Recognition and receptor-mediated uptake of phosphorylated high mannose-type oligosaccharides by cultured human fibroblasts.
Open Access
- 1 March 1983
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 96 (3) , 915-919
- https://doi.org/10.1083/jcb.96.3.915
Abstract
The intracellular transport of newly synthesized lysosomal hydrolases to lysosomes requires the presence of one or more phosphorylated high mannose-type oligosaccharides per enzyme. A receptor that mediates mannose-6-PO4-specific uptake of lysosomal enzymes is expressed on the surface of fibroblasts and presumably accounts for the intracellular transport of newly synthesized enzymes to the lysosome. In this study, we examined the internalization of lysosomal enzyme-derived phosphorylated oligosaccharides by cultured human fibroblasts. Oligosaccharides of known specific activity bearing a single phosphate in monoester linkage were internalized with Kuptake of 3.2 X 10(-7) M, whereas oligosaccharides bearing two phosphates in monoester linkage were internalized with a Kuptake of 3.9 X 10(-8) M. Thus, phosphorylated high mannose-type oligosaccharides appear to be the minimal structure required for recognition and uptake by the fibroblast receptor. The finding that the Kuptake for monophosphorylated oligosaccharides is 100-fold less than the reported Ki for mannose-6-phosphate indicates that the fibroblast phosphomannosyl receptor contains a binding site that recognizes features of the oligosaccharide in addition to mannose-6-phosphate.Keywords
This publication has 30 references indexed in Scilit:
- Beta-glucuronidase binding to human fibroblast membrane receptors.Journal of Biological Chemistry, 1980
- Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues.Journal of Biological Chemistry, 1980
- Fibroblast receptor for lysosomal enzymes mediates pinocytosis of multivalent phosphomannan fragmentThe Journal of cell biology, 1980
- Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of beta-glucuronidase by human fibroblasts.Proceedings of the National Academy of Sciences, 1979
- Identification of mannose 6-phosphate in glycoproteins that inhibit the assimilation of β-galactosidase by fibroblastsProceedings of the National Academy of Sciences, 1979
- Direct demonstration of binding of a lysosomal enzyme, alpha-L-iduronidase, to receptors on cultured fibroblasts.Proceedings of the National Academy of Sciences, 1979
- Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages.Proceedings of the National Academy of Sciences, 1978
- Recognition and receptor-mediated uptake of a lysosomal enzyme, α-l-iduronidase, by cultured human fibroblastsCell, 1977
- Phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases by human fibroblasts.Journal of Clinical Investigation, 1977
- Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts.Proceedings of the National Academy of Sciences, 1977