Open AccessThe activity of class I, II, III, and IV alcohol dehyrogenase isoenzymes and aldehyde dehydrogenase in endometrial cancer
Author(s) -
Orywal Karolina,
Jelski Wojciech,
Zdrodowski Michał,
Szmitkowski Maciej
Publication year - 2010
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.20412
Subject(s) - aldehyde dehydrogenase , endometrial cancer , isozyme , alcohol dehydrogenase , chemistry , cancer , enzyme , enzyme assay , acetaldehyde , alcohol , biochemistry , medicine , endocrinology , biology , ethanol
Objective : The metabolism of cancerous cells is in many ways different than in healthy cells. In endometrial cancer, cells exhibit activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which participate in the metabolism of many biological substances. The aim of this study was to compare the metabolism of endometrial cancer cells and normal endometrial cells by measurement of ADH isoenzymes and ALDH activities in these tissues. Methods : The study material consists of cancerous endometrial tissues obtained from 34 patients. Total ADH activity was measured using the photometric method and ALDH activity using the fluorometric method. For the measurement of class I and II ADH isoenzyme activity, we employed the fluorometric method, with class‐specific fluorogenic substrates. The activity of class III and IV ADH was measured using the photometric method. Results : The activity of the class I ADH isoenzyme was significantly higher in the endometrial cancer tissues when compared with normal endometrial tissues. The other classes of ADH tested did not show significant differences between activity of cancerous cells and healthy endometrium. The activity of total ADH was also significantly higher in endometrial cancer. Conclusion : The increased activity of total ADH in endometrial cancer, especially the class I isoenzyme and normal activity of ALDH, may be the cause of disorders in metabolic pathways that use these isoenzymes and could increase the concentration of acetaldehyde, which is cancerogenic substance. J. Clin. Lab. Anal. 24:334–339, 2010. © 2010 Wiley‐Liss, Inc.