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Analysis of the interaction of IGF-I analogs with the IGF-I receptor and IGF binding proteins
1Department of Molecular Pharmacology and biochemistry, Merck Research Laboratories, Rahway, NJ 07065.
Distinct domains of IGF-I are important for maintaining high affinity for the IGF-I receptor and for the various species of IGFBPs. The analogs that selectively bind the receptor have proven useful in determining the relative importance of IGFBPs in the regulation of the biological activity of IGF-I. Analogs with poor affinity for the receptor have also been useful in order to demonstrate that a given activity of IGF-I is mediated by the type 1 IGF receptor. These studies confirm that the role of these various proteins in IGF-I action is complex, and may be cell or tissue-type specific.
Distinct domains of IGF-I are important for maintaining high affinity for the IGF-I receptor and for the various species of IGFBPs. The analogs that selectively bind the receptor have proven useful in determining the relative importance of IGFBPs in the regulation of the biological activity of IGF-I. Analogs with poor affinity for the receptor have also been useful in order to demonstrate that a given activity of IGF-I is mediated by the type 1 IGF receptor. These studies confirm that the role of these various proteins in IGF-I action is complex, and may be cell or tissue-type specific.