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The Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPS)

  • Chapter
Growth Hormone

Part of the book series: Endocrine Updates ((ENDO,volume 4))

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Abstract

Twenty years after the initial discovery of IGF (Salmon and Daughaday 1957) it was first realised that in the circulation, a huge proportion of IGF was bound to a “carrier protein” increasing its apparent molecular weight from 7.5kDa to between 50 and 150kDa (Zapf et al 1975). It wasn’t until 1989 that this carrier protein was analysed in detail and shown to comprise the predominant serum binding protein, now termed IGFBP-3 and an ∼85kDa, acid labile subunit (ALS) (Baxter and Martin 1989). To date there are now six specific IGF binding proteins named sequentially from IGFBP-1 to -6 according to their discovery in time and temporal publication of their sequences (See Shimasaki and Ling 1991 for review after IGFBPs 1–6 had been identified, Kim et al 1997 for more recent discussion on biological roles of all IGFBPs). In addition to this, there are other proteins with structural and possible functional homology to these proteins, which will be discussed later. Typically, the affinity of the intact binding proteins for IGF is higher than that of IGF for its receptor, resulting in a high concentration of systemic or locally produced IGF remaining effectively inactive. Therefore, the principle function of the binding proteins would appear to be to simply restrict the availability of IGF to its receptor, although this is achieved through a variety of mechanisms. In addition, tissue specificity can be grossly achieved through differences in expression of the various IGF binding proteins. Other means include not only changes in the absolute amounts of binding protein, but also in their post-translational modifications. The precise means of regulation at any one time can vary depending on physiological or pathological conditions. The following section will outline the individual binding proteins and our understanding of the role that they play in the modulation of IGF effects, as well as novel IGF independent actions. This review will concentrate on IGFBPs 1-6 as these are most fully characterised and have the highest affinity for IGF. Their role in various disease states will also be discussed.

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Authors and Affiliations

  1. Department of Medicine Division of Surgery, Bristol Royal Infirmary, University of Bristol, BS2 8HW, UK

    Jeff M. P. Holly & Janet K. Fernihough

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  1. Jeff M. P. Holly
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  2. Janet K. Fernihough
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Editors and Affiliations

  1. Sahlgrenska University Hospital, Göteborg, Sweden

    Bengt-Åke Bengtsson M.D.

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© 1999 Springer Science+Business Media New York

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Holly, J.M.P., Fernihough, J.K. (1999). The Insulin-Like Growth Factor (IGF) Binding Proteins (IGFBPS). In: Bengtsson, BÅ. (eds) Growth Hormone. Endocrine Updates, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5163-8_5

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  • DOI: https://doi.org/10.1007/978-1-4615-5163-8_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7351-3

  • Online ISBN: 978-1-4615-5163-8

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