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Science 4 March 1988:
Vol. 239. no. 4844, pp. 1134 - 1137
DOI: 10.1126/science.2964083
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Articles

Science, Vol 239, Issue 4844, 1134-1137
Copyright © 1988 by American Association for the Advancement of Science

articles

A single receptor binds both insulin-like growth factor II and mannose-6-phosphate

RG MacDonald, Pfeffer SR, L Coussens, MA Tepper, CM Brocklebank, JE Mole, JK Anderson, E Chen, MP Czech, and A Ullrich

Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01655.

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 receptorCI), 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 125I-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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