Carbohydrate-deficient transferrin depends on disease activity in rheumatoid arthritis and systemic sclerosis.

OBJECTIVES: Changes in the glycosylation of plasma proteins have been linked to the aetiology of the rheumatic diseases. The aim of this study was to determine and compare the levels of carbohydrate-deficient transferrin (CDT) in patients with rheumatoid arthritis (RA), systemic sclerosis (SSc), and systemic lupus erythematosus (SLE). METHOD: Studies were carried out in 29 female patients with RA, 27 with SSc, and 17 with SLE. CDT was assayed by the N Latex CDT immunonephelometric assay. RESULTS: The levels of %CDT in the sera of RA, SLE, and SSc patients were significantly higher than in controls while the absolute concentrations of CDT were unchanged. %CDT, CDT, and transferrin do not differ significantly between patients with rheumatic diseases. In RA and SSc patients, a positive correlation was observed between %CDT and C-reactive protein (CRP), as well as a positive correlation in RA patients between %CDT and 28-joint Disease Activity Score (DAS28). CONCLUSIONS: The changes in the serum %CDT concentration in patients with RA and SSc correlated with disease activity markers.

Relationship between CDT and disease activity in rheumatoid arthritis.

The aim of this study was to estimate the serum concentration of carbohydrate-deficient transferrin (CDT) in patients with rheumatoid arthritis (RA) and the relationship between the CDT level and disease activity in RA patients. Studies were carried out in 47 female patients with RA and 32 healthy women. Disease activity of RA was evaluated using the 28-joint count Disease Activity Score (DAS 28). Serum CDT was determined by particle-enhanced immunononephelometry using the N Latex CDT test. Patients with RA had significantly lower serum concentrations of CDT compared with controls. The correlation study showed the significant negative relationship between CDT and DAS 28 (r = - 0.483, p = 0.011). There were no correlations between serum CDT level and patient's age, disease duration, number of tender and swollen joints, and degree of disability evaluated by the Health Assessment Questionnaire. The level of CDT in patients with RA was significantly decreased and confirms the changes in transferrin glycosylation which are dependent on the disease activity. Therefore, measurement of CDT in the sera of patients with RA can be useful for the evaluation of disease activity in these patients.

Relationship between serum acute-phase proteins and high disease activity in patients with rheumatoid arthritis.

PURPOSE: The aim of this study was to assess the relationship between serum acute-phase proteins and high disease activity evaluated by activity score (DAS28) in patients with rheumatoid arthritis. MATERIAL/METHODS: Studies were carried out on 27 females with RA and 32 control women. Acute-phase proteins were divided into 4 fractions as follows: alpha1-globulins represented by alpha1-acid glycoprotein (AGP) and alpha1-antitrypsin (AAT); alpha2-globulins - haptoglobin (Hp); beta-globulins - complement C3 (C3) and total transferrin (Tf); gamma-globulins - C reactive protein (CRP), rheumatoid factor (RF) and immunoglobulin G (IgG), and determined by immunoturbidimetric methods. RESULTS: The serum levels of acute-phase proteins changed in RA patients. On account of the alterations of concentration, acute-phase proteins are placed in the downgrade scale as follows: CRP, Hp, AGP, C3, AAT and Tf. None of the acute-phase proteins correlated with the RF and the majority of them were closely related to ESR. Almost all of the acute-phase proteins (without C3) were closely related to RA activity (based on DAS28) and their places in the downgrade scale were as follows: CRP, Tf, AGP, Hp and AAT. The degree of disability evaluated by Health Assessment Questionnaire has affected on the concentrations of AGP, Tf and CRP. Serum AGP, AAT and RF levels significantly correlated with the patient's age. No correlations were observed between IgG, TP levels, and clinical data. CONCLUSIONS: Among the entire panel, the CRP and AGP appeared to be the most useful biochemical markers for evaluation of the disease activity of patients with RA.

Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with colorectal cancer.

Various isoenzymes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) exist in human colorectal mucosa. In our last experiments we have shown that ADH and ALDH are present also in colorectal cancer cells. Moreover the activities of total ADH and class I isoenzymes were significantly higher in cancer tissue than healthy mucosa. This may suggest that these changes may be reflected by enzyme activity in the serum. Therefore, we have measured the activity of total ADH, and classes I-IV of this enzyme and ALDH in the sera of patients suffering from this cancer. Total ADH activity was measured by a 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 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 formaldehyde and class IV with m-nitrobenzaldehyde as a substrate. Serum samples were taken for routine biochemical investigations from 52 patients with colorectal carcinoma before treatment. A statistically significant increase of class I ADH isoenzymes was found. Therefore the total ADH activity was also significantly increased. The total ALDH and the activity of other tested ADH isoenzymes were unchanged. We also observed the increasing tendency of ADH I activity in accordance with the advance of disease. The activity of class I ADH isoenzymes was elevated in the serum of patients with colorectal cancer. This activity was derived from colorectal cancer cells and probably from severely damaged liver by metastatic disease.

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.

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.

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.

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 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.

[Human aldehyde dehydrogenase (ALDH)]. / Dehydrogenaza aldehydowa (ALDH) czlowieka.

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.

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.

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.

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.

[Human gastric alcohol dehydrogenase]. / Ludzka zoladkowa dehydrogenaza alkoholowa.

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.

[Chylomicronemia syndrome complicating type 1 hyperlipoproteinemia with concomitant insulin-dependent diabetes]. / Zespól chylomikronemii w przebiegu hiperlipoproteinemii typu 1 z towarzyszaca cukrzyca insulinozalezna.

The case of chylomicronaemia syndrome complicating clinical course of type-1 hyperlipoproteinaemia and insulin-dependent diabetes is described. The patient required hypoglycaemic and lipid-lowering therapy.

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.

[Metabolism of ethyl alcohol in the human body]. / Metabolizm alkoholu etylowego w organizmie ludzkim.

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.

[CDT (desialylated transferrin)--a new biochemical marker of alcohol abuse]. / CDT (desialowana transferyna)--nowy biochemiczny marker naduzywania alkoholu.

Serum concentration of carbohydrate-deficient transferrin (CDT) is used for laboratory diagnosis of chronic alcohol abuse. Several earlier studies reported sensitivities of 90% or above for CDT, with a specificity of 90-100%, although other investigators found lower sensitivities. In general, CDT has been reported to be highly specific (92%) and relatively sensitive (80%) for the detection and monitoring of alcoholism. There are no correlation between CDT concentration and gamma-GT activity. Any alteration in serum total transferrin concentration markedly decreases the CDT assay specificity. This should be considered when interpreting the assay results in patients with elevated serum transferrin. There are differences between the CDT isoforms (asialo-Tf and monosialo-Tf) in males and females relative to alcohol consumption. Alcohol consumption increases the levels of asialo-Tf and monosialo-Tf in women more strongly than in men. Sensitivity of CDT assay is also related to age of patients. There is a significantly higher sensitivity of CDT in patients above 40 years of age as compared to younger patients. The measurement of carbohydrate-deficient transferrin may be used as a marker of excessive alcohol abuse in patients with liver diseases (also in cirrhosis). The specificity of CDT in patients with non-alcoholic liver disease was consistently higher than that of gamma-GT (80% vs 60%). Disulfiram therapy during detoxification does not influence the serum level of CDT.

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.