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J. Biol. Chem., Vol. 255, Issue 23, 11081-11084, Dec, 1980
HH Freeze, AL Miller and A Kaplan
Acid hydrolases from mammalian sources contain phosphorylated
oligosaccharides which function as recognition markers for their
receptor-mediated endocytosis by human fibroblasts. The discovery that
glycopeptides derived from the slime mold, Dictyostelium discoideum,
contain mannose 6-phosphate led to the suggestion that acid hydrolases from
this source might also bear the marker. To test this hypothesis, the
binding and endocytosis of purified beta-D-glucosidase (EC 3.2.1.21),
beta-N-acetyl-D-hexosaminidase (EC 3.2.1.52), and alpha-D- mannosidase (EC
3.2.1.24) by human fibroblasts were investigated. These enzymes underwent
endocytosis with efficiencies of 8.6 to 60%/mg/h, and 1 mM mannose
6-phosphate markedly inhibited their uptake (80 to 100%). The specificity
of inhibition by sugar phosphates, the saturation kinetics of endocytosis,
and the binding properties of D. discoideum acid hydrolases were similar to
those reported for enzyme preparations derived from mammalian sources. In
addition, 95 to 100% of the beta-D- glucosidase or alpha-D-mannosidase
molecules from D. discoideum preparations were competent for in vitro
clearance. Furthermore, the three purified acid hydrolases contain 5 to 7
mol of mannose 6- phosphate/mol of enzyme. This indicates that, unlike many
mammalian enzyme preparations, most if not all of these enzyme molecules
from D. discoideum contain the phosphomannosyl recognition marker.
Acid hydrolases from Dictyostelium discoideum contain phosphomannosyl recognition markers
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