Publications by authors named "Wojciech Jelski"

73 Publications

The comparison of total bile acid concentration and alcohol dehydrogenase activity as markers of intrahepatic cholestasis of pregnancy.

Acta Biochim Pol 2021 Nov 24. Epub 2021 Nov 24.

1Department of Biochemical Diagnostics, Medical University, Bialystok, Poland; 2Department of Neurodegeneration Diagnostics, Medical University, Bialystok, Poland.

Introduction: Intrahepatic cholestasis of pregnancy (ICP) is the liver disorder in the second or early third trimester of pregnancy. It is characterized by pruritus with increased serum bile acids concentration and other liver function tests. ICP is connected with increased risk of fetal mortality but is unfortunately detected quite late. Therefore, it is important to recognize the disease in its early stages. We aimed to investigate the serum alcohol dehydrogenase (ADH) activity and compare it with the concentration of total bile acid (TBA) in women with ICP.

Methods: Serum samples were taken for routine investigation from 80 pregnancies with ICP in the second or third trimester of pregnancy and from 80 healthy pregnant women at the same time of pregnancy. For measurement of class I activity, we used the spectrofluorometric methods. The total ADH activity was measured by the photometric method.

Results: The analysis of results shows a statistically significant increase in the activity of ADH I and ADH total (about 60% and 41.3%, respectively). Activity of ADH I correlated well with aminotransferases (alanine ALT and aspartate AST) and total bile acids (TBA) concentration. The total ADH activity was also positively correlated with ALT, AST and total bile acids.

Conclusion: We can state that the activity of class I alcohol dehydrogenase isoenzyme in the sera of patients with ICP is increased and seems to be a good indicator of liver cells destruction during this disease and is comparable with the value of other markers.
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http://dx.doi.org/10.18388/abp.2020_5841DOI Listing
November 2021

Molecular and Circulating Biomarkers of Brain Tumors.

Int J Mol Sci 2021 Jun 29;22(13). Epub 2021 Jun 29.

Department of Biochemical Diagnostics, Medical University, 15-269 Bialystok, Poland.

Brain tumors are the most common malignant primary intracranial tumors of the central nervous system. They are often recognized too late for successful therapy. Minimally invasive methods are needed to establish a diagnosis or monitor the response to treatment of CNS tumors. Brain tumors release molecular information into the circulation. Liquid biopsies collect and analyze tumor components in body fluids, and there is an increasing interest in the investigation of liquid biopsies as a substitute for tumor tissue. Tumor-derived biomarkers include nucleic acids, proteins, and tumor-derived extracellular vesicles that accumulate in blood or cerebrospinal fluid. In recent years, circulating tumor cells have also been identified in the blood of glioblastoma patients. In this review of the literature, the authors highlight the significance, regulation, and prevalence of molecular biomarkers such as O-methylguanine-DNA methyltransferase, epidermal growth factor receptor, and isocitrate dehydrogenase. Herein, we critically review the available literature on plasma circulating tumor cells (CTCs), cell-free tumors (ctDNAs), circulating cell-free microRNAs (cfmiRNAs), and circulating extracellular vesicles (EVs) for the diagnosis and monitoring of brain tumor. Currently available markers have significant limitations. While much research has been conductedon these markers, there is still a significant amount that we do not yet understand, which may account for some conflicting reports in the literature.
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http://dx.doi.org/10.3390/ijms22137039DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8268709PMC
June 2021

Serology in COVID-19: Comparison of Two Methods.

Int J Environ Res Public Health 2021 Jun 16;18(12). Epub 2021 Jun 16.

Department of Infectious Diseases, Neuroinfections Medical University in Bialystok, Żurawia 14, 15-540 Białystok, Poland.

Background: The aim of our study was to examine the performance of two assays in detecting SARS-CoV-2 antibodies.

Methods: A total of 127 COVID-19 disease contacts from the Infectious Diseases Department were included. Two serological tests were used: SARS-CoV-2 IgG CMIA on the Alinity system (Abbott) and LIAISON SARS-CoV-2 S1/S2 IgG CLIA (DiaSorin).

Results: The assays exhibited a 96.85% (123/127 patients) test result agreement. In two cases, the positive results obtained by SARS-CoV-2 IgG CMIA on the Alinity system (Abbott) were negative based on the LIAISON SARS-CoV-2 S1/S2 IgG CLIA (DiaSorin) test, and in two cases, negative results from the LIAISON SARS-CoV-2 S1/S2 IgG CLIA (DiaSorin) test were positive with the SARS-CoV-2 IgG CMIA on the Alinity system (Abbott).

Conclusions: Based on the results of our study, we conclude that in population medicine, the assessments of anti-SARS-CoV-2 antibodies after exposure to SARS-CoV-2 virus based on spike protein or nucleocapsid protein show comparable effectiveness.
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http://dx.doi.org/10.3390/ijerph18126497DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8296394PMC
June 2021

Activity of Alcohol Dehydrogenase and Aldehyde Dehydrogenase in Lung Cancer Cells.

Anticancer Res 2020 Jul;40(7):3857-3863

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

Background: The aim of this study was to define the alterations in the activity of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in normal and cancerous lung cells.

Materials And Methods: Lung tissues were taken from 36 patients during surgical resection of cancer. The activities of tested enzymes were measured by spectrofluorometric method (ADH I, ADH II, total ALDH) and photometric method (ADH III, ADH IV, total ADH).

Results: The activities of class II and III ADH were significantly lower in lung cancer cells compared to histologically normal lung tissue.

Conclusion: Reduced activity of isoenzyme class II ADH may affect disorders in retinoic acid biosynthesis, leading to its deficit. Lower ADH III activity may result in depletion of glutathione, and in initiation of oxidative stress, leading to cancer progression. These data suggest that alterations in ADH isoenzyme activities can contribute to carcinogenesis in human lungs.
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http://dx.doi.org/10.21873/anticanres.14375DOI Listing
July 2020

Biochemical Markers of Colorectal Cancer - Present and Future.

Cancer Manag Res 2020 22;12:4789-4797. Epub 2020 Jun 22.

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

According to a report by the National Cancer Institute, colorectal cancer (CRC) is one of the most common types of cancer worldwide. CRC is often recognized too late for successful therapy. Tumor markers have been sought for a number of years to detect the transformation of malignant cells at the earliest possible stage. They are usually proteins associated with a malignancy and might be clinically useful in patients with cancer. Several classical markers have been used to recognize colorectal cancer, including carcinoembryonic antigen (CEA), carbohydrate antigen (CA 19.9), tissue polypeptide specific antigen (TPS) and tumor-associated glycoprotein-72 (TAG-72). None of these tests, however, have excellent diagnostic accuracy. Recent studies have been conducted on the use of hematopoietic growth factors (HGFs) and various enzymes in the diagnosis and prognosis of colorectal cancer. These include macrophage-colony stimulating factor (M-CSF) and granulocyte-macrophage-colony stimulating factor (GM-CSF), interleukin-3, interleukin-6 and enzymes (alcohol dehydrogenase and lysosomal exoglycosidases). Significantly, most cancer deaths are not caused by the primary tumor itself but by its spread. Analysis of circulating cancer cells (CTCs), ie, factors responsible for metastasis, may be a source of information useful in the treatment of patients with colorectal cancer. Currently available markers have significant limitations.
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http://dx.doi.org/10.2147/CMAR.S253369DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7319530PMC
June 2020

Intrahepatic Cholestasis in Pregnancy: Review of the Literature.

J Clin Med 2020 May 6;9(5). Epub 2020 May 6.

Department of Biochemical Diagnostics, Medical University, 15-268 Bialystok, Poland.

Intrahepatic cholestasis of pregnancy (ICP) is the most common hepatic disorder related to pregnancy in women. It usually develops within the third trimester of pregnancy and presents with pruritus as well as elevated levels of bile acid and/or alanine aminotransferase. Clinical signs quickly resolve after delivery; however, there is a high risk of the disorder recurring in subsequent pregnancies. ICP is associated with an increased risk of perinatal complications (premature birth, respiratory disorders, even stillbirth). Elevated levels of gestational hormones and genetic predispositions are important factors for the development of ICP; among the latter, mutations in hepatobiliary transport proteins (multidrug resistance protein 3-MDR3, bile salt export pump- BSEP) play a major role. Clinical and biochemical symptoms of ICP include pruritus and increased levels of total bile acids (TBA). Serum levels of TBA should be monitored in ICP patients throughout the pregnancy as concentrations above 40 μmol/L, which define that severe ICP isassociated with an increased risk of fetal complications. Therapeutic management is aimed at reducing the clinical symptoms, normalizing maternal biochemistry and preventing complications to the fetus. Pharmacological treatment of intrahepatic cholestasis of pregnancy consists of the administration of ursodeoxycholic acid to lower the levels of TBA and possibly reduce pruritus. If the treatment fails, premature delivery should be considered.
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http://dx.doi.org/10.3390/jcm9051361DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7290322PMC
May 2020

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

Anticancer Res 2020 Apr;40(4):1997-2001

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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http://dx.doi.org/10.21873/anticanres.14155DOI Listing
April 2020

Biochemical diagnostics of pancreatic cancer - Present and future.

Clin Chim Acta 2019 Nov 17;498:47-51. Epub 2019 Aug 17.

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

Pancreatic cancer is one of the deadliest cancers having an exceptionally high mortality rate. Despite a relatively low incidence (10th among cancers), it is the fourth leading cause of cancer-related deaths in most developed countries. Improving early diagnosis of pancreatic cancer and strengthening the standardised comprehensive treatment remain the main focus of pancreatic cancer research. Tumor markers are usually tumor-associated proteins of clinical relevance in these patients. Although tumor markers carbohydrate antigen (CA 19-9) and carcino-embryonic antigen (CEA) are commonly used, neither demonstrate high diagnostic accuracy. Recently, hematopoietic growth factors (HGFs) and various enzymes have been reported as potential biomarkers for pancreatic cancer. These include macrophage-colony stimulating factor (M-CSF) and granulocyte-colony stimulating factor (G-CSF), interleukin-3 (IL-3), macrophage inhibitory cytokine (MIC-1) and various enzymes (alcohol dehydrogenase, aldehyde dehydrogenase, lysosomal exoglycosidases). With the development of molecular technology, detecting K-ras mutation in serum via polymerase chain reaction (PCR) is becoming more common and efficient. Because K-ras mutation rates are high in many cancers, some regard it as a potential tumor marker. Others have shown the value of serum miRNAs in detection of pancreatic cancer. Unfortunately, there are currently no effective methods of sufficient diagnostic accuracy to detect early-stage surgically resectable pancreatic cancer. In this article we highlight these biomarkers and summarise recent developments in the diagnosis and treatment of pancreatic cancer.
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http://dx.doi.org/10.1016/j.cca.2019.08.013DOI Listing
November 2019

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

Anticancer Res 2018 Jul;38(7):4005-4009

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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http://dx.doi.org/10.21873/anticanres.12688DOI Listing
July 2018

The Association Between Long-Term Acenocoumarol Treatment and Vitamin D Deficiency.

Front Endocrinol (Lausanne) 2018 4;9:226. Epub 2018 May 4.

Department of Family Medicine, Medical University of Bialystok, Bialystok, Poland.

Objective: Both vitamin D and K2 are involved in a number of metabolic processes, including bone metabolism; however, associations between the vitamins are not fully understood. The aim of the study was to evaluate serum concentrations of 25-hydroxyvitamin D [25(OH)D] in adult patients receiving long-term acenocoumarol (AC) treatment.

Participants And Methods: In this cross-sectional study, 58 Caucasian patients (31 women, 27 men) with a median age of 65 years receiving long-term AC therapy were evaluated and compared with 35 age- and gender-matched healthy controls. The AC treatment was used due to recurrent venous thromboembolism (34.5%), atrial fibrillation (31%), or mechanical heart valve prostheses (34.5%). Medical records and a questionnaire were used to obtain information about chronic diseases, smoking habits, and the duration of therapy and weekly dose of AC. Anthropometric measurements were performed, and serum concentration of 25(OH)D and total alkaline phosphatase (ALP) activity were measured.

Results: Among the 58 patients receiving long-term AC treatment, a high proportion (46.6%) demonstrated significant vitamin D deficiency with concentrations of 25(OH)D lower than 20 ng/mL. The median concentration of 25(OH)D in subjects receiving AC was significantly lower compared to the control group [20.4 (17.4; 26.1) vs. 28.2 (24; 32.7);  < 0.001]. No differences were found between women and men receiving AC therapy. In patients receiving AC, a negative correlation was found between the concentration of 25(OH)D and the weekly dose of AC ( = -0.337,  = 0.01). Patients with concentrations of 25(OH)D < 20 ng/mL were found to have a significantly higher median dose of AC, compared to those with concentrations of 25(OH)D ≥ 20 ng/mL [21 (17; 31) vs. 17 (12; 28);  = 0.045].

Conclusion: In conclusion, treatment with AC is associated with low 25-hydroxyvitamin D levels, although the path leading to this phenomenon is not entirely clear. Long-term administration of AC in adults may increase the risk of chronic vitamin D deficiency, thus, effective supplementation of vitamin D in these individuals needs careful consideration.
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http://dx.doi.org/10.3389/fendo.2018.00226DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5945821PMC
May 2018

The Activity of Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase in the Sera of Patients with Autoimmune Hepatitis.

Clin Lab 2018 Apr;64(4):477-481

Background: Autoimmune hepatitis (AIH) is a progressive inflammatory hepatopathy and an important cause of end-stage liver. The liver cells' destruction is reflected by increased activity of different enzymes in the serum. These enzymes include alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which play a significant role in the metabolism of many biological substances and exist mainly in the liver. In this study we investigated the activity of alcohol dehydrogenase and its isoenzymes and the total activity of ALDH in the sera of patients with autoimmune hepatitis.

Methods: Serum samples were taken for routine biochemical investigation from 32 patients with autoimmune hepatitis and from 40 healthy subjects. Class I and II of ADH and ALDH activity was measured by the spectrofluorometric method. For measurement of class III ADH and total ADH activity we employed the photometric methods.

Results: The activity of the class I ADH isoenzyme was significantly higher in the sera of patients with autoimmune hepatitis. The median activity of this isoenzyme in the patients group was approximately 63% (3.94 mU/L) higher than the control level (1.46 mU/L). For this reason, the total ADH activity was also significantly increased. The activities of other ADH isoenzymes and ALDH tested were unchanged.

Conclusions: The activity of total ADH and class I isoenzymes in the sera of patients with autoimmune hepatitis is increased, and it seems to be caused by the release of alcohol dehydrogenase from damaged liver cells.
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http://dx.doi.org/10.7754/Clin.Lab.2017.170925DOI Listing
April 2018

The Alcohol Dehydrogenase Isoenzyme as a Potential Marker of Pancreatitis.

Anticancer Res 2018 05;38(5):3019-3024

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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http://dx.doi.org/10.21873/anticanres.12556DOI Listing
May 2018

Activity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in sera of patients with hepatitis C.

Arch Med Sci 2018 Mar 7;14(2):281-287. Epub 2016 Jun 7.

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

Introduction: The changes of enzyme activity in the hepatocytes in the course of different liver diseases are reflected by increase of the corresponding enzyme activity in the plasma. For example, the activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) correlate with the severity of the condition during cirrhosis. In this study we measured the activity of ADH isoenzymes and ALDH in the sera of patients with hepatitis C.

Material And Methods: Serum samples were taken from 60 patients suffering from viral hepatitis C and from 66 control subjects. Total ADH activity and class III and IV isoenzymes were measured by the photometric method and ALDH activity, ADH I and II by the fluorometric method.

Results: The ADH activity was significantly higher in patients with hepatitis C than in healthy ( < 0.001). The total activity of ADH was 1284 mU/l in patients, and 745 mU/l (controls). The activity of isoenzymes classes ADH I and ADH II in the hepatitis C group increased respectively 55% (4.24 vs. 1.88 mU/l; < 0.001) and 47% (26.63 vs. 14.11 mU/l; < 0.001) in the comparison to the control. There was significant increase in the activity of ADH I isoenzyme (4.96 vs. 3.81 mU/l; < 0.001) and ADH total (1833 vs. 1105 mU/l; < 0.001) in patients with high viral load in comparison to patients with low viral load.

Conclusions: The activity of class I and II ADH isoenzymes in the sera of patients with hepatitis C is increased, and it seems to be caused by the release of these isoenzymes from damaged liver cells.
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http://dx.doi.org/10.5114/aoms.2016.60406DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5868663PMC
March 2018

The Activity of Class I-IV Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase in Bladder Cancer Cells.

Cancer Invest 2018 Jan 30;36(1):66-72. Epub 2018 Jan 30.

a Department of Biochemical Diagnostics , Medical University , Bialystok , Podlaskie , Poland.

Objectives: The aim of this study was to determine the differences in the activity of Alcohol Dehydrogenase (ADH) isoenzymes and Aldehyde Dehydrogenase (ALDH) in normal and cancerous bladder cells.

Methods: Class III, IV of ADH and total ADH activity were measured by the photometric method and class I, II ADH and ALDH activity by the fluorometric method.

Results: Significantly higher total activity of ADH was found in both, low-grade and high-grade bladder cancer, in comparison to healthy tissues.

Conclusion: The increased activity of total ADH in bladder cancer cells may be the cause of metabolic disorders in cancer cells, which may intensify carcinogenesis.
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http://dx.doi.org/10.1080/07357907.2017.1422511DOI Listing
January 2018

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

Anticancer Res 2017 09;37(9):4961-4965

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

Background/aim: The aim of this study was to investigate a potential role of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) as tumor markers for prostate cancer (PCa).

Materials And Methods: Serum samples were obtained from 52 patients with PCa, 34 patients with benign prostatic hyperplasia (BPH) and 60 healthy subjects. 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, ADH III and ADH IV were found in the sera of both, PCa and BPH patients compared with healthy individuals. The diagnostic sensitivity for ADH III activity was 94.2%, specificity 100%, PPV (positive predictive value) and NPV (negative predictive value) were 100% and 95.2% respectively. Area under receiver-operating characteristics (ROC) curve for ADH III activity was 0.993.

Conclusion: The results suggest a potential role of ADH III activity as a parameter included in the panel of markers for PCa.
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http://dx.doi.org/10.21873/anticanres.11906DOI Listing
September 2017

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

Adv Med Sci 2018 Mar 28;63(1):1-4. Epub 2017 Jul 28.

Department of Biochemical Diagnostics, Medical University of Białystok, Białystok, Poland.

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.
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http://dx.doi.org/10.1016/j.advms.2017.05.001DOI Listing
March 2018

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

Anticancer Res 2017 07;37(7):3537-3541

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

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.
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http://dx.doi.org/10.21873/anticanres.11722DOI Listing
July 2017

The diagnostic value of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) measurement in the sera of patients with brain tumor.

Arch Med Sci 2017 Mar 23;13(2):346-352. Epub 2017 Jan 23.

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

Introduction: Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) exist in the brain. Alcohol dehydrogenase and ALDH are also present in brain tumor cells. Moreover, the activity of class I isoenzymes was significantly higher in cancer than healthy brain cells. The activity of these enzymes in tumor tissue is reflected in the serum and could thus be helpful for diagnostics of brain neoplasms. The aim of this study was to investigate the potential role of ADH and ALDH as markers for brain tumors.

Material And Methods: Serum samples were taken for routine biochemical investigation from 115 patients suffering from brain tumors (65 glioblastomas, 50 meningiomas). For the measurement of the activity of class I and II ADH isoenzymes and ALDH activity, fluorometric methods were used. The total ADH activity and activity of class III and IV isoenzymes were measured by the photometric method.

Results: There was a significant increase in the activity of ADH I isoenzyme and ADH total in the sera of brain tumor patients compared to the controls. The diagnostic sensitivity for ADH I was 78%, specificity 85%, and positive and negative predictive values were 86% and 76% respectively. The sensitivity and specificity of ADH I increased with the stage of the carcinoma. Area under receiver-operating characteristic curve for ADH I was 0.71.

Conclusions: The results suggest a potential role for ADH I as a marker for brain tumor.
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http://dx.doi.org/10.5114/aoms.2017.65366DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5332462PMC
March 2017

Serum Alcohol Dehydrogenase and Aldehyde Dehydrogenase Activity in the Course of Hepatitis C.

Clin Lab 2016 Nov;62(11):2155-2159

Background: Hepatistis C virus (HCV) affects approximately 170 million people, and it is the leading cause of the chronic liver disease. The destruction of liver cells is reflected by an increase of different enzyme activities in the serum. These enzymes include alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which play a significant role in the metabolism of many biological substances and exist mainly in the liver. In this study we investigated the activity of alcohol dehydrogenase and its isoenzymes and the total activity of ALDH in the sera of patients with hepatitis C.

Methods: Serum samples were taken for routine biochemical investigations from 50 patients with hepatitis C and from 50 healthy subjects. The activity of class I and II ADH isoenzymes and ALDH activity were measured by spectrofluorometric methods. For the measurement of total ADH activity and activity of class III and IV isoenzymes, the photometric methods were used.

Results: The analysis of our results shows a statistically significant increase in the activity of ADH I and ADH II (2.5-fold and 2-fold, respectively). Activities of both classes of alcohol dehydrogenase isoenzymes have good correlation with alanine and aspartate aminotransferase. The observed increase in total alcohol dehydrogenase activity was not very high but confirmed the elevation of class I and II isoenzyme activity.

Conclusions: We can state that the activity of class I and II alcohol dehydrogenase isoenzymes in the sera of patients with hepatitis C is increased and it seems to be caused by the release of these isoenzymes from damaged liver cells.
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http://dx.doi.org/10.7754/Clin.Lab.2016.160401DOI Listing
November 2016

The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in the sera of bladder cancer patients.

Acta Biochim Pol 2017 8;64(1):81-84. Epub 2016 Oct 8.

Department of Biochemical Diagnostics, Medical University, Białystok, Poland.

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.
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http://dx.doi.org/10.18388/abp.2016_1289DOI Listing
April 2017

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

Anticancer Res 2016 May;36(5):2265-9

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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May 2016

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

Exp Mol Pathol 2016 06 14;100(3):416-20. Epub 2016 Apr 14.

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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http://dx.doi.org/10.1016/j.yexmp.2016.04.001DOI Listing
June 2016

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

Exp Mol Pathol 2015 Jun 14;98(3):403-6. Epub 2015 Mar 14.

Department of Biochemical Diagnostics, Medical University, Bialystok, Poland.

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.
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http://dx.doi.org/10.1016/j.yexmp.2015.03.012DOI Listing
June 2015

The alcohol dehydrogenase isoenzyme alcohol dehydrogenase IV as a candidate marker of Helicobacter pylori infection.

Arch Med Sci 2014 Oct 23;10(5):951-5. Epub 2014 Oct 23.

Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland.

Introduction: Helicobacter pylori infection is associated with decreased alcohol dehydrogenase (ADH) activity in the gastric mucosa. The decrease in gastric ADH activity depends on the severity of inflammation and mucosal injury. This damage can be a reason of the release of enzyme from gastric mucosa and leads to the increase of the ADH activity in the sera of patients with H. pylori infection.

Material And Methods: Serum samples were taken from 140 patients with H. pylori infection. Total ADH activity was measured by photometric method with p-nitrosodimethylaniline as a substrate and ALDH activity by the fluorometric method with 6-methoxy-2-naphtaldehyde. 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 ADH was measured by the photometric method with n-octanol and class IV with m-nitrobenzaldehyde as a substrate.

Results: The activity of ADH IV in the serum of patients with H. pylori infection increased about 42% (7.86 mU/l) in the comparison to the control level (4.52 mU/l). Total activity of ADH was 1105 mU/l in patients group and 682 mU/l in control. The diagnostic sensitivity for ADH IV was 88%, specificity 90%, positive and negative predictive values were 91% and 84% respectively. Area under ROC curve for ADH IV was 0.84.

Conclusions: Helicobacter pylori infection of gastric mucosa is reflected in the serum by significant increase of class IV and total ADH activity. The results suggest a potential role for ADH IV as a marker of H. pylori infection.
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http://dx.doi.org/10.5114/aoms.2014.46215DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4223140PMC
October 2014

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

Neurochem Res 2014 Dec 10;39(12):2313-8. Epub 2014 Oct 10.

Department of Biochemical Diagnostics, Medical University, Waszyngtona 15 A, 15-269, Bialystok, Poland,

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.
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http://dx.doi.org/10.1007/s11064-014-1402-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4246134PMC
December 2014

Salivary alcohol dehydrogenase in non-smoking and smoking alcohol-dependent persons.

Alcohol 2014 Sep 28;48(6):611-6. Epub 2014 Jun 28.

Department of Emergency Medicine and Disasters, Medical University of Białystok, ul. Szpitalna 37, 15-295 Białystok, Poland.

Increasing attention to the importance of saliva testing is not surprising because smoking and alcohol drinking act synergistically on oral tissues, and their metabolite levels, e.g., acetaldehyde, are much higher in saliva than in blood. The activity of salivary alcohol dehydrogenase (ADH) comes from oral microbiota, mucosa, and salivary glands. The purpose of this study was to investigate the involvement of ADH in the oral health pathology of smoking (AS) and non-smoking (ANS) alcohol-dependent males. The results indicated that the AS group had a more significant and longer duration (until the 30th day of alcohol abstinence) decrease in ADH activity and output than the ANS group (until the 15th day of alcohol abstinence) compared to controls (social drinkers; C). The decreased salivary flow (SF) in alcoholics was observed longer in the ANS group (until the 30th day of alcohol abstinence), whereas in the AS group SF normalized at the 15th day, probably due to the irritating effect of tobacco smoke on the oral mucosa. Because saliva was centrifuged to remove cells and debris (including microbial cells), the detected salivary ADH activity was derived from salivary glands and/or oral mucosa. A more profound and longer decrease in ADH activity/output in smoking than non-smoking alcoholics was likely due to the damaged salivary glands and/or oral mucosa, caused by the synergistic effect of alcohol drinking and smoking. The lower values of salivary ADH in smoking than non-smoking alcoholics might also be partly due to the reversed/inhibited ADH reaction by high levels of accumulated acetaldehyde.
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http://dx.doi.org/10.1016/j.alcohol.2014.04.003DOI Listing
September 2014

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

Acta Biochim Pol 2013 19;60(3):489-93. Epub 2013 Sep 19.

Department of Biochemical Diagnostics, Medical University, Białystok, Poland.

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.
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April 2014

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

Anticancer Res 2013 Sep;33(9):3725-30

Department of Biochemical Diagnostics, Medical University of Bialystok, Waszyngtona 15 A, PL 15-276, Bialystok, Poland.

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.
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September 2013

[Alcohol dehydrogenase - physiological and diagnostic Importance].

Postepy Hig Med Dosw (Online) 2013 Aug 27;67:901-7. Epub 2013 Aug 27.

Zakład Diagnostyki Biochemicznej Uniwersytetu Medycznego w Białymstoku.

Alcohol dehydrogenase (ADH) is a polymorphic enzyme, existing in multiple isoenzymes divided into several classes and localized in different organs. ADH plays a significant role in the metabolism of many biologically important substances, catalyzing the oxidation or reduction of a wide spectrum of specific substrates. The best characterized function of ADH is protection against excess of ethanol and some other exogenous xenobiotics and products of lipid peroxidation. The isoenzymes of alcohol dehydrogenase also participate in the metabolism of retinol and serotonin. The total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy organs (e.g. liver, stomach, colorectum). The changes in activity of particular ADH isoenzymes in the sera of patients with different cancers (especially of the digestive system) seem to be caused by release of these isoenzymes from cancer cells, and may play a potential role as markers of this cancer. The particular isoenzymes of ADH present in the serum may indicate the cancer localization. Alcohol dehydrogenase may also be useful for diagnostics of non-cancerous liver diseases (e.g. viral hepatitis, non-alcoholic cirrhosis).
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http://dx.doi.org/10.5604/17322693.1064330DOI Listing
August 2013

The activity of class I, II, III and IV of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in brain cancer.

Neurochem Res 2013 Jul 27;38(7):1517-21. Epub 2013 Apr 27.

Department of Biochemical Diagnostics, Medical University, Sklodowskiej-Curie 24 A, 15-276, Bialystok, Poland.

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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http://dx.doi.org/10.1007/s11064-013-1053-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671125PMC
July 2013
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