By Jamie Goode
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Extra resources for Biology of IGF-1: Its Interaction with Insulin in Health and Malignant States (Novartis Foundation Symposia)
Its action is essential for growth, development, homeostasis of glucose, fat, and protein metabolism, and the proper function of pancreatic b cells (LeRoith & Zick 2001). At the molecular level, insulin binding to its transmembrane receptor (IR) stimulates the intrinsic Tyr kinase activity of the receptor (IRK) which then phosphorylates selected Tyr residues of target proteins. IR substrates include the three isoforms of Shc, IRS proteins (IRS1^6), p60dok, Cbl, APS and Gab-1 (LeRoith & Zick 2001, Zick 2001, Khan & Pessin 2002, Saltiel & Pessin 2002).
Protein tyrosine phosphatases (PTPs) also have a prominent role in the control of IR signalling. PTPs dephosphorylate the IR and its substrates and thus serve to terminate IR signalling. Several PTPs have been implicated in the negative regulation of insulin action. These include PTPIB and its close homologue TCPTP. For example, mice lacking PTP1B have increased insulin sensitivity and resistance to obesity induced by a high-fat diet (Elchebly et al 1999), while loss of TCPTP enhances IR activation (Galic et al 2003).
The main concern in administering GH, or other manipulations to raise IGF-1 levels, to counter the e¡ects of ageing, would then not be the risk of initiating new cancers, but what e¡ect this would have on the sub-clinical cancers that would normally not present before the individual dies of a cardiovascular incident. Modus operandi The two growth factors IGF-1 and IGF-2 are single polypeptides that share a high degree of homology with proinsulin. Their actions on cells are mediated by a classical transmembrane tyrosine kinase cell surface receptor.