The changes in activities of some ammonia metabolizing enzymes in liver and brain of rats intoxicated by chronic administration of acetaldehyde.
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Biomedical subjects
Publications and source records attributed to R Farbiszewski.
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The data from literature on the mechanism of development and spread of malignant tumors and metastasis taking into account the role of growth factors produced by tumor cells and by blood platelets. The second part of this article describes platelet-aggregating activities of metastasizing tumour cells.
The latest observations suggest that a decreased level of serum branched-chain amino acids plays a role in the pathogenesis of liver encephalopathy. In this study we analysed the behaviour of the serum concentrations of: ammonia, phenols, alpha-amino nitrogen, tyrosine, phenylalanine and tryptophan in rats with thioacetamide-induced liver encephalopathy. The first group of rats was on protein-free diet and Aminosteril-Hepa (Fresenius FRG)--an amino acids solution with predominance of branched-chain amino acids. The second group of rats received a diet with 1 g/kg b.w. of protein daily. The levels of biochemical indices were analysed 0, 3, 5 and 7 days after liver encephalopathy development. The results of our study indicate a favourable influence of infusion a branched-chain amino acids solution (Aminosteril-Hepa) on the biochemical indices, particularly phenols and alpha-amino nitrogen in experimental liver encephalopathy.
The content of sulfhydryl compounds in proteins and non-proteins of plasma, liver and brain after acute and chronic administration of acetaldehyde (ACH) was investigated in rats. After ACH 1.5% w/v ingestion for 1 and 4 weeks (0.3 ml/kg) daily, proteins and non-proteins in plasma and liver were decreased significantly. After acute ACH administration SH-groups in brain proteins were not significantly decreased, but in the brain non-proteins these groups were increased significantly.
The changes in the activities of ammonia-metabolizing enzymes in liver and brain after ethanol intoxication has been investigated in rats. After administration of ethanol 30% (w/v) 6g kg-1 for 4 weeks we found an increase in liver glutamate dehydrogenase and glutaminase activity. In brain tissue the glutaminase activity was significantly higher and glutamate dehydrogenase was significantly lower. Glutamine synthetase activity in liver and brain was practically unchanged. The reasons for these changes in the activities of some ammonia-metabolizing enzymes in liver and brain after ethanol ingestion have been discussed.
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It has been found that cationic protein breakdown product--3H-L-arginine labelled peptide fraction--interacts with fibrinogen in the presence of thrombin. The formation of the fibrin clot under these conditions makes the clot resistant to the fibrinolytic action of plasmin.
The liver peptide fractions labelled with 3H-arginine after chronic administration of ethanol to rats have been analysed by gel filtration chromatography and tlc. Specific 3H-arginine radioactivity in the liver peptide fraction calculated per micrograms of alpha-amino nitrogen was significantly decreased by alcohol. The amount of peptide spots obtained by tlc in the ethanol-treated group was reduced in comparison with the control group. The findings suggest a change in the protein metabolism in hepatic dysfunction in rats receiving ethanol over a prolonged period.
The content of sulfhydryl compounds in proteins and non-proteins of plasma, liver and brain after acute and chronic ethanol administration was investigated in rats. After ethanol ingestion for 4 weeks (6 g/kg, day 30% w/v) significant changes were observed in plasma proteins and in liver proteins and non-proteins. In brain proteins and non-proteins we did not find any changes in sulfhydryl compounds content after acute and chronic ethanol administration.
With the use of 3H-arginine labelled cationic proteins derived from fibrosarcoma induced by methylcholanthrene it has been shown in studies in vitro that these proteins interact with fibrinogen under the influence of thrombin. The effect of this reaction depends on the concentration of cationic proteins. it was calculated that 1 mg of fibrinogen can be interacted with 2.5 micrograms of 3H-arginine labelled cationic proteins. The clinical role of cationic proteins appearing in circulation in malignancy have been discussed briefly.
The blood plasma peptide fractions labelled with 3H-leucine after chronic administration of ethanol or acetaldehyde in rats have been analysed. Total 3H-leucine radioactivity in peptide fraction calculated per millilitre of plasma in both study groups was significantly decreased. The amount of peptide spots obtained by tlc in the ethanol-treated group or acetaldehyde-treated group was reduced in comparison with the control group. Analysis of amino acid composition of atypical spots occurring in both test groups revealed the presence of aromatic amino acids and methionine, but was associated with the absence of branched-chain amino acids, such as valine, leucine and isoleucine. These findings suggest a change in protein metabolism in hepatic dysfunction in rats receiving ethanol or acetaldehyde.
The changes in the level and pattern of free amino acids in plasma and liver after ethanol or acetaldehyde intoxication has been investigated in rats. After administration of 30% (w/v) ethanol, 6 g kg-1, or 1.5% (w/v) acetaldehyde, 0.3 ml kg-1, for 4 weeks we found a decrease in plasma and liver branched-chain amino acids and an increase in plasma aromatic amino acids and methionine. The results are analogous to those found in studies of damaged liver.
The proteins binding and neutralizing the heparin of sarcoma induced by methylcholantrene are basic proteins. They are a mixture of at least three different proteins, possessing cathodic mobility in polyacrylamide gel electrophoresis of pH 2.7 and having a low molecular weight.
With the use of 3H-arginine it is shown that among soluble cytosol of fibrosarcoma, induced by 20-methylcholanthrene in rats there appear cationic proteins rich in arginine with content of amino acid of about 10%. The amount of these proteins in cytosol fraction is higher than in cytosol of another types of experimental tumors. The role of arginine-rich cationic proteins in cytosol fraction is briefly discussed.
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Low molecular weight ninhydrin positive peptide fractions of the Ehrlich tumour cell cytoplasm were isolated and characterized. After preliminary gel filtration of the cytoplasm on Sephadex G-25 column, the peptide mixture was fractionated on cationic exchanger SP-Sephadex C-25 column and eluted with increasing pH gradient. Five peaks were obtained. Only the first peak contained sugar component. All five peptides were studied with respect to molecular weight, isoelectric point and electrophoretic homogeneity. The cytoplasm of Ehrlich tumour cells contains one peptide of acidic (pI-5.0), two slightly basic (pI-7.7 and pI-7.7) and two strongly basic nature (pI-8.7 and pI-8.9). Molecular weights varied from 8 500 to 18 500 daltons. The origin of these peptides is briefly discussed.