Recent Advances in Our Understanding of Insulin Action and Insulin Resistance
- 1 March 2001
- journal article
- review article
- Published by American Diabetes Association in Diabetes Care
- Vol. 24 (3) , 588-597
- https://doi.org/10.2337/diacare.24.3.588
Abstract
Insulin signaling at the target tissue results in a large array of biological outcomes. These events are essential for normal growth and development and for normal homeostasis of glucose, fat, and protein metabolism. Elucidating the intracellular events after activation of the IR has been the primary focus of a large number of investigators for decades, and for excellent reasons. Understanding the signaling pathways involved in insulin action could lead to a better understanding of the pathophysiology of insulin resistance associated with obesity and type 2 diabetes, and identifying key molecules and processes could lead to newer and more effective therapeutic agents for treating these common disorders. This review summarizes our previous understanding of how insulin acts and outlines some recent developments in our understanding of insulin action and insulin resistance at the cellular level, beginning with a discussion on the discovery of evolutionarily conserved molecules of the insulin signaling pathways. This article will also provide a summary of a few in vitro and cellular models of insulin resistance and a description of some new paradigms in the cellular mechanisms of insulin action. This review will not attempt to be all-inclusive; for a more comprehensive understanding, readers are referred to more complete reviews on insulin action (1–5).Keywords
This publication has 120 references indexed in Scilit:
- Cell Cycle and Hormonal Control of Nuclear-Cytoplasmic Localization of the Serum- and Glucocorticoid-inducible Protein Kinase, Sgk, in Mammary Tumor CellsJournal of Biological Chemistry, 1999
- Interaction of Insulin Receptor Substrate-1 (IRS-1) with Phosphatidylinositol 3-Kinase: Effect of Substitution of Serine for Alanine in Potential IRS-1 Serine Phosphorylation SitesEndocrinology, 1998
- daf-2 , an Insulin Receptor-Like Gene That Regulates Longevity and Diapause in Caenorhabditis elegansScience, 1997
- TNF -Mediated Inhibition and Reversal of Adipocyte Differentiation Is Accompanied by Suppressed Expression of PPAR without Effects on Pref-1 ExpressionEndocrinology, 1997
- Conformational Changes of the Insulin Receptor upon Insulin Binding and Activation As Monitored by Fluorescence SpectroscopyBiochemistry, 1997
- Activation of Protein Kinase C (α, β, and ζ) by Insulin in 3T3/L1 CellsJournal of Biological Chemistry, 1997
- Desensitization of Ras Activation by a Feedback Disassociation of the SOS-Grb2 ComplexJournal of Biological Chemistry, 1995
- Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects.Journal of Clinical Investigation, 1995
- mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer.Genes & Development, 1994
- Regulation of phosphatidylinositol 3-kinase activity in liver and muscle of animal models of insulin-resistant and insulin-deficient diabetes mellitus.Journal of Clinical Investigation, 1993