| Literature DB >> 569630 |
K Ullrich, G Mersmann, M Fleischer, K von Figura.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1978 PMID: 569630 DOI: 10.1515/bchm2.1978.359.2.1591
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888