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J. Biol. Chem., Vol. 263, Issue 6, 2585-2588, 02, 1988
PY Tong, SE Tollefsen and S Kornfeld
The bovine cation-independent mannose 6-phosphate receptor (CI-MPR) and the
human insulin-like growth factor II (IGF-II) receptor have recently been
shown to be 80% identical in their amino acid sequences as deduced from
cDNA clones (Morgan, D. O., Edman, J. C., Standring, D. N., Fried, V. A.,
Smith, M. C., Roth, R. A., and Rutter, W. J. (1987) Nature 329, 301-307).
We have studied the binding of IGF-II to affinity-purified CI- MPR in order
to obtain direct evidence that the same protein binds mannose
6-phosphate-containing ligands and IGF-II. In equilibrium binding studies,
the CI-MPR bound 0.95 mol of IGF-II/mol of receptor with a Kd of 0.2 nM.
The pH optimum of binding was 7.4. The addition of mannose 6-phosphate did
not affect binding, indicating that the two ligands interact with different
binding sites on the receptor. IGF-I bound to the receptor with a much
lower affinity (Kd of 0.4 microM), and insulin binding could not be
detected. IGF-II did not bind to the cation-dependent mannose 6-phosphate
receptor. We conclude that the cation-independent mannose 6-phosphate
receptor and the IGF-II receptor are the same protein.
The cation-independent mannose 6-phosphate receptor binds insulin-like growth factor II
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
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