Karolina Orywal

The activity of class I, II, III and IV of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the wall of abdominal aortic aneurysms

OBJECTIVE Human blood vessels contain a huge amount of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which play a significant role in the metabolism of many biological substances and participate in various metabolic pathways. The aim of this study was the investigation of the differences between the activities of ADH and ALDH in the wall of aortic aneurysm and wall of healthy aorta, that can explain the pathological background of aneurysm development. METHODS For the measurement of the activity of class I and II ADH isoenzymes and ALDH activity the fluorometric methods was employed. The total ADH activity and activity of class III and IV isoenzymes was measured by the photometric method. The study material consisted of vessels wall samples obtained from 45 abdominal aortic aneurysm. RESULTS The activity of the class I ADH isoenzyme was significantly lower in the wall of aortic aneurysm than in healthy aorta. The other tested classes of ADH showed the tendency to lower level of the activity in aneurysm tissue than that in wall of unchanged aorta. The activities of total ADH and ALDH were also not significantly lower in the aneurysms. CONCLUSION The decrease of the activity of class I ADH isoenzymes in the wall of aortic aneurysm may be a factor of some disorders in metabolic pathways with participation of these isoenzymes.

The activity of class I, II, III, and IV alcohol dehyrogenase isoenzymes and aldehyde dehydrogenase in endometrial cancer

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.

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 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.

The diagnostic value of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) measurement in the sera of gastric cancer patients

Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in gastric cancer cells (GC). Moreover, the activity of total ADH and class IV isoenzymes is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is probably reflected in the sera and could thus be helpful for diagnostics of gastric cancer. The aim of this study was to investigate a potential role of ADH and ALDH as tumor markers for gastric cancer. We defined diagnostic sensitivity, specificity, predictive value for positive and negative results, and receiver-operating characteristics (ROC) curve for tested enzymes. Serum samples were taken from 168 patients with gastric cancer before treatment and from 168 control subjects. Total ADH activity and class III and IV isoenzymes were measured by photometric but ALDH activity and ADH I and II by the fluorometric method, with class-specific fluorogenic substrates. There was significant increase in the activity of ADH IV isoenzyme and ADH total in the sera of gastric cancer patients compared to the control. The diagnostic sensitivity for ADH IV was 73%, specificity 79%, positive and negative predictive values were 81 and 72% respectively. Area under ROC curve for ADH IV was 0.67. The results suggest a potential role for ADH IV as marker of gastric cancer.

Alcohol dehydrogenase and aldehyde dehydrogenase in malignant neoplasms

According to International Agency for Research on Cancer, ethanol and acetaldehyde belong to group 1 of human carcinogens. The accurate mechanism by which alcohol consumption enhances carcinogenesis is still unexplained. Alcohol is oxidized primarily by alcohol dehydrogenase (ADH) to acetaldehyde, a substance capable of initiating carcinogenesis by forming adducts with proteins and DNA and causing mutations. Next, acetaldehyde is metabolized by aldehyde dehydrogenase (ALDH) to acetate. In tissues of many cancers, we can observe significantly higher activity of total alcohol dehydrogenase with any change in aldehyde dehydrogenase activity in comparison with healthy cells. Moreover, in malignant diseases of digestive system, significantly increased activity of ADH isoenzymes class I, III and IV was found. The gynecological, brain and renal cancers exhibit increased activity of class I ADH. ADH and ALDH can play also a crucial regulatory role in initiation and progression of malignant diseases by participation in retinoic acid synthesis and elimination of toxic acetaldehyde. Besides, changes of enzymes activities in tumor cells are reflected in serum of cancer patients, which create the possibilities of application ADH isoenzymes as cancer markers.

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in cervical cancer.

OBJECTIVE The aim of this study was to compare the metabolism of cervical cancer cells and normal cervical cells by measurement of ADH isoenzymes and ALDH activities. METHODS The study material consisted of 40 cancerous cervical tissues. Class III, IV of ADH and total ADH activity was measured by the photometric method and class I, II ADH and ALDH activity by the fluorometric method with class-specific fluorogenic substrates. RESULTS The activity of the class I ADH isoenzyme and the total ADH were significantly higher in cervical cancer as compared to healthy tissues. Class I of ADH and total ADH activity are significantly higher in every stage of cancer as compared to the control. There are no significant differences between planoepitheliale and adenocarcinoma. CONCLUSION The increased activity of total ADH in cervical cancer may be the cause of some metabolic disorders in cancer cells, which may intensify carcinogenesis in this organ.

Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with acute and chronic pancreatitis

OBJECTIVE Acute and chronic pancreatitis is a major complication of alcohol abuse. The pancreas can metabolize ethanol via oxidative pathway involving the enzymes - alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) as well as the nonoxidative pathway. Human pancreas tissue contains various ADH isoenzymes and possesses also ALDH activity. In this paper we have measured the activity of alcohol dehydrogenase isoenzymes, and aldehyde dehydrogenase in the sera of patients with acute and chronic pancreatitis. METHODS Serum samples were taken for routine biochemical investigation from 46 patients suffering from acute pancreatitis and 32 patients with chronic pancreatitis. Total ADH activity was measured by photometric method with p-nitrosodimethylaniline (NDMA) as a substrate and ALDH activity by the fluorometric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I isoenzymes we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was measured by the photometric method with n-octanol and class IV with m-nitrobenzaldehyde as a substrate. RESULTS A statistically significant increase of class III alcohol dehydrogenase isoenzymes was found in the sera of patients with acute and chronic pancreatitis. The median activity of this class isoenzyme in the patients group increased about 35% in the comparison to the control level. The total alcohol dehydrogenase activity was also significantly higher (23.5%) among patients with pancreatitis than healthy ones. The activities of other tested ADH isoenzymes and total ALDH were unchanged. The activity of the class I ADH isoenzyme was significantly higher in the sera of heavy drinkers with pancreatitis. CONCLUSION We can state that the increase of the activity of class III alcohol dehydrogenase isoenzyme in the sera of pancreatitis patients seems to be caused by the release of this isoenzyme from damaged pancreatic cells.

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in renal cell carcinoma

OBJECTIVES Ethanol has been considered as a lifestyle risk factor for cancer in humans. While some studies have indicated that alcohol intake has a preventive effect for renal cell cancer, others have not. The metabolism of alcohol in cancer cells may be in many ways different than in healthy tissue and its disturbances could be associated with carcinogenesis. The aim of this study was to compare the metabolism of renal cell cancer cells and normal renal cells by measurement of ADH isoenzymes and ALDH activities in these tissues. MATERIAL AND METHODS The study material consisted of 43 cancerous renal tissues (14 patients in stage II, 19 in stage III and 10 in stage IV). Class III and IV ADH and total ADH activities were measured by the photometric method and class I and II ADH and ALDH activities by the fluorometric method with class-specific fluorogenic substrates. RESULTS The activity of the class I ADH isoenzyme and the total ADH was significantly higher in every stage of renal cell cancer as compared to healthy tissues. Analysis of ALDH activity did not show statistically significant differences between cancer and healthy cells. CONCLUSION The increased activity of total ADH in renal cell cancer, especially the class I isoenzyme and normal activity of ALDH, may be the factor intensifying carcinogenesis because of increasing the ability to highly carcinogenic acetaldehyde formation and causing disorders in metabolism of many biologically important substances.

Enamel mineral content in patients with severe tooth wear.

PURPOSE The amounts of calcium (Ca), magnesium (Mg), zinc (Zn), and copper (Cu) in enamel may be crucial for maintaining its integrity and to attenuate potential environmental effects on teeth. The aim of this study was to examine whether the mineral composition of enamel could influence tooth wear. MATERIALS AND METHODS A total of 50 patients with severe tooth wear were compared with 20 healthy volunteers. Tooth wear was assessed using clinical examination according to the protocol of Smith and Knight. Subsequently, the maxillary central incisors of each subject were subjected to acid biopsies to assess the mineral composition in the enamel. Atomic absorption spectroscopy with an air/acetylene flame was used to analyze for Ca, Zn, and Mg. Graphite furnace atomic absorption spectroscopy was used to analyze for Cu. RESULTS The concentrations of Ca and Mg in tooth enamel were comparable in the study and control groups. Zn enamel content was higher in patients with tooth wear, and Cu enamel content was lower in these patients compared with the control group. CONCLUSION The differing Zn and Cu contents in tooth enamel might offer a reason for excessive tooth wear in these patients. However, the results require further, more detailed study.

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in ovarian cancer and ovarian cysts

PURPOSE The metabolism of cancerous cells is in many ways different than in healthy cells. In ovarian cancer, cells exhibit activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which participate in metabolism of many biological substances. The aim of this study was to compare the metabolism of ovarian cancer cells, ovarian cysts and normal ovarian cells by measurement of ADH isoenzymes and ALDH activities. MATERIAL AND METHODS The study material consisted of 36 cancerous ovarian tissues. Class III, IV of ADH and total ADH activity was measured by the photometric method and class I, II ADH and ALDH activity by the fluorometric method with class-specific fluorogenic substrates. RESULTS The activity of the class I ADH isoenzyme and the total ADH was significantly higher in ovarian cancer as compared to ovarian cysts and healthy tissues but there are no significant differences between ovarian cysts and healthy cells. The other classes of ADH tested, did not show significant differences between activity of cancerous cells and healthy ovary. CONCLUSION The increased activity of total ADH in ovarian cancer, especially the class I isoenzyme and normal activity of ALDH, may be the factor for the disturbances in important biological substances metabolism and could increase the concentration of highly carcinogenic acetaldehyde.