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Receptor-mediated endocytosis of alpha-N-acetylglucosaminidase by cultured epithelial rat liver cells is inhibited by mannose, L-fucose and most effectively by mannose 6-phosphate. Endocytosis of alpha-N-acetylglucosaminidase is lost after treatment of the enzyme with alkaline phosphatase. These findings indicate that epithelial rat liver cells possess cell surface receptors that recognize a phosphorylated carbohydrate on alpha-N-acetylglucosaminidase, as was previously reported for cell surface receptors of human skin fibroblasts. Inhibition of alpha-mannosidase endocytosis by epithelial rat liver cells in the presence of mannose 6-phosphate and loss of enzyme endocytosis after treatment with alkaline phosphatase suggest that this enzyme is recognized by the same receptor.
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Ullrich et al. (1978) studied this question.
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