By Morris F. White (auth.), Ashok K. Srivastava, Barry I. Posner (eds.)
In 1996 the seventy fifth anniversary of the invention of insulin used to be celebrated on the college of Toronto, the scene of that discovery in 1921. This quantity used to be influenced by means of the clinical software which was once staged at the moment and taken jointly a lot of the world's most sensible expertise to debate and research the newest advancements in our realizing of pancreatic functionality, insulin secretion, the interplay of insulin with its goal tissues, the mechanism of insulin motion on the mobile point, and the defects which underlie either kind I (insulin-dependent diabetes mellitus, IDDM) and sort II (noninsulin-dependent diabetes mellitus, NIDDM) varieties of the sickness. now we have selected to concentration the current quantity on paintings regarding insulin action.
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Extra resources for Insulin Action
Evidence as to the contribution of Ras-MAPK to the insulin regulation of the expression of genes encoding metabolic enzymes is insufficient at present to allow a general conclusion. In contrast, Ras is critical to insulin's ability to promote the differentiation of 3T3 Ll cells to adipocytes. The latter is not unexpected, as the control of cellular differentiation appears to be the most consistent function of the Ras protooncogene based on studies in cultured mammalian cells, as well as from genetic evidence in invertebrates.
Diacylglycl,rol binding directly activates PKC, although an intermediate phosphorylation may be required for some isoforms. Insulin receptor activation results in the GTP-charging of Ras which creates a high affinity ligand for the protein kinases of the Raf family. Once bound to Ras at the membrane, Raf undergoes further modification by one of several (SerlThr) or (Tyr) kinases, depending on the initiating stimulus. Insulin receptor activation also activates PI-3 kinase, which generates a variety of 3-0H phosphorylated Ptd Ins derivatives, each of which acts as a binding partner for a variety of protein kinases, including some PKC isoforms.
E. glucose or amino acids . The ability of insulin, acting on intact cells. to alter the activity of intracellular enzymes under conditIons where changes in the concentrations of the substrates and known allosteric regulators did not occur , together with experiments that suggested that insulin could induce these changes without entering the cell , pointed to the need to identify a mechanism by which signals generateJ at the cell surface could be conveyed to targets in the cell interior.
Insulin Action by Morris F. White (auth.), Ashok K. Srivastava, Barry I. Posner (eds.)