Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
Inhibitory Effect of Ethanol and Colchicine on the Intracellular Processing of β-Glucuronidase Which Occurs in the Golgi Complex
Yukio NISHIMURAKeitaro KATOKimimitsu ODAMasaru HIMENO
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1995 Volume 18 Issue 7 Pages 938-944

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Abstract

To investigate the effect of ethanol or colchicine on the intracellular proteolytic processing of lysosomal β-glucuronidase, which is considered to occur in the Golgi complex in the intracellular sorting pathway, three rat liver Golgi subfractions, GF-1, GF-2, and GF-3, were isolated from ethanol-or colchicine-treated rats, and the electrophoretic patterns of the extracted Golgi β-glucuronidase on polyacrylamide gel were examined. The isolated Golgi subfractions from the drug-treated rats gave a better yield of fraction than that from the control rats. The enzymatic characterization of these three subfractions showed no significant contamination by other subcellular structures such as plasma membranes, microsomes, or lysosomes, and no inhibitory effect of the drugs was observed. On the other hand, suppressed galactosyltransferase activity, a marker enzyme of the Golgi complex, was detected in the colchicine-treated rats. The electrophoretic pattern of Golgi β-glucuronidase on polyacrylamide gel revealed one major band which moved to the same position as the lysosomal enzyme type in the control rats. In contrast, in the ethanol-and colchicine-treated rats, Golgi β-glucuronidase was found to have two major bands stained for enzyme activity resulting from a mixture of microsomal-and lysosomal-type enzymes. These results suggested that the post-translational modification step, during conversion from a microsomal-type enzyme to a lysosomal-type enzyme, was apparently inhibited. Taken together, these findings indicated that ethanol or colchicine administration to rats caused an inhibitory effect on the intracellular post-translational modification of Golgi β-glucuronidase destined for targeting to the lysosomes.

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