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Molecular Biology of the IGF Binding Proteins

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Part of the book series: Contemporary Endocrinology ((COE,volume 17))

Abstract

In adult animals, 80–85% of insulin-like growth factor-I and -II (IGFs) circulate as 150-kDa ternary complexes. These ternary complexes are comprised of one molecule each of IGF, IGF binding protein-3 (IGFBP-3), the predominant IGFBP in serum, and an acid-labile subunit (ALS) (1). Serum also contains lower molecular weight complexes that are not fully saturated with IGFs. These complexes are comprised of the other smaller binding proteins (IGFBP-1, -2, -4, -5, and -6). These six IGFBPs are structurally related to each other (Fig. 1) and bind IGF-I and IGF-II with high affinity (2,3), but share no homology with the IGF receptors. These proteins, however, have different biochemical and biological characteristics that are due to differences in their primary structure. The present chapter summarizes current molecular information on the six IGFBPs and ALS (regulation of gene expression, cDNA, and gene organization). This summary, however, does not attempt to be encyclopedic, but rather to provide a general outline on the molecular aspects of the six high-affinity IGF-binding proteins, underlying their similarities and differences.

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Ooi, G.T., Boisclair, Y.R. (1999). Molecular Biology of the IGF Binding Proteins. In: Rosenfeld, R.G., Roberts, C.T. (eds) The IGF System. Contemporary Endocrinology, vol 17. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-712-3_6

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  • DOI: https://doi.org/10.1007/978-1-59259-712-3_6

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