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L Chrostek

Publications and source records attributed to L Chrostek.

At least 19 recordsLinked to original sources
PubMed2006

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

Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) play a significant role in the metabolism of many biological substances. ADH participates in the metabolism of ethanol, retinoic acid, lipid peroxidation products, leukotriene and glutathione metabolism. ALDH is responsible for oxidation of acetaldehyde and other aldehydes and metabolism of histamine and retinoic acid. The aim of this study was to compare the metabolism in breast cancer cells and normal breast parenchyma by measuring ADH isoenzymes and ALDH activities in these tissues. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline (NDMA) as a substrate. For the measurement of the activity of ALDH and class I and II isoenzymes of ADH we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was detected by the photometric method with n-octanol and class IV with m-nitrobenzaldehyde as substrates. The samples were taken surgically during resection of breast carcinoma from 75 women. The activity of the class I ADH isoenzyme was significantly lower in breast cancer cells than in healthy tissues. The other tested classes of ADH had a tendency for higher levels of activity in cancer cells than in normal mammary tissue. The activity of total ADH and ALDH was also not significantly lower in the cancer cells. The decrease of activity of class I ADH isoenzyme in breast cancer tissues may be a factor of some disorders in metabolic pathways with participation of these isoenzymes that can lead to carcinogenesis.

Alcohol Dehydrogenase↗
PubMed2005

Carbohydrate-deficient isoforms of transferrin (%CDT) and sialic acid (SA) in iron-deficiency anemia.

This study has investigated the serum levels of carbohydrate-deficient isoforms of transferrin (CDT) and sialic acid (SA) in iron-deficiency anemia (IDA). Blood samples were collected from 60 women with IDA and from 20 healthy controls. CDT was estimated by anion-exchange chromatography on minicolumns followed by photometric detection of transferrin and was expressed as a percentage of total transferrin (%CDT). SA was measured by an enzymatic method. There was no difference in the mean level of %CDT between patients with IDA (2.26%) and control patients (2.05%). SA increased significantly from control level 0.61 to 0.69 g/l in anemic patients. We concluded that elevated concentration of total transferrin in IDA did not change the relative value of low sialylated isoforms (%CDT) and the increase of total SA level in the sera of anemic patients is not related to the increase of total transferrin.

Adult↗
PubMed2005

The effect of green tea on the activity of aldehyde dehydrogenase (ALDH) in the liver of rats during chronic ethanol consumption.

PURPOSE: Alterations in the redox state during chronic ethanol consumption are associated with the oxidation of ethanol via alcohol and aldehyde dehydrogenase. Among various antioxidants present in food, strong antioxidative effects have been attributed to polyphenols of green tea. The aim of the present study was to investigate the effect of green tea consumption during chronic ethanol intake on the activity of aldehyde dehydrogenase in the liver of rats during maturation and aging. MATERIALS AND METHODS: The activity of ALDH was measured in the livers of rats aged 2 (young), 12 (adult) and 24 months (old). The rats were fed with a control liquid Lieber DeCarli diet, control liquid diet containing green tea (3 g/l), ethanol liquid diet (with increasing ethanol dose from 2.3% to 7%) and ethanol liquid diet containing green tea. RESULTS: Chronic ethanol consumption significantly increased the liver ALDH activity in young and adult rats but decreased this activity in old animals. The drinking of green tea did not alter ALDH activity in ethanol-consuming rats. Drinking green tea alone significantly increased ALDH activity in young and adult rats but did not alter this activity in old rats. CONCLUSIONS: These results demonstrate that green tea administered during chronic ethanol consumption does not prevent the changes in the hepatic ALDH activity in the rats at each age.

Aldehyde Dehydrogenase↗
PubMed2002

Effect of Helicobacter pylori infection on the activity of class I, III and IV alcohol dehydrogenase in the human stomach.

BACKGROUND/AIMS: In the human stomach various alcohol dehydrogenase (ADH) isoenzymes exist. The gastric ADH activity is affected by a number of factors including also the infection of Helicobacter pylori. The objective was to investigate the activity of alcohol dehydrogenase isoenzymes of class I, III and IV in endoscopic specimens of gastric mucosa from the different parts of the stomach of men and women, considering the H. pylori infection. METHOD: Biopsy samples of gastric mucosa were taken from the corpus and antrum of 68 patients (42 of men and 26 of women) suspected for gastric ulcer. The colonization of H. pylori was present in 22 samples of men and 13 samples of women. The activity of class I isoenzyme was measured by the fluorimetric method with a specific substrate (4-methoxy-1-naphthaldehyde) and the activity of class III and IV by the photometric method with n-octanol and m-nitrobenzaldehyde as a substrates, respectively. RESULTS: In infected samples from the antrum and corpus of men's and women's stomachs the activity of class IV isoenzyme was decreased as compared to non-infected specimens. The activity of class III isoenzyme was decreased in the infected samples from the corpus of male patients, but the activity of class I does not significantly differ between infected and noninfected specimens from both sexes. CONCLUSION: H. pylori infection leads to significant decrease in the activity of class IV ADH in the stomach of men and women.

Alcohol Dehydrogenase↗
PubMed2001

Alcohol and aldehyde dehydrogenase activity measured with fluorogenic substrates in the liver of rats poisoned with methanol.

The effect of methanol poisoning of rats on the hepatic activities of enzymes metabolizing alcohols was evaluated. The activities of alcohol (ADH) and aldehyde dehydrogenase (ALDH) in the liver of rats dosed with 1.5 and 3 g of methanol/kg b.w. were measured with new fluorogenic substrates (4-methoxy-1-naphthaldehyde [MONAL-41] for ADH and 6-methoxy-2-naphthaldehyde [MONAL-62] for ADH and ALDH) after 6, 12 and 24 hours and 2, 5 and 7 days. The methanol intoxication led to a dose dependent induction of ADH and ALDH activities. The higher dose of methanol induced the activities measured with both MONAL-41 and MONAL-62 with the peak on day 5; its effect was largest on the activity of ADH measured with MONAL-41. Only ADH activity measured with this substrate was induced by the lower dose of methanol during the whole time of the experiment; the activity of ADH measured with MONAL-62 and that of ALDH were induced only on day 1 of the intoxication. It is evident that sublethal methanol intoxication induces the hepatic activities of ADH and ALDH measured with fluorogenic substrates, and this induction depends on the dose of this alcohol.

Alcohol Dehydrogenase↗
PubMed2001

Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol.

The activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured with fluorogenic naphthaldehydes in the stomach and small intestine homogenates of rats dosed with 6 g methanol/kg bw after 6, 12, 24 h and 2, 5, 7 days. After intoxication with a sublethal dose, the ADH activity measured with these naphthaldehydes and ALDH activities in the stomach and small intestine were significantly decreased. This inhibition is stronger in the stomach and probably depends on cell damage and protein denaturation. We conclude that the activity measured with 6-methoxy-2-naphthaldehyde (MONAL-62) may be due to the activity of rat ADH-1 isoenzyme, and the activity detected with 4-methoxy-1-naphthaldehyde (MONAL-41) to the activity of rat ADH-2 isoenzyme.

Alcohol Dehydrogenase↗
PubMed2001

[Human aldehyde dehydrogenase (ALDH)].

The paper presents the molecular and kinetics aspects of aldehyde dehydrogenase polymorphism. The role in acetaldehyde metabolism and differences in substrate specificity of isoenzymes are discussed.

Alcoholism↗
PubMed2000

The activity of class I and II alcohol dehydrogenase isoenzymes in the sera of patients with liver tumours.

We have measured the activity of class I and II alcohol dehydrogenase isoenzymes in the sera of patients with liver tumours, using class-specific fluorogenic naphthaldehydes as substrates. The activity of the tested isoenzymes was unchanged in primary tumours and significantly increased (class I) in metastatic liver tumours. The total enzyme activity was also increased (3-fold) in this group of patients. The elevated activity of class I isoenzymes in secondary tumours seems to be caused by the enzyme released from primary cells originating in the other organs, but increased total enzyme activity measured with chromogenic substrates may be proof of the presence of other classes of isoenzymes. These results show that the elevated class I isoenzymes and total enzyme activity in the sera of patients with liver tumours may indicate the metastatic origin of these tumours.

Adult↗
PubMed1999

Isoenzymes of class I and II alcohol dehydrogenase in chronic hepatitis.

Using class-specific fluorogenic substrates, the activities of class I and II alcohol dehydrogenase (ADH) isoenzymes were determined in the sera of patients with chronic hepatitis. The activity of the total alcohol dehydrogenase and indicator enzymes of liver damage were also investigated. We found a statistically significant increase of class I alcohol dehydrogenase isoenzymes in the total tested group which included those with the viral hepatitis. The (2-fold) increase in the activity of class I isoenzymes was similar to the increase of aminotransferases. The serum activity of class II isoenzymes was unchanged. Here an increase in total enzyme activity was not statistically significant. Class I isoenzymes and total enzyme activity correlated well with aminotransferases. These results demonstrate that serum activity of class I ADH measured with fluorogenic substrates confirms liver cell damage and may be useful in the diagnosis of chronic hepatitis.

Adolescent↗
PubMed1999

[Human gastric alcohol dehydrogenase].

A new form of alcohol dehydrogenase (class IV), designated mu-ADH or sigma-ADH, was identified in human stomach mucosa. We report here the enzymatic properties and molecular characterization of this human class IV and her contribution in ethanol and other biological substances metabolism.

Alcohol Dehydrogenase↗
PubMed1999

Distribution, activity and concentration of cathepsin B and cystatin C in the wall of aortic aneurysm.

Intensity of immunohistochemical reaction to cathepsin B is stronger and to cystatin C weaker in the wall of aortic aneurysm than in normal aorta. Localization of cathepsin B and cystatin C in the aneurysm wall is different from that in the control aorta, but activity and concentration of cystatin C in the aneurysmal wall is lower than in normal aorta. The parietal thrombus of aneurysm also shows high activity of cathepsin B. The obtained results point to participation of cathepsin B in degradation of aneurysmal structural proteins and in enlargement of the aneurysmal size.

Adult↗
PubMed1999

[Metabolism of ethyl alcohol in the human body].

More than 90% of ingested ethanol is metabolized in the body to acetaldehyde and acetate. Ethanol is metabolized in the liver via three distinct enzymatic pathways: alcohol dehydrogenase (ADH), the microsomal ethanol oxidizing system (MEOS) and catalase. It is generally accepted that alcohol dehydrogenase is the predominant pathway for hepatic ethanol oxidation. Acetaldehyde is metabolized to acetate by a group of dehydrogenase enzymes called aldehyde dehydrogenase.

Alcohol Dehydrogenase↗
PubMed1998

Serum activities of classes I and II alcohol dehydrogenases in toxic liver damage.

The activities of classes I and II alcohol dehydrogenase isoenzymes were determined in the sera of patients with toxic hepatitis using class-specific fluorogenic substrates. The activities of total alcohol dehydrogenase and enzymes indicative of liver damage were also measured. We found a statistically significant increase of class I alcohol dehydrogenase isoenzymes. The increase in class I (two-fold) was similar to the increase of alkaline phosphatase. In a correlated study, we observed a good correlation of the activity of class II isoenzymes with alanine aminotransferase. The total alcohol dehydrogenase activity was enhanced and correlated with lactate dehydrogenase. These results demonstrated that the alcohol dehydrogenase and class I isoenzymes are indicatory enzymes of liver cell damage, and may be diagnostically useful in toxic hepatitis.

Adult↗
PubMed1998

[Genetic evaluation of tolerance to alcohol].

Alcohol sensitivity which is genetically controlled changes the risk of alcoholic diseases development in such individuals. There are differences in the allelic frequencies of the ALDH2, ADH2 and ADH3 loci, between alcoholics and nonalcoholics. It was shown that the atypical ALDH2/2 is an alcohol-rejecting gene and the usual ALDH1/2 gene is a major "alcoholic" gene. The kinetic differences of ADH2 isozymes may also affect drinking behavior. In conclusion, genetic polymorphism of the ALDH and ADH genes influence the risk of alcoholism development. It may be possible to control alcoholism by suppression of "alcoholic" genes expression through genomic intervention.

Alcohol Dehydrogenase↗
PubMed1998

The activity of enzymes oxidizing alcohols in the liver of rats after methanol intoxication measured with fluorogenic substrates.

The activities of alcohol dehydrogenase isoenzymes (class ADH I and ADH II) and aldehyde dehydrogenase (ALDH) were measured using fluorogenic substrates in the liver of rats. Animals were dosed with 6 g of methanol/kg b.w. after 6, 12, 24 hours and 2, 5 and 7 days. Liver ADH I and ADH II activities were gradually increased after 6 h and up to 7 days after intoxication. ALDH activity in the liver had the highest elevation at 6 h, and then it decreased but was higher than the control value. It is concluded that subacute administration of methanol to rats leads to induction of hepatic enzymes involved in alcohols metabolism and that tested fluorogenic substrates are useful for these measurements.

Alcohol Dehydrogenase↗
PubMed1997

Activity of class I and II isoenzymes of alcohol dehydrogenase measured by a fluorometric method in the sera of patients with obstructive jaundice.

Using new fluorogenic substrates, we measured the activity of class I and II alcohol dehydrogenase (ADH) isoenzymes in the sera of patients with obstructive jaundice. The activity of class I isoenzymes was elevated two-fold, whereas that of class II isoenzymes was unchanged. This increase of class I isoenzymes explains low increase of total serum ADH activity. ADH isoenzymes and total enzyme activities correlated better with aminotransferases, than with alkaline phosphatase and gamma-glutamyltransferase, but we can conclude that class I ADH isoenzymes measured with fluorogenic substrates are indicative of obstructive jaundice.

Adult↗