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Effect of swainsonine on rat epididymal glycosidases

Summary. Each epididymis of control and swainsonine-fed rats (5 µg/ml drinking water) was divided into 5 segments, and tissue, spermatozoa and sperm-free supernatants were prepared from each segment. When levels of 3 lysosomal glycosidases and total protein were determined, the proximal cauda contained the greatest concentration of each glycosidase. The specific-activity profile for β-glucuronidase and β-galactosidase was similar in swainsonine-fed and control rats. However, the concentration of -D-mannosidase in tissue of all segments was significantly greater in swainsonine-fed rats than in age-matched controls. Enzyme activity for -D-mannosidase after swainsonine treatment was significantly greater in spermatozoa from the caput, than in spermatozoa from the corpus and the cauda epididymidis. Since the -D-mannosidase activity was optimal at pH 4·5 and studies with highly specific antibody to lysosomal -D-mannosidase immunoprecipitated all of the -D-mannosidase present in detergent extracts of epididymal tissue, spermatozoa, and sperm-free supernatant, the enzyme studied is of lysosomal origin.

Keywords: epididymis; glycosidases; swainsonine; rat

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