Abstract
The insulin-like growth factors (IGF) are present in the serum, other biological fluids and tissue extracts in association with high affinity binding proteins. Six members of this family of binding proteins have been identified and both rodent and human cDNAs encoding these proteins have been isolated. In serum from rodents and humans the majority of IGF is present as a complex of approximately 150-200 kDa. This complex is composed of IGF-I or IGF-II, a 100 kDa acid-labile protein and IGFBP-3. Under normal conditions only a small fraction of IGF-I or IGF-II in the plasma is free and there appears to be an excess of available binding sites for IGF. Although IGFBP-3 is responsible for the majority of the IGF binding capacity in the plasma, other binding proteins are also detectable in plasma and there is evidence that the different binding proteins serve to compartmentalize the IGFs into pools with different functional half-lifes and capacities1.
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Murphy, L.J., Barron, D., Seneviratne, C. (1994). Hormonal Regulation of Insulin-Like Growth Factor Binding Protein-1 Expression and the Development of Transgenic Mouse Models to Study IGFBP-1 Function. In: Le Roith, D., Raizada, M.K. (eds) Current Directions in Insulin-Like Growth Factor Research. Advances in Experimental Medicine and Biology, vol 343. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2988-0_27
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DOI: https://doi.org/10.1007/978-1-4615-2988-0_27
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