Effect of Chronic Ethanol Consumption on the Cellular and
Subcellular Distribution of γ-Glutamyltransferase in Rat Liver

Halsall, S.; Peters, T J

doi:10.1159/000469530

Enzyme

1984

DOI: 10.1159/000469530

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Effect of Chronic Ethanol Consumption on the Cellular and Subcellular Distribution of γ-Glutamyltransferase in Rat Liver

S. Halsall¹,

T J Peters²

Abstract: After 6 weeks of chronic ethanol consumption hepatic γ-glutamyl-transferase and -hydrolase activities increased compared with pair-fed controls. There was no change in 5'-nucleotidase activity. It was found that the increase in γ-glutamyltransferase activity occurred exclusively in the parenchymal cells although the principal cellular localisation for this enzyme is the biliary tract in both control and ethanol-fed rats. In both groups of animals the γ-glutamyltransferase activities were localised by analytica… Show more

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1986

1992

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Cited by 8 publications

References 20 publications

(32 reference statements)

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Gamma‐glutamyltransferase isoenzyme pattern in workers exposed to tetrachloroethylene

Gennari

Naldi

Motta

et al. 1992

American J Industrial Med

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In compliance with the mandatory medical surveillance of workers exposed to tetrachloroethylene (PCE) in Italy, isoenzyme fractioning of serum gamma-glutamyltransferase (GGT) was performed on 141 workers of both sexes and on 130 control subjects. None of the workers showed any clinical symptoms of liver disease and their enzymatic profiles, including AST, ALT, 5'-NU, ALP, and GGT, were within the normal reference limits. A statistically significant increase in total GGT serum level was found in the exposed subjects, which was associated with an increase in one of the two fractions normally present in healthy individuals (GGT-2), as well as with the appearance and progressive increase of the level of a fraction (GGT-4) considered to be an expression of hepato-biliary impairment. Further research is ongoing among these workers, which will clarify whether or not electrophoretic GGT tests may be useful in detecting liver function changes due to occupational exposure to PCE.

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Gamma‐glutamyltransferase isoenzyme pattern in workers exposed to tetrachloroethylene

Gennari

Naldi

Motta

et al. 1992

American J Industrial Med

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Mechanism of γ-glutamyl transpeptidase release in serum during intrahepatic and extrahepatic cholestasis in the rat: A histochemical, biochemical and molecular approach

et al. 1990

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The mechanism of the elevation of serum gamma-glutamyl transpeptidase activity in cholestasis is not clear. We therefore analyzed rat gamma-glutamyl transpeptidase activities in liver, bile and serum during intrahepatic cholestasis induced by a single dose of alpha-naphthyl isothiocyanate (20 mg/100 gm body weight) and during extrahepatic cholestasis after bile duct ligation. At days 1 and 2 after alpha-naphthyl isothiocyanate ingestion, we saw a fivefold and a 60-fold increase in serum and bile gamma-glutamyl transpeptidase activities, respectively. These increases were associated with a decrease in hepatic gamma-glutamyl transpeptidase activity and of corresponding mRNA. Simultaneously, necrosis of the biliary epithelium appeared in portal tracts. From day 2 to day 14, gamma-glutamyl transpeptidase activity in bile and serum progressively returned to basal levels; in the liver, cholangiolar proliferation was mild and was associated with moderate elevation of the gamma-glutamyl transpeptidase activity and of its corresponding mRNA. In extrahepatic cholestasis, a 10-fold increase in serum gamma-glutamyl transpeptidase activity was detected between day 0 and day 14. This increase was associated with major cholangiolar proliferation and with a progressive rise in hepatic gamma-glutamyl transpeptidase activity and in specific mRNA; in bile, gamma-glutamyl transpeptidase activity was slightly elevated. In these two models of cholestasis, histochemically detected gamma-glutamyl transpeptidase activity was largely predominant in biliary cells. We found no significant induction of gamma-glutamyl transpeptidase activity in hepatocytes. These results suggest that in these two models of cholestasis, the increase in serum gamma-glutamyl transpeptidase activity is of biliary cell origin and does not originate from hepatocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

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Subcellular fractionation of liver organelles from phenobarbital-treated rats by counter-current partition and sucrose gradient centrifugation

Morris

Smith

1986

Biochemical Pharmacology

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Effect of Chronic Ethanol Consumption on the Cellular and Subcellular Distribution of γ-Glutamyltransferase in Rat Liver

Cited by 8 publications

References 20 publications

Gamma‐glutamyltransferase isoenzyme pattern in workers exposed to tetrachloroethylene

Gamma‐glutamyltransferase isoenzyme pattern in workers exposed to tetrachloroethylene

Mechanism of γ-glutamyl transpeptidase release in serum during intrahepatic and extrahepatic cholestasis in the rat: A histochemical, biochemical and molecular approach

Subcellular fractionation of liver organelles from phenobarbital-treated rats by counter-current partition and sucrose gradient centrifugation

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