Biology of IGF-1: Its Interaction with Insulin in Health and by Jamie Goode

By Jamie Goode

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Additional resources for Biology of IGF-1: Its Interaction with Insulin in Health and Malignant States (Novartis Foundation Symposia)

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I also have a comment with respect to pregnancy and cancer risk. There is a very slight increase in the risk of breast cancer in pregnancy and the ¢rst year after. But it is very low, and also it should be borne in mind that pregnancy doesn’t just involve one hormone. It is a totally homeostatic change so it is very di⁄cult to identify the factors involved. There is no doubt that this is related to a more rapid growth of cancers that were already present and not induction of new tumours. Carbone: I have a question regarding the NEJM paper correlating obesity with increased cancer risk (Calle et al 2003).

The Tyr-phosphorylated IR substrates function as signalling sca¡olds, providing a docking interface for proteins with Src-homology 2 (SH2) domains. Some of the SH2 proteins are enzymes, including the P-Tyr phosphatase SHP2 (SH-PTP2) and the cytoplasmic Tyr kinase Fyn. Other SH2 proteins, such as the p85 regulatory subunit of PI3K, Grb2 or APS function as adaptor proteins for 36 MOLECULAR BASIS OF INSULIN ACTION 37 downstream e¡ectors that further propagate the metabolic and growth-promoting e¡ects of insulin.

Shc can interact with the JM domain of IR through its PTB domain, while its SH2 domain binds the Tyr-phosphorylated CT domain of IR. Tyr-phosphorylated Shc serves as docking site for downstream e¡ectors having SH2 domains such as Grb2. The Ser/Thr phosphatase PP2A can also bind to the PTB domain of Shc and inhibit its interaction with IR. 38 ZICK domain functions as a binding site to the NPXY motif of the juxtamembrane (JM) region of IR, IGF-1R and other receptors (Wolf et al 1995). The C-terminal region of IRS proteins is poorly conserved.

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Biology of IGF-1: Its Interaction with Insulin in Health and by Jamie Goode
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