A macrophage receptor for liver lysosomal beta-glucosidase.
beta-Glucosidase was purified from lysosomal membranes isolated from rat liver. Binding and uptake of the purified beta-glucosidase were mediated via an apparently single binding site on rat peritoneal macrophages. The number of sites and the Kd were 4.20 X 10(4)/cell and 1.00 X 10(-7) M, respectively. Neither of the processes was inhibited by ligands for mannose/fucose receptors, mannose 6-phosphate receptors, or scavenger receptors, or by other glycoproteins and sugar compounds. A portion of the beta-glucosidase taken up into the macrophages was degraded rapidly. These results suggested that liver lysosomal beta-glucosidase was endocytosed via a receptor not previously described.
Imai
K
K
Shimane Medical University, Department of Biochemistry, Japan.
D000818:Animals; D002241:Carbohydrates / Q000494:pharmacology; D005959:Glucosidases / Q000378:metabolism*; D006023:Glycoproteins / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008264:Macrophages / Q000378:metabolism*; D010529:Peritoneal Cavity / Q000166:cytology*; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism*; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*
D002241:Carbohydrates; D006023:Glycoproteins; D011956:Receptors, Cell Surface; D005959:Glucosidases; D001617:beta-Glucosidase