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J. Biol. Chem., Vol. 262, Issue 1, 123-129, 01, 1987
B Hoflack, K Fujimoto and S Kornfeld
We have analyzed the interaction of phosphorylated oligosaccharides and
lysosomal enzymes with immobilized bovine liver cation-dependent
mannose-6-P receptor. Oligosaccharides with phosphomonoesters were the only
species that interacted with the receptor, and molecules with two
phosphomonoesters showed the best binding. Lysosomal enzymes with several
oligosaccharides containing only one phosphomonoester had a higher affinity
for the receptor than did the isolated oligosaccharides, indicating the
possible importance of multivalent interactions between weakly binding
ligands and the receptor. The binding of a mixture of phosphorylated
lysosomal enzymes to the cation- dependent Man-6-P receptor was markedly
influenced by pH. At pH 6.3, almost all of the lysosomal enzymes bound to
the receptor; whereas at pH 7.0-7.5, approximately one-third of the
material passed through the column, one-third interacted weakly, and
one-third bound tightly. The distribution of individual lysosomal enzyme
activities was similar to that of the total material. The species of
phosphorylated oligosaccharides present on the lysosomal enzymes which
interacted poorly with the receptor were similar to those found on the
tightly bound material and included species of oligosaccharides with two
phosphomonoester groups. Isolated oligosaccharides of this type bound to
the receptor over the entire pH range tested. These findings indicate that
at neutral pH the phosphorylated oligosaccharides on some lysosomal enzyme
molecules are oriented in a manner which makes them inaccessible to the
binding site of the cation-dependent Man-6-P receptor. Since the same
enzymes bind to the cation-independent Man-6-P receptor at neutral pH, at
least a portion of the phosphomannosyl residues must be exposed. We
conclude that small variations in the pH of the Golgi compartment where
lysosomal enzymes bind to the receptors could potentially modulate the
extent of binding to the two receptors.
The interaction of phosphorylated oligosaccharides and lysosomal enzymes with bovine liver cation-dependent mannose 6-phosphate receptor
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