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A Single Receptor Binds Both Insulin-Like Growth Factor II and Mannose-6-Phosphate

Richard G. MacDonald, Suzanne R. Pfeffer, Lisa Coussens, Mark A. Tepper, Carol M. Brocklebank, John E. Mole, Jacqueline K. Anderson, Ellson Chen, Michael P. Czech and Axel Ullrich
Science
New Series, Vol. 239, No. 4844 (Mar. 4, 1988), pp. 1134-1137
Stable URL: http://www.jstor.org/stable/1700585
Page Count: 4
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A Single Receptor Binds Both Insulin-Like Growth Factor II and Mannose-6-Phosphate
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Abstract

Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II (IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptor$^{\text{CI}}$), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for $^{125}$I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P--containing proteins.

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