Selective noncompetitive assimilation of bovine testicular beta-galactosidase and bovine liver beta-glucuronidase by generalized gangliosidosis fibroblasts.
Bovine liver beta-glucuronidase and testicular beta-galactosidase were assimilated by generalized gangliosidosis fibroblasts at respectively rates of 90 and 464 times the rate of assimilation of horseradish peroxidase. Assimilation of either of the two enzymes by the fibroblasts was saturable, suggesting the participation of receptor-mediated adsorptive endocytosis for internalization. The rate of assimilation of either enzyme was not affected by high levels of the other enzyme, suggesting that distinct receptors for each enzyme occur on the fibroblasts' cell surface. Furthermore, although assimilation of beta-galactosidase was inhibited by mannose, methyl mannosides, mannosyl alpha 1 leads to 2 mannose, and mannose-6-phosphate, these compounds did not detectably inhibit the assimilation of beta-glucuronidase. These results suggest that testicular beta-galactosidase was assimilated by the well-established phosphomannosyl recognition system. However, liver beta-glucuronidase was assimilated by a distinct, noncompeting, and as yet undefined, recognition system.
D000818:Animals; D002417:Cattle; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology; D005696:Galactosidases / Q000378:metabolism*; D005733:Gangliosidoses / Q000201:enzymology*; D005966:Glucuronidase / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D008358:Mannose / Q000031:analogs & derivatives / Q000494:pharmacology; D009928:Organ Specificity; D012867:Skin / Q000187:drug effects / Q000201:enzymology; D013045:Species Specificity; D013737:Testis / Q000201:enzymology; D001616:beta-Galactosidase / Q000378:metabolism*
D005696:Galactosidases; D001616:beta-Galactosidase; D005966:Glucuronidase; D008358:Mannose