The Nature and Regulation of the Receptors for Insulin-Like Growth Factors

The Nature and Regulation of the Receptors for Insulin-Like Growth Factors The two insulin-like growth factors IGF-I and IGF-II1 are chemically similar to each other as well as to insulin (60). The IGFs and insulin elicit the same biological responses (e.g. stimulation of fibroblast DNA synthesis and of adipose cell glucose metabolism), typically nonadditively, suggesting con­ vergence of their effector pathways. Competitive binding experiments showed that IGF receptors were distinct from insulin receptors ( 1 1, 26, IGF-II and in their reactivity with insulin 3 1) and that two SUbtypes of IGF receptors existed that differed in their affinity for IGF-I and (4 1,43). Although the receptors for IGFs and insulin preferentially bound the homologous ligand, insulin receptors also had weak affinity for IGFs, and one subtype of IGF receptor (type I) had a weak affinity for insulin. IFor simplicity, we will refer to IGF-I and IGF-II from human plasma as prototypes of the two the rat major families oflGFs. We consider IGF-I, somatomedin C (21), and basic somatomedin (2) to be chemically andlor homolog of IGF-II (25) functionally identical. MSA (multiplication-stimulating activity) is and functionally interchangeable with it. 0066-4278/85/0315-0425$02.00 RECHLER & NISSLEY Recently, covalent cross-linking of 12510dine-Iabeled IGFs to receptors has clearly established that the two subtypes of http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Physiology Annual Reviews

The Nature and Regulation of the Receptors for Insulin-Like Growth Factors

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Abstract

The two insulin-like growth factors IGF-I and IGF-II1 are chemically similar to each other as well as to insulin (60). The IGFs and insulin elicit the same biological responses (e.g. stimulation of fibroblast DNA synthesis and of adipose cell glucose metabolism), typically nonadditively, suggesting con­ vergence of their effector pathways. Competitive binding experiments showed that IGF receptors were distinct from insulin receptors ( 1 1, 26, IGF-II and in their reactivity with insulin 3 1) and that two SUbtypes of IGF receptors existed that differed in their affinity for IGF-I and (4 1,43). Although the receptors for IGFs and insulin preferentially bound the homologous ligand, insulin receptors also had weak affinity for IGFs, and one subtype of IGF receptor (type I) had a weak affinity for insulin. IFor simplicity, we will refer to IGF-I and IGF-II from human plasma as prototypes of the two the rat major families oflGFs. We consider IGF-I, somatomedin C (21), and basic somatomedin (2) to be chemically andlor homolog of IGF-II (25) functionally identical. MSA (multiplication-stimulating activity) is and functionally interchangeable with it. 0066-4278/85/0315-0425$02.00 RECHLER & NISSLEY Recently, covalent cross-linking of 12510dine-Iabeled IGFs to receptors has clearly established that the two subtypes of

Journal

Annual Review of PhysiologyAnnual Reviews

Published: Mar 1, 1985

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