In:
Biochemical Journal, Portland Press Ltd., Vol. 182, No. 2 ( 1979-08-15), p. 329-335
Abstract:
Cultured non-parenchymal rat liver cells internalize human urine α-N-acetylglucosaminidase, human skin β-N-acetylglucosaminidase and pig kidney α-mannosidase. Different heat-stabilities of endocytosed and endogenous α-mannosidase activity provided indirect evidence that the increase in intracellular activity resulted from uptake. The high efficiency and the saturation kinetics of uptake indicated that these enzymes become internalized by adsorptive endocytosis. Competition experiments with glycoproteins bearing known carbohydrates at their non-reducing terminals, with mannans, methyl glycosides and monosaccharides, established that the uptake of these three lysosomal enzymes is mediated by the binding to cell-surface receptors that recognize mannose and N-acetylglucosamine residues. The decreased uptake after treatment of these enzymes with either β-N-acetylglucosaminidase or α-mannosidase was in accordance with the results of the inhibition experiments. Removal of oligosaccharides of the high-mannose type by treatment with endoglucosaminidase H inhibited uptake almost completely, suggesting that the sugars recognized by cell-surface receptors of non-parenchymal liver cells are located in the outer core of these oligosaccharides. A comparison of the uptake of these three lysosomal enzymes by parenchymal and non-parenchymal rat liver cells indicates that infused α-N-acetylglucosaminidase is taken up preferentially by hepatocytes, whereas α-mannosidase and β-N-acetylglucosaminidase are localized predominantly in non-parenchymal rat liver cells.
Type of Medium:
Online Resource
ISSN:
0306-3283
Language:
English
Publisher:
Portland Press Ltd.
Publication Date:
1979
detail.hit.zdb_id:
1473095-9
