title: A histochemical study about changes in rat liver plasma membrane enzyme activities after galactosamine administration.
abstract: In rats changes in plasma membrane enzyme activities due to Gal-N intoxication were studied by enzymehistochemical methods. The bile canalicular 5'-nucleotidase and nucleoside polyphosphatase activities decreased; the sinusoidal 5'-nucleotidase remained unchanged. The bile canalicular leucyl-beta-naphthyl-amidase showed an increase in activity; the alkaline phosphatase activity remained unchanged. In contrast to the spotty necrosis, changes in plasma membrane enzyme activities were seen in all liver cells, suggesting that changes of these activities, occurring after Gal-N treatment, do not correlate with cell death. The conclusion was drawn that the deviations of the enzyme activities might be due to changes in the lipid environment of the enzyme proteins in the membrane. With the exception of alkaline phosphatase, partial hepatectomy caused the same changes in enzyme activities as did Gal-N intoxication. Nevertheless Gal-N administration to partial hepatectomized rats did not lead to hepatic necrosis. Galactose given simultaneously or within two hours after Gal-N prevented both changes in plasma membrane enzyme activities and hepatocellular damage. This suggests an important role of galactolipids and galactoproteins in the plasma membrane alterations.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D001653:Bile Ducts, Intrahepatic / Q000166:cytology; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology*; D005688:Galactosamine / Q000494:pharmacology*; D006498:Hepatectomy; D007931:Leucyl Aminopeptidase / Q000378:metabolism; D008099:Liver / Q000166:cytology* / Q000201:enzymology; D008297:Male; D009708:Nucleotidases / Q000378:metabolism; D051381:Rats
chemical_list: D005688:Galactosamine; D009708:Nucleotidases; D000469:Alkaline Phosphatase; D007931:Leucyl Aminopeptidase; D000251:Adenosine Triphosphatases