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Abstract

Based on long-existing evidence (reviewed in Ref. 1), it has been known that the insulin-like growth factors (IGF-I and IGF-II) bind with high affinity to two different cell surface receptors. The type I receptor binds IGF-I with high affinity. It also binds IGF-II with somewhat lower affinity, and insulin very weakly. It has a heterotetrameric structure (Fig. 1) very similar to that of the insulin receptor, with which it shares a striking primary sequence homology. Like the insulin receptor, it consists of two identical extracellular alpha chains that contain the IGF binding domain and two identical beta chains that span the cell membrane and whose cytoplasmic domain, like that of insulin, displays ligand-activated tyrosine kinase activity, believed to be important in the transmission of the biologic effects of the IGFs2.

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© 1989 Plenum Press, New York

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Polychronakos, C. (1989). The Insulin-Like Growth Factor-II/Mannose 6-Phosphate Receptor. In: LeRoith, D., Raizada, M.K. (eds) Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5685-1_31

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  • DOI: https://doi.org/10.1007/978-1-4684-5685-1_31

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