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1.
Postepy Hig Med Dosw ; 55(1): 113-20, 2001.
Article in Polish | MEDLINE | ID: mdl-11355526

ABSTRACT

The authors presented the aspects of diagnostics of alcohol dependence paying special attention to its laboratory and biochemical side. Biological sensitive and specific markers of alcohol dependence and abuse: N-acetyl-beta-hexosoaminidase, carbohydrate deficient transferrin and protein-acetaldehyde adducts were also presented.


Subject(s)
Alcoholism/diagnosis , Substance Abuse Detection/methods , Acetaldehyde/blood , Alcoholism/blood , Biomarkers/blood , Humans , Liver Function Tests , Sensitivity and Specificity , Transferrin/analysis , beta-N-Acetylhexosaminidases/blood
2.
Psychiatr Pol ; 34(3): 411-21, 2000.
Article in Polish | MEDLINE | ID: mdl-11055180

ABSTRACT

This article discusses biochemical changes of ethyl alcohol in human organism, concentrating especially on the negative influence on the metabolism of liver. The authors describe the process of oxidation of alcohol with alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) and emphasize the role of ADH i ALDH isoenzymes in creating individual tolerance of ethanol. Two other ways of ethanol metabolism are also presented. These are: microsomal ethanol oxidation system (MEOS) connected with cytochrome P-450 and peroxisome catalase system. The article also describes the influence of alcohol and its products of metabolism on the structure of liver proteins, on different metabolic processes taking place in this organ, and on the changes in the immunological system in the course of the alcoholic liver disease. Moreover, the authors present some information about the changes in histopathological picture of liver as the result of alcohol abuse.


Subject(s)
Alcoholism/metabolism , Ethanol/metabolism , Liver/drug effects , Liver/metabolism , Humans , Liver/pathology
3.
Acta Biochim Pol ; 46(4): 977-83, 1999.
Article in English | MEDLINE | ID: mdl-10824868

ABSTRACT

The activity of N-acetyl-beta-hexosaminidase was found to be significantly higher in the placentas collected after delivery from women in puerperium with symptoms of prolonged pregnancy or complicated by EPH gestosis, than in placentas from normal pregnancy. Isoelectrofocusing of placenta homogenates showed the presence of isoenzymes A, P and B of N-acetyl-beta-hexosaminidase. Different isoenzyme A patterns in homogenates were observed in placentas obtained from normal and prolonged pregnancies and in those complicated by EPH gestosis.


Subject(s)
Isoenzymes/metabolism , Pregnancy Complications/enzymology , beta-N-Acetylhexosaminidases/metabolism , Case-Control Studies , Female , Humans , Isoelectric Focusing , Placenta/enzymology , Pre-Eclampsia/enzymology , Pregnancy , Pregnancy, Prolonged/metabolism
4.
Rocz Akad Med Bialymst ; 40(1): 148-55, 1995.
Article in English | MEDLINE | ID: mdl-8528985

ABSTRACT

Exoglycosidases catabolize glycoconjugates (proteoglycans, glycolipids and glycoproteins) at a rate depending on tissue and pathological changes. We determined exoglycosidase activity in successive sections of alimentary tract, spleen, liver and kidney of rats subjected to hemorrhagic shock. We found significant difference in exoglycosidase activity between alimentary tract segments in control animals and no significant changes in homologous tissues of the shocked rats comparing with control.


Subject(s)
Digestive System/enzymology , Glycoside Hydrolases/metabolism , Shock, Hemorrhagic/metabolism , Animals , Female , Kidney/enzymology , Liver/enzymology , Rats , Rats, Wistar , Spleen/enzymology
5.
Acta Biochim Pol ; 42(3): 297-9, 1995.
Article in English | MEDLINE | ID: mdl-8588479

ABSTRACT

Inhibition by ethanol of the activities of lysosomal exoglycosidases in stomach, small intestine, liver and brain of rats exposed to cadmium (Cd2+) was determined. Out of the glycosidases tested the most distinct effect of Cd2+ and ethanol administered to the rats in vivo was observed in the small intestinal mucosa in a decreasing order: N-acetyl-beta-hexosaminidase, beta-galactosidase and alpha-fucosidase.


Subject(s)
Cadmium/toxicity , Ethanol/toxicity , Glycoside Hydrolases/metabolism , Animals , Brain/drug effects , Brain/enzymology , Drug Synergism , Glycoconjugates/metabolism , Glycoside Hydrolases/antagonists & inhibitors , Intestinal Mucosa/drug effects , Intestinal Mucosa/enzymology , Liver/drug effects , Liver/enzymology , Lysosomes/enzymology , Male , Mannosidases/antagonists & inhibitors , Mannosidases/metabolism , Rats , Rats, Wistar , Stomach/drug effects , Stomach/enzymology , alpha-L-Fucosidase/antagonists & inhibitors , alpha-L-Fucosidase/metabolism , alpha-Mannosidase , beta-Galactosidase/antagonists & inhibitors , beta-Galactosidase/metabolism , beta-N-Acetylhexosaminidases/antagonists & inhibitors , beta-N-Acetylhexosaminidases/metabolism
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