells. The samples were taken from 62 brain cancer patients (36 glioblastoma, 26 meningioma). For the measurement of the activity of class I and II ADH isoenzymes and ALDH activity, the fluorometric methods were used. The total ADH activity and activity of class III and IV isoenzymes were measured by the photometric method. The total activity of ADH, and activity of class I ADH were significantly higher in cancer cells than in healthy tissues. The other tested classes of ADH and ALDH did not show statistically significant differences of activity in cancer and in normal cells. Analysis of the enzymes activity did not show significant differences depending on the location of the tumor. The differences in the activity of total alcohol dehydrogenase, and class I isoenzyme between cancer tissues and healthy brain cells might be a factor for metabolic changes and disturbances in low mature cancer cells and additionally might be a reason for higher level of acetaldehyde which can intensify the carcinogenesis.
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spelling pubmed-36711252013-06-06 The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer Laniewska-Dunaj, Magdalena Jelski, Wojciech Orywal, Karolina Kochanowicz, Jan Rutkowski, Robert Szmitkowski, Maciej Neurochem Res Original Paper The brain being highly sensitive to the action of alcohol is potentially susceptible to its carcinogenic effects. Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the main enzymes involved in ethanol metabolism, which leads to the generation of carcinogenic acetaldehyde. Human brain tissue contains various ADH isoenzymes and possess also ALDH activity. The purpose of this study was to compare the capacity for ethanol metabolism measured by ADH isoenzymes and ALDH activity in cancer tissues and healthy brain cells. The samples were taken from 62 brain cancer patients (36 glioblastoma, 26 meningioma). For the measurement of the activity of class I and II ADH isoenzymes and ALDH activity, the fluorometric methods were used. The total ADH activity and activity of class III and IV isoenzymes were measured by the photometric method. The total activity of ADH, and activity of class I ADH were significantly higher in cancer cells than in healthy tissues. The other tested classes of ADH and ALDH did not show statistically significant differences of activity in cancer and in normal cells. Analysis of the enzymes activity did not show significant differences depending on the location of the tumor. The differences in the activity of total alcohol dehydrogenase, and class I isoenzyme between cancer tissues and healthy brain cells might be a factor for metabolic changes and disturbances in low mature cancer cells and additionally might be a reason for higher level of acetaldehyde which can intensify the carcinogenesis. Springer US 2013-04-27 2013 /pmc/articles/PMC3671125/ /pubmed/23624825 http://dx.doi.org/10.1007/s11064-013-1053-9 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Original Paper
Laniewska-Dunaj, Magdalena
Jelski, Wojciech
Orywal, Karolina
Kochanowicz, Jan
Rutkowski, Robert
Szmitkowski, Maciej
The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title_full The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title_fullStr The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title_full_unstemmed The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title_short The Activity of Class I, II, III and IV of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in Brain Cancer
title_sort activity of class i, ii, iii and iv of alcohol dehydrogenase (adh) isoenzymes and aldehyde dehydrogenase (aldh) in brain cancer
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671125/
https://www.ncbi.nlm.nih.gov/pubmed/23624825
http://dx.doi.org/10.1007/s11064-013-1053-9
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