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Acid phosphatase and beta-glucosidase are unique among lysosomal enzymes in that they have both high mannose and complex type sugasr chains, whereas oligosaccharide chains of lysosomal enzymes in matrix are of high mannose type. We have previously shown that beta-glucosidase was endocytosed into macrophages via an unidentified receptor different from a mannose/fucose receptor (K. Imai, Cell Struct. Funct. 13, 325-332, 1988). Here, we show that uptake of acid phosphatase purified from rat liver lysosomes into rat macrophages was inhibited by ligands for a mannose/fucose receptor and was mediated via an apparently single binding site with Kuptake of 24.7 nM. These results indicate that acid phosphatase and beta-glucosidase recognize different types of receptors even if they have similar sugar chains. Polyvalent concanavalin A which binds both to the enzyme and to macrophages specifically stimulated the uptake in a dose dependent manner, whereas wheat germ agglutinin and phytohaemagglutinin did not.
K Imai, and
T Yoshimura
March 1979,
Biochimica et biophysica acta,
K Imai, and
T Yoshimura
June 1992,
European journal of cell biology,
K Imai, and
T Yoshimura
February 1992,
Current opinion in immunology,
K Imai, and
T Yoshimura
January 2009,
Biological chemistry,
K Imai, and
T Yoshimura
March 1968,
Archives of biochemistry and biophysics,
K Imai, and
T Yoshimura
June 1971,
Comptes rendus des seances de la Societe de biologie et de ses filiales,
K Imai, and
T Yoshimura
January 1970,
Protoplasma,
K Imai, and
T Yoshimura
February 1984,
The Biochemical journal,
K Imai, and
T Yoshimura
May 1967,
Toxicology and applied pharmacology,
K Imai, and
T Yoshimura
June 1989,
Cell,
