PubMed Health⌕ Search

Biomedical subjects

Lech Chrostek

Publications and source records attributed to Lech Chrostek.

At least 19 recordsLinked to original sources
PubMed2007

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

The metabolism of cancer is in many way different than in healthy cells. Increased metabolism of several carcinogenic substances may take place in cancer cells. The one of them was ethanol, that is oxidized by alcohol dehydrogenase (ADH) to high concentration of acetaldehyde, a toxic and carcinogenic compound. The enzyme responsible for oxidation of acetaldehyde is aldehyde dehydrogenase (ALDH). The aim of this study was to compare the capacity for ethanol metabolism measured by ADH isoenzymes and ALDH activity between gastric cancer and normal gastric mucosa. 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 used 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. The samples were taken surgically during routine operations of gastric carcinomas from 55 patients. The activities of total ADH, and the most important in gastric mucosa, class IV ADH were significantly higher in cancer cells than in healthy tissues. The other tested classes of ADH and ALDH showed a tendency toward higher activity in cancer than in healthy mucosa. The activities of all tested enzymes and isoenzymes were not significantly higher in men than in women in wither gastric cancer tissues or normal mucosa. The increased ADH IV activity may be 1 of the factors intensifying carcinogenesis by the increased ability to acetaldehyde formation from ethanol.

Acetaldehyde↗
PubMed2006

Serum level of sialic acid (SA) and carbohydrate-deficient transferrin (CDT) in type 2 diabetes mellitus with microvascular complications.

Sialic acid (SA) is responsible for the composition of different isoforms of transferrin and is reported to be a marker of microvascular complications in type 2 diabetes mellitus. Therefore, we explored the serum concentration of SA, and the less sialylated isoforms of transferrin, termed carbohydrate-deficient transferrin (CDT), in relation to the presence of microvascular complications in type 2 diabetes mellitus. We studied 21 patients with type 2 diabetes with microangiopathy and 22 patients without complications who were hospitalized at a diabetic clinic. The prevalence of microvascular complications was based on clinical history, fundoscopy, and laboratory tests. Blood samples were taken for measurements of SA, CDT, total transferrin, glucose, HbA1c, fibrinogen, C-reactive protein (CRP), and indicators of renal dysfunction (i.e., creatinine, urea, albumin excretion rate (AER), and glomerular filtration rate (GFR)). A rise in serum SA and a decrease in CDT concentrations were observed in both diabetic groups with and without complications, and there were no differences between the two groups of patients. There was a statistically significant correlation between serum SA and CDT in diabetic subjects with microvascular complications, but not in patients without such complications. This proves that the serum changes in CDT and SA levels in the course of type 2 diabetes mellitus are associated with each other in the presence of microangiopathy.

Adult↗
PubMed2006

Activity of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the sera of patients with breast cancer.

Numerous experiments have shown that alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) play a significant role in the metabolism of many biological substances. Some metabolic disorders that can lead to breast carcinogenesis may be the cause of changes in ADH and ALDH activity. In previous experiments we found a changed level of class I ADH activity in breast cancer tissues. The changed level of this enzyme in cancer cells may be reflected by the enzyme's activity in the serum. Therefore, in this study we measured the activity of ADH isoenzymes and ALDH in the sera of patients with breast cancer. Serum samples were taken for routine biochemical investigation from 45 women with breast cancer before treatment. Among all tested classes of ADH isoenzymes, only class I had higher activity in the serum of patients with breast cancer in stage IV. The total ADH and ALDH activities were not significantly higher in patients with breast cancer than in healthy controls. The changes in activity, especially in class I ADH, appear to be caused by isoenzymes being released from the organ damaged by metastatic disease.

Aged↗
PubMed2006

[New methods for the determination of transferrin isoforms in the diagnostics of alcohol abuse].

The new biochemical marker of chronic alcohol abuse are transferrin isoforms with a reduced number of sialic acids (asialo-, monosialo-, and disialotransferrin) called carbohydrate-deficient transferrins (CDTs). The usefulness of this indicator in the diagnostics of alcohol abuse has clearly been confirmed during the last years. The sensitivity and specificity of the CDT method as a marker of chronic alcohol abuse are higher than those found in commonly used tests. In routine analysis, CDTs have been assayed in the laboratories for ten years. Current CDT techniques allow for the determination of total CDT concentration (the absolute and/or relative amount) and provide the possibility of assaying its isoforms. In this paper the molecular structure of transferrin and different methods of CDT analysis are shown, with particular attention given to commercial tests. Analytical specificity and method-dependent (electrophoretic and chromatographic) reference values or cut-offs for serum CDT concentrations indicating chronic alcohol abuse are given in a table. Electrophoretic methods are characterized by higher selectivity (genetic variants) and higher sensitivity than chromatographic techniques. Isoelectric focusing, capillary electrophoresis, and high-performance liquid chromatography are used as the reference methods. Commercial procedures are based on transferrin saturation with iron followed by fractionation of protein (separating CDTs from non-CDT forms) by ion-exchange chromatography using microcolumns and a quantitative determination of CDT isoforms by immunological methods (radioimmunoassay, enzyme immunoassay, and turbidimetric immunoassay). Due to the different existing analytical methods, further standardization of CDT analysis and a redefinition of CDTs are necessary.

Alcoholism↗
PubMed2006

[Biochemical basic of alcoholic liver injury].

The liver is the main place of ethanol oxidation and is especially sensitive to the toxic effects of alcohol. Alcoholic liver disease is caused by chronic alcohol abuse. The article presents the negative effect of alcohol and its metabolites on the different biochemical processes in the liver.

Acetaldehyde↗
PubMed2005

The diagnostic accuracy of carbohydrate-deficient transferrin, sialic acid and commonly used markers of alcohol abuse during abstinence.

BACKGROUND: The normalization of alcohol abuse markers during the abstinence depends on the time since the last drinking. The aim of this study was to evaluate the diagnostic accuracy (area under the curve-AUC, sensitivity and specificity) of CDT, sialic acid and others biochemical and hematological markers of chronic alcohol abuse during abstinence. METHODS: We studied 75 patients admitted to the treatment of alcohol dependence. The blood samples were collected upon admission to the hospital. CDT was estimated using an immunoturbidimetric assay after anion-exchange chromatography and sialic acid by enzymatic colorimetric method. RESULTS: Mean values of all markers were significantly higher. All tests, except SA, negatively correlated with time of abstinence but not with age, duration of dependence and amounts of weekly alcohol consumption. The area under the curve (AUC) for all tested markers decreased progressively during the abstinence. The highest AUC was obtained for CDT (0.98) and the lowest for ALT (0.78) when alcohol was consumed in the last week. AUC for sialic acid was lower than of CDT but higher than of ALT. CONCLUSIONS: We conclude that the diagnostic accuracy for tested laboratory markers depends on the self-reported time of abstinence being the highest for CDT in the first week of abstinence. The accuracy of sialic acid was observed between GGT and ALT.

Adult↗
PubMed2005

Activity of enzymes with different subcellular localization in the blood plasma of patients with aortic aneurysm.

BACKGROUND: The wall of an abdominal aorta aneurysm shows increased activity of metalloproteinases, aspartyl cathepsins and cystein cathepsins, and decreased activity of inhibitors of these enzymes, as compared to the wall of a normal aorta. Parietal thrombi of the aneurysm also show marked proteolytic activity. The aim of our study was to determine the activity of secretory enzymes, membrane enzymes, cytosol enzymes, mitochondrial enzymes and lysosomal enzymes in the blood plasma of patients with abdominal aortic aneurysm. MATERIAL/METHODS: Blood for examinations was collected from 15 patients with abdominal aorta aneurysm without coexisting diseases, and from the same number of healthy subjects, to determine the activity of lactic acid dehydrogenase (LDH), 5' nucleotidase (5'NT), gamma-glutamyltranspeptidase (GGTP) and cholinesterase (ChE), alanine aminotransferase (ALT), aspartic aminotransferase (AST), cathepsin B (CB), cathepsin D (CD), and cathepsin L (CL). RESULTS: The plasma activity of ALT, AST and GGTP in the blood of patients with aortic aneurysm is lower than in the plasma of healthy subjects. The activity of LDH, 5'NT and ChE, CB and CL does not significantly differ in the plasma of patients with aortic aneurysm compared to the plasma of healthy subjects. The activity of CD is increased in the plasma of patients with aortic aneurysm. CONCLUSIONS: Determination of cathepsin D activity may be helpful in the diagnosis of aortic aneurysm.

Aged↗
PubMed2005

[Diagnostic value of total and lipid-bound sialic acid in malignancies].

Malignancies are the second cause of death among people after cardiovascular diseases. The early detection of tumors could increase the possibility of a favorable treatment outcome. Many biochemical tumor markers have become known during the last forty years, but each of them has some clinical limitations. Recently, the main attention of researchers is focused on tumor-derived compounds as possible markers of neoplasia. In this paper, the diagnostic value of serum total sialic acid (TSA) and lipid-bound sialic acid (LSA) has been summarized in malignant disease including the diagnosis, staging, prognosis and follow up of cancers. The clinical studies showed that TSA and LSA concentrations in serum were significantly elevated in different types of cancers compared to values of healthy people and with nonmalignant diseases. In the initial phase of malignant diseases, TSA and LSA as single tests for detection of cancers are not useful according to low diagnostic sensitivity. TSA and LSA concentrations in serum allow with some probability to assay the staging of cancer. LSA is more sensitive and specific test than TSA. Besides, serum TSA and LSA levels good reflect effectiveness of therapy. The decrease of concentration indicates on tumor regression (effective therapy) and the increase means the progression of disease (failing therapy). TSA and LSA can be useful biochemical indicators for staging, prognosis, monitoring of effectiveness treatment of cancers and early detection of recurrence or metastases, especially in combination with other tumor markers.

Biomarkers, Tumor↗
PubMed2004

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

Chronic ethanol consumption is associated with an increased risk for cancer of the colorectum. The highly toxic and carcinogenic compound is acetaldehyde, the product of ethanol metabolism. Ethanol is metabolized to acetaldehyde by alcohol dehydrogenase (ADH) in colorectal mucosa and bacteria. The enzyme responsible for oxidation of acetaldehyde is aldehyde dehydrogenase. The aim of this study was to compare ADH isoenzymes and ALDH activity in colorectal cancer with the activity in normal colonic mucosa. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline (NDMA) as substrate, and ALDH activity by a fluorometric method with 6-methoxy-2-naphthaldehyde as a substrate. For measurement of the activity of class I and II isoenzymes we employed fluorometric methods, with class-specific fluorogenic substrates. The activity of class III ADH was measured by the photometric method with n-octanol as substrate, and class IV with m-nitrobenzaldehyde as substrate. Samples were taken surgically during routine operations of colorectal carcinomas from 32 patients. The activities of total ADH and, the most important in colon mucosa, class I ADH were significantly higher in cancer than in healthy tissues. The other tested classes of ADH had a tendency to higher-level activity in cancer cells than in healthy mucosa. ALDH activity was not significantly lower in the cancer cells. The activities of all tested enzymes and isoenzymes were not significantly higher in drinkers than in nondrinkers both in colorectal cancer and in normal mucosa. The differences in activities of total ADH and class I isoenzyme between cancer tissues and normal colon mucosa might be a factor for metabolic changes and disturbances in low-mature cancer cells and, additionally, might be a reason for the higher level of acetaldehyde, which can intensify carcinogenesis.

Adenocarcinoma↗
PubMed2004

[Sialic acid as a new marker of excessive alcohol consumption].

Alcoholism is one of the most frequent addictions among people. The early identification of alcohol abuse could increase the possibility of a favorable treatment outcome and reduce health care costs. Many biochemical laboratory markers of alcohol abuse have been used for several years, but each of them has clinical limitations. Recently, sialic acid (SA) has been suggested as a new potential marker of excessive alcohol consumption. In this paper, the general characteristic of SA has been given including the usefulness in the identifying of alcohol abuse. The clinical studies showed that serum and saliva sialic acid concentration was significantly higher in female and male alcoholics compared to social drinkers. It has been established also, that the serum SA level in male alcoholics was significantly increased after a short period of relapse to heavy alcohol drinking. In addition, the serum SA level was significantly decreased during an alcoholism treatment and abstinence. Sialic acid seems to be interesting biochemical marker of alcohol abuse (detecting, monitoring) with the diagnostic efficiency as good as, or even better, than the traditional markers used today.

Alcohol Drinking↗
PubMed2003

Gender-related differences in hepatic activity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in humans.

Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which are most abundant in the liver, are the main enzymes involved in ethanol metabolism in humans. Gender-related differences in total liver ADH and ALDH activity among different animal species have been observed in many studies. We measured total ADH and ALDH activity, and the activity of class I-IV ADH in the livers of male and female patients. Total ADH and class I and II ADH activities were significantly higher in males than in females (P=0.0052, P=0.0074, P=0.020, respectively). Class III and IV ADH and total ALDH activities were not significantly different between the genders (P=0.2917, P=0.0590, P=0.2940, respectively). The results of our study clearly show that there is a difference in enzymatic activity between male and female patients for those isoenzymes that actively participate in ethanol oxidation in the liver (class I and II ADH), although the main form of ADH in this organ is class III ADH.

Adult↗
PubMed2003

Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the human pancreas.

Ethanol metabolism in the pancreas occurs predominantly by way of an nonoxidative pathway to fatty acid ethyl esters but oxidative routes to acetaldehyde also may contribute to injury of pancreatic cells. Three metabolic systems are responsible for the oxidative metabolism of ethanol, among which the cytochrome P-4502E1 and alcohol dehydrogenase have been found in the pancreas. The aims of this study were to detect ADH and ALDH in the human pancreas and to assess which ADH isoenzymes are present in this organ. ADH activity was measured by the photometric method and ADH isoenzyme activity was determined using sensitive and specific substrates. ALDH activity was measured by the fluorometric method. We have shown that the activities of ADH and ALDH are present in the pancreas, although the activity of ALDH was not proportionally as low as ADH activity. The class III isoenzyme exhibited the highest activity of all ADH isoenzymes tested and it was about 7 times higher than the activity of class I. The activities of classes II and IV were low. The activities of ADH isoenzymes of classes I, II, and III in the pancreas of men were significantly higher than in women. This study demonstrates that alcohol dehydrogenase and aldehyde dehydrogenase are present in the pancreas.

Adult↗
PubMed2003

[Alcohol and risk for the cancer].

Chronic alcohol consumption is associated with an increased risk for cancer especially of the upper aerodigestive tract and also liver, colorectum and breast. The role of ethanol alone and acetaldehyde in the etiology of many cancers is evident. The concentrations of ethanol and acetaldehyde after alcohol drinking depend on the activity of two main enzymes. The one is the alcohol dehydrogenase (ADH) and the next aldehyde dehydrogenase (ALDH). The different isoenzymes of ADH and ALDH genetically encoded have different catalytic properties. Therefore, the polymorphism of these enzymes might be an risk factor for cancer in the case of chronic alcohol consumption.

Alcoholism↗
PubMed2002

Activity of class I, II, III, and IV alcohol dehydrogenase isoenzymes in human gastric mucosa.

The gastric alcohol dehydrogenase (ADH) plays an important role in the "first pass" metabolism of ethanol. Human ADH exists in multiple forms, grouped into six classes and located in different tissues. In present study we investigated the activity of four classes (I, II, III, and IV) of alcohol dehydrogenase isoenzymes in the different parts of stomach (corpus and antrum) in patients with suspected gastric ulcer. The aim of the study was assess the particular role of different classes of ADH in the gastric dehydrogenase activity. For the measurement of the activity of class I and class II isoenzymes, we employed new fluorometric methods with specific 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, respectively. All biopsy specimens were taken from less changed areas of the antrum and body of the stomach of 68 patients suspected of having gastric ulcer. It was found that ADH IV (gastric) activity was the highest (14.76 +/- 0.68 in the corpus of the stomach in men; and 7.61 +/- 0.68 in women, respectively). The activity of the ADH III isoenzyme was lower than that of ADH IV. The activities of class I and II ADH isoenzymes were barely detectable. All tested classes of ADH had higher activity in the corpus than in the antrum and in males than in females. In conclusion, the most important form of gastric ADH is isoenzyme of class IV, less important is the isoenzyme of class III. ADH classes I and II seem to have no role in the stomach.

Adult↗