The Alterations in Alcohol Dehydrogenase Activity in the Sera of Women With Intrahepatic Cholestasis of Pregnancy.

BACKGROUND/AIM: The liver of pregnant women undergoes physiological and pathological changes and the changes in liver enzyme activity and release reflect changes in serum enzymatic activity. We aimed to assess the activity of alcohol dehydrogenase (ADH) isoenzymes, and aldehyde dehydrogenase (ALDH) in the sera of women with intrahepatic cholestasis of pregnancy (ICP), the most common pregnancy-related liver disease. PATIENTS AND METHODS: Serum samples were taken from 40 women with ICP in the second or third trimester of pregnancy. Serum samples were also obtained from 40 healthy pregnant women at the same time of pregnancy and 40 healthy non-pregnant women. Class I and II of ADH and ALDH activity was measured by a spectrofluorometric method. Class III, IV ADH and total ADH activity was measured by photometric methods. RESULTS: The total ADH activity was significantly higher in women with ICP than in healthy pregnant and non-pregnant women (about 42%). The median total activity of ADH was 1067 mU/l in women with ICP, 628 mU/l in healthy pregnant and 605 mU/l in non-pregnant women. A statistically significant increase in class I ADH isoenzymes was found in the sera of pregnant women with ICP. The median activity of this class in the ICP group increased about 62% and 80% in comparison to the healthy pregnant women and non-pregnant women, respectively. CONCLUSION: The activity of class I ADH isoenzymes in the sera of women with ICP is statistically significantly increased and may have a diagnostic significance.

Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Activity in the Serum of Patients with Non-alcoholic Fatty Liver Disease.

BACKGROUND/AIM: Non-alcoholic liver disease (NAFLD) is one of the most common causes of chronic liver disease, and its prevalence and medical importance is increasing worldwide. Changes in enzyme activity in liver cells in various liver diseases are reflected by an increase in serum enzymatic activity. For example, alcohol dehydrogenase activity (ADH) and aldehyde dehydrogenase (ALDH), that occur in the liver in large quantities, correlate with disease severity during cirrhosis. In the current study, the activity of ADH isoenzymes and ALDH in the serum of patients with NAFLD was investigated. MATERIALS AND METHODS: Serum samples were collected for routine biochemical studies from 55 patients with NAFLD patients and from 50 healthy individuals. Class I and II ADH and ALDH activity were measured by spectrofluorometric method. Photometric methods were used to measure ADH class III, IV and total ADH activity. RESULTS: Total ADH activity was significantly higher in non-alcoholic fatty liver (NAFL) and non-alcoholic steatohepatitis (NASH) than in healthy individuals (44 and 48.5% activity, respectively). The median total activity of ADH was 1,164 mU/l in patients with NAFLD, 1,258 mU/l in NASH and 648 mU/l in the control group. The increase in ADH class I and II isoenzyme in serum of patients with NAFL and NASH was statistically significant. The activity of ADH I, ADH II, and total ADH significantly increased with increasing disease progression. CONCLUSION: The activity of isozymes of class I and II alcohol dehydrogenase in patients with NAFLD is enhanced and appears to be due to the release of these isoenzymes from damaged hepatocytes.

The Alcohol Dehydrogenase Isoenzyme as a Potential Marker of Pancreatitis.

BACKGROUND/AIM: Human pancreas parenchyma contains various alcohol dehydrogenase (ADH) isoenzymes and also possesses aldehyde dehydrogenase (ALDH) activity. The altered activities of ADH and ALDH in damaged pancreatic tissue in the course of pancreatitis are reflected in the human serum. The aim of this study was to investigate a potential role of ADH and ALDH as markers for acute (AP) and chronic pancreatitis (CP). PATIENTS AND METHODS: Serum samples were collected for routine biochemical investigations from 75 patients suffering from acute pancreatitis and 70 patients with chronic pancreatitis. Fluorometric methods were used to measure the activity of class I and II ADH and ALDH activity. The total ADH activity and activity of class III and IV isoenzymes were measured by a photometric method. RESULTS: There was a significant increase in the activity of ADH III isoenzyme (15.06 mU/l and 14.62 mU/l vs. 11.82 mU/l; p<0.001) and total ADH activity (764 mU/l and 735 mU/l vs. 568 mU/l) in the sera of patients with acute pancreatitis or chronic pancreatitis compared to the control. The diagnostic sensitivity for ADH III was about 84%, specificity was 92 %, positive and negative predictive values were 93% and 87% respectively in acute pancreatitis. Area under the Receiver Operating Curve (ROC) curve for ADH III in AP and CP was 0.88 and 0.86 respectively. CONCLUSION: ADH III has a potential role as a marker of acute and chronic pancreatitis.

The alterations in alcohol dehydrogenase and aldehyde dehydrogenase activities in the sera of patients with renal cell carcinoma.

PURPOSE: In a previous study we showed that the total activity of alcohol dehydrogenase (ADH) and its isoenzyme class I was significantly higher in renal cancer (RCC) cells compared to normal kidney. The aim of this study was to compare the activities of ADH isoenzymes and aldehyde dehydrogenase (ALDH) in the sera of patients with different stages of RCC and healthy subjects. MATERIALS AND METHODS: Serum samples were taken from 54 patients with clear cell RCC (17 patients in stage II, 22 in stage III and 15 in stage IV) and 52 healthy patients. Class III, IV of ADH and the total ADH activity was measured by the photometric method. For the measurement of ADH class I, II and the total ALDH activity we employed the fluorometric method. RESULTS: The total activity of ADH and its isoenzyme class I were significantly higher in the sera of patients with every stage of RCC compared to healthy subjects. The analysis of ALDH activity did not indicate significant differences between tested groups. CONCLUSIONS: The increased activity of total ADH and its isoenzyme class I in the sera of patients with RCC, seems to be caused by isoenzymes being released from cancerous cells and may be useful for diagnostics of renal cancer.

The Diagnostic Significance of Serum Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Activity in Urinary Bladder Cancer Patients.

BACKGROUND: The aim of this study was to investigate a potential role of alcohol dehydrogenase and aldehyde dehydrogenase as tumor markers for urinary bladder cancer. MATERIALS AND METHODS: Serum samples were obtained from 41 patients with bladder cancer and 52 healthy individuals. Class III and IV of ADH and total ADH activity were measured by the photometric method. For measurement of class I and II ADH and ALDH activity, the fluorometric method was employed. RESULTS: Significantly higher total activity of ADH was found in sera of both, low-grade and high-grade bladder cancer patients. The diagnostic sensitivity for total ADH activity was 81.5%, specificity 98.1%, positive (PPV) and negative (NPV) predictive values were 97.4% and 92.3% respectively. Area under ROC curve for total ADH activity was 0.848. CONCLUSION: A potential role of total ADH activity as a marker for bladder cancer, is herein proposed.

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 the sera of bladder cancer patients.

OBJECTIVES: Studies on alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity in the sera of patients with malignant neoplasms show that cancer cells in many organs may release ADH isoenzymes into the blood. The aim of this study was to investigate the differences in the activity of ADH isoenzymes and ALDH in the sera of patients with bladder cancer (BCa), and with different grades of the disease. MATERIAL AND METHODS: Blood samples were taken from 39 patients with BCa (15 patients with low-grade and 24 with high-grade BCa) and from 60 healthy subjects. Class III and IV of ADH and total ADH activity were measured using the photometric method, while class I and II ADH and ALDH activity using the fluorometric method with class-specific fluorogenic substrates. RESULTS: The activity of the class I ADH isoenzyme and total ADH was significantly higher in the sera of BCa patients as compared to control group. Analysis of ALDH activity did not show statistically significant differences between the tested groups. Significantly higher total activity of ADH in comparison to control was found in both, low-grade and high-grade BCa group. The activity of ADH class I was also significantly higher in high-grade BCa group when compared to low-grade patients and controls. CONCLUSION: The increase of total ADH activity in the sera of BCa patients seems to be caused by isoenzymes released from cancerous cells. The higher activity of ADH I probably resulted from metastatic tumors as significant increase was detected only in the sera of high-grade bladder cancer patients.

Circulating Tumor Cells Expressing Markers of Tumor-Initiating Cells Predict Poor Survival and Cancer Recurrence in Patients with Pancreatic Ductal Adenocarcinoma.

Purpose: Circulating tumor cells (CTCs) have been identified in the blood of patients with pancreatic adenocarcinoma (PDAC), but little is known about the exact phenotype of these cells. We assessed expression of aldehyde dehydrogenase (ALDH), CD133, and CD44 as markers of CTCs with a tumor-initiating cell (TIC) phenotype in patients with PDAC and the relationship of this expression to patient outcomes.Experimental Design: Peripheral blood from 60 consecutive patients with PDAC undergoing surgical resection was obtained and processed using the Isolation by Size of Epithelial Tumor (ISET) method. Immunofluorescence was used to identify CTCs expressing cytokeratin, CD133, CD44, and ALDH.Results: Forty-seven patients (78%) had epithelial CTCs staining positive for pan-cytokeratin and at least one TIC marker. Forty-six patients (77%) had epithelial CTCs that labeled with antibodies to cytokeratin and ALDH. By separate analysis, 34 (57%) had cytokeratin-positive, CD133-positive, and CD44-positive (triple-positive) CTCs, whereas 40 (67%) had cytokeratin-positive, CD133-positive, CD44-negative CTCs. The remaining 13 patients did not have CTCs, as defined by cytokeratin expression. ALDH-positive CTCs and triple-positive CTCs were significantly associated with worse survival by univariate analysis, even when accounting for other significant prognostic factors (all, P ≤ 0.01). ALDH-positive CTCs, triple-positive CTCs, and dual cytokeratin- and CD133-positive CTCs were independent predictors of tumor recurrence by logistic regression analysis and associated with decreased disease-free survival (all, P ≤ 0.03).Conclusions: CTCs labeling with one or more markers of TICs are found in a majority of patients with PDAC and are independently predictive of decreased disease-free and overall survival. Clin Cancer Res; 23(11); 2681-90. ©2016 AACR.

The diagnostic significance of serum alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase activity in renal cell cancer patients.

OBJECTIVES: In previous experiments, we have found an increased level of class I ADH and total ADH activity in RCC tissues. Changes in cancer cells may be reflected by ADH activity in the serum and could thus be helpful for diagnostics of renal cancer. The aim of this study was to investigate a potential role of ADH and ALDH as tumor markers for RCC. MATERIAL AND METHODS: Serum samples were taken from 59 patients with RCC and 52 healthy subjects. Class III and IV of ADH and total ADH activity was measured by the photometric method. For measurement of class I and II ADH and ALDH activity, we employed the fluorometric method. RESULTS: The total activity of ADH and ADH I was significantly higher in the serum of patients with every stage of RCC compared to healthy subjects. The diagnostics criteria was higher for ADH I than for total ADH activity. The diagnostic sensitivity for ADH I was 73.36%, specificity 85.61%, predictive values of positive and negative results were 79.12 and 75.03% respectively. Area under ROC curve for ADH I was 0.748 and for total ADH 0.689. CONCLUSION: The results suggest a potential role of ADH I as a marker for RCC.

The Diagnostic Value of Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Measurement Sera of Cervical Cancer Patients.

AIM: The aim of this study was to investigate a potential role of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) as tumor markers for cervical cancer. MATERIALS AND METHODS: Blood samples were obtained from 43 women with cervical cancer. Isoenzymes class III, IV of ADH and total ADH activity were measured in the sera by the photometric method and class I, II ADH and ALDH activity by the fluorometric method. RESULTS: The total activity of ADH and ADH I was significantly higher in the serum of patients with cervical cancer than in control groups. The diagnostic sensitivity for ADH I was 61,76%, specificity 65,7%, PPV and NPV were 70 and 62,16% respectively. AUC for ADH I was 0,654 and for total ADH 0,618. CONCLUSION: The results suggest a potential role of ADH I as a marker for cervical cancer.

Exploring the heterogeneity of the hematopoietic stem and progenitor cell pool in cord blood: simultaneous staining for side population, aldehyde dehydrogenase activity, and CD34 expression.

BACKGROUND: The stem cell content in cord blood (CB) units is routinely assessed regarding nucleated cells, CD34+ cell count, and number of colony-forming units (CFUs). Efforts are made toward finding better ways of defining stemness of CB units. Side population (SP) phenotype and activity of aldehyde dehydrogenase (ALDH) are functional markers of stemness that can be assayed using flow cytometry. STUDY DESIGN AND METHODS: We have developed a protocol for simultaneous determination of CD34+, SP, and ALDH+ populations in relation to immature white blood cells (CD45dim) in CB. Viable nucleated cells were consecutively stained for SP and ALDH activity and with antibodies against the CD45, CD34, and CD117 antigens. RESULTS: The SP and ALDH+ populations could reliably be measured simultaneously. The median sizes of the SP and the ALDH+ populations were 0.85 and 3.3% of CD45dim cells, respectively. There was no overlap between the SP and ALDH+ populations. Cells that were ALDH+ expressed CD34 and CD117, but SP cells were negative for these markers. The ALDH+ cell content correlated with CD34+ cell content (p < 0.001) and with CFU-granulocyte-macrophage (GM; p = 0.03) but not with total CFUs. SP did not correlate with CD34+, CFU-GM, or total CFU. CONCLUSIONS: We show that simultaneous detection of the CD34, SP, and ALDH+ cells is clearly feasible using only small amounts of CB. In CB, ALDH+, and CD34+ cells are overlapping populations distinctly separated from the SP population. The difference in relation to the capacity for colony growth between ALDH+ and SP underlines that they define different cell populations.

The activity of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the sera of patients with brain cancer.

Human brain tissue contains various alcohol dehydrogenase (ADH) isoenzymes and possess also aldehyde dehydrogenase (ALDH) activity. In our last experiments we have shown that ADH and ALDH are present also in the brain tumour cells. Moreover the activities of total ADH and class I isoenzymes were significantly higher in cancer tissue than healthy cells. It can suggests that these changes may be reflected by enzyme activity in the serum of patients with brain cancer. Serum samples were taken for routine biochemical investigation from 62 patients suffering from brain cancer (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. A statistically significant increase of class I alcohol dehydrogenase isoenzymes was found in the sera of patients with brain cancer. The median activity of this class isoenzyme in the patients group increased about 24 % in the comparison to the control level. The total alcohol dehydrogenase activity was also significantly higher (26 %) among patients with brain tumour than healthy ones. The activities of other tested ADH isoenzymes and total ALDH were unchanged. The increase of the activity of total ADH and class I alcohol dehydrogenase isoenzyme in the sera of patients with brain cancer seems to be caused by the release of this isoenzyme from tumour's cells.

Serum ALDH1A1 is a tumor marker for the diagnosis of non-small cell lung cancer.

BACKGROUND: ALDH1A1 (aldehyde dehydrogenase 1 family, member A1) is highly expressed in non-small-cell lung cancer (NSCLC). We assessed the potential clinical value of serum ALDH1A1 in the diagnosis and prognosis of non-small-cell lung cancer. METHOD: Between 2010 and 2011, serum samples from 100 non-small-cell lung cancer patients before tumor resection, 60 patients with benign lung disease, and 60 healthy volunteers were collected and analyzed retrospectively for ALDH1A1, using sandwich ELISA. We further evaluated the serum and tumor ALDH1A1 levels of non-small-cell lung cancer patients before and after surgery. We compared the diagnostic and prognostic values of serum ALDH1A1 with that of carcinoembryonic antigen. RESULTS: Elevated serum ALDH1A1 levels were observed in 55 of the 100 (55%) non-small-cell lung cancer patients. The ALDH1A1 levels were much higher in patients with advanced stages than in those with early stage tumors. Of the 30 non-small-cell lung cancer patients who underwent surgery, 19 had elevated serum ALDH1A1 levels before surgery, but the serum ALDH1A1 level was undetectable by postoperative day 7. Analysis of receiver operating characteristic curves showed that ALDH1A1 might be better than carcinoembryonic antigen in distinguishing non-small-cell lung cancer from benign disease or the healthy control. Combined application of ALDH1A1 and carcinoembryonic antigen significantly increased the sensitivity of carcinoembryonic antigen alone, with an accuracy of 83%. CONCLUSIONS: Our results showed that serum levels of ALDH1A1 were correlated with carcinogenesis and progression of non-small-cell lung cancer. Detection of serum ALDH1A1 can be helpful in the diagnosis and prognosis of non-small-cell lung cancer. The diagnosis rate of non-small-cell lung cancer could be significantly improved when carcinoembryonic antigen is combined with ALDH1A1.

[Influence of dinitrosyl iron complexes on blood metabolism in rats with thermal trauma].

The dynamics in the oxidative and energy metabolism and enzyme systems of blood detoxification in animals with thermal trauma injected with dinitrosyl iron complexes was explored. The positive effect of dinitrosyl iron complexes on the state of blood pro- and antioxidant systems in animals with experimental thermal injury having profound oxidative stress is shown. This effect is observed as a considerable reduction of the intensity (normalization) of lipid peroxidation processes against significant elevation of antioxidant potential of blood plasma. This tendency was also fixed in erythrocyte membranes. It is also stated, that dinitrosyl iron complexes clearly normalized erythrocyte energy metabolism already by the 3rd day after trauma. In addition, infusions of dinitrosyl iron complexes caused marked stimulation of aldehyde dehydrogenase catalytic activity in burned rats via mechanism, associated with enzyme detoxification properties.

The diagnostic value of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase measurement in the sera of patients with endometrial cancer.

BACKGROUND/AIM: The aim of this study was to investigate the potential role of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) as tumor markers for endometrial cancer. PATIENTS AND METHODS: Serum samples were obtained from 40 women with endometrial cancer, 52 with myoma uteri and 52 healthy individuals. Class III, IV of ADH and total ADH activity was measured by a photometric method and class I, II ADH and ALDH activity, by a fluorometric method. RESULTS: The total activity of ADH and ADH class I was significantly higher in the serum of patients with endometrial cancer than in healthy individuals and patients with myoma. The diagnostic sensitivity for ADH I was 69%, specificity 77%, positive predictive value and negative predictive value were 75% and 71% respectively. The area under curve for ADH I was 0.682 and for total ADH was 0.623. CONCLUSION: The results suggest a potential role of ADH I as a marker for endometrial cancer.

The alcohol dehydrogenase isoenzyme (ADH IV) as a candidate tumour marker of esophageal cancer.

OBJECTIVE: Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in esophageal cancer cells. Moreover the total activity of ADH as well as the activity of class IV ADH isoenzyme is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is reflected in the sera and could thus be helpful for diagnostics of esophageal cancer. The aim of this study was to investigate a potential significance of ADH isoenzymes and ALDH as tumour markers of esophageal cancer. We defined diagnostic sensitivity, specificity, predictive value for positive and negative results, and receiver-operating characteristics (ROC) curve for tested enzymes. METHODS: Serum samples were taken for routine biochemical investigation from 180 patients with esophageal cancer before treatment. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline as a substrate and ALDH activity by a fluorometric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I and II isoenzymes we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was measured by a photometric method with formaldehyde and class IV with m-nitrobenzaldehyde as a substrate. RESULTS: There was a significant increase in the activity of class IV of ADH isoenzyme (7.65 mU/l vs 5.88 mU/l) and total ADH activity (1198 mU/l vs 848 mU/l) in the sera of esophageal cancer patients compared to the control. The diagnostic sensitivity for ADH IV was 72%, the specificity 76%, the positive and negative predictive values were 80% and 72% respectively. The area under the ROC curve for ADH IV was 0.65. CONCLUSION: The results suggest a potential significance of ADH IV as a marker of esophageal cancer.

Polymorphisms of alcohol dehydrogenase-1B and aldehyde dehydrogenase-2 and the blood and salivary ethanol and acetaldehyde concentrations of Japanese alcoholic men.

BACKGROUND: The effects of genetic polymorphism of aldehyde dehydrogenase-2 (ALDH2) on alcohol metabolism are striking in nonalcoholics, and the effects of genetic polymorphism of alcohol dehydrogenase-1B (ADH1B) are modest at most, whereas genetic polymorphisms of both strongly affect the susceptibility to alcoholism and upper aerodigestive tract (UADT) cancer of drinkers. METHODS: We evaluated associations between ADH1B/ADH1C/ALDH2 genotypes and the blood and salivary ethanol and acetaldehyde levels of 168 Japanese alcoholic men who came to our hospital for the first time in the morning and had been drinking until the day before. RESULTS: The ethanol levels in their blood and saliva were similar, but the acetaldehyde levels in their saliva were much higher than in their blood, probably because of acetaldehyde production by oral bacteria. Blood and salivary ethanol and acetaldehyde levels were both significantly higher in the subjects with the less active ADH1B*1/*1 genotype than in the ADH1B*2 carriers, but none of the levels differed according to ALDH2 genotype. Significant linkage disequilibrium was detected between the ADH1B and ADH1C genotypes, but ADH1C genotype did not affect the blood or salivary ethanol or acetaldehyde levels. High blood acetaldehyde levels were found even in the active ALDH2*1/*1 alcoholics, which were comparable with the levels of the inactive heterozygous ALDH2*1/*2 alcoholics with less active ADH1B*1/*1. The slope of the increase in blood acetaldehyde level as the blood ethanol level increased was significantly steeper in alcoholics with inactive heterozygous ALDH2*1/*2 plus ADH1B*2 allele than with any other genotype combinations, but the slopes of the increase in salivary acetaldehyde level as the salivary ethanol level increased did not differ between the groups of subjects with any combinations of ALDH2 and ADH1B genotypes. CONCLUSIONS: The ADH1B/ALDH2 genotype affected the blood and salivary ethanol and acetaldehyde levels of nonabstinent alcoholics in a different manner from nonalcoholics, and clear effects of ADH1B genotype and less clear effects of ALDH2 were observed in the alcoholics. Alterations in alcohol metabolism as a result of alcoholism may modify the gene effects, and these findings provide some clues in regard to associations between the genotypes and the risks of alcoholism and UADT cancer.

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.

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

BACKGROUND: The activity of total alcohol dehydrogenase (ADH) and class I isoenzymes is significantly higher in colorectal 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 diagnosing colorectal cancer. AIM: The aim of this study was to investigate a potential role of ADH and aldehyde dehydrogenase (ALDH) as tumor markers for colorectal cancer. We defined diagnostic sensitivity, specificity, positive and negative predictive values, and receiver-operating characteristics (ROC) curve for tested enzymes. METHODS: Serum samples were taken from 182 patients with colorectal cancer before treatment and from 160 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. RESULTS: There was significant increase in the activity of ADH I isoenzyme and ADH total in the sera of colorectal cancer patients compared to the control. The diagnostic sensitivity for ADH I was 76%, specificity 82%, AND positive and negative predictive values were 85 and 74%, respectively. The sensitivity and specificity of ADH I increased with the stage of the carcinoma. The area under ROC curve for ADH I was 0.72. CONCLUSION: The results suggest a potential role for ADH I as marker for colorectal cancer.

Circulating tumor cells with a putative stem cell phenotype in peripheral blood of patients with breast cancer.

The CD44(+)/CD24(-/low) and ALDH1(+) cell phenotypes are associated with stemness and enhanced tumorigenic potential in breast cancer. We assessed the expression of CD44, CD24 and ALDH1 on tumor cells circulating in the peripheral blood (CTCs) of patients with metastatic breast cancer using triple-marker immunofluorescence microscopy. Among a total of 1439 CTCs identified in 20 (66.7%) out of 30 patients, 35.2% had the stem-like/tumorigenic phenotype CD44(+)/CD24(-/low), whereas 17.7% of the CTCs analyzed in seven patients, were ALDH1(high)/CD24(-/low). In conclusion, we report the existence of a subpopulation of CTCs with putative stem cell progenitor phenotypes in patients with metastatic breast cancer.