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, Axel Ullrich

Research output: Contribution to journalArticlepeer-review

291 Scopus citations


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 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 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.

Original languageEnglish (US)
Pages (from-to)1134-1137
Number of pages4
Issue number4844
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • General


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