1. Nat. Rev. Endocrinol. doi:10.1038/nrendo.2015.194
Figure 1 Potential sites of action of statins on cellular insulin action identified from in vitro studies
Figure 1 | Potential sites of action of statins on cellular insulin action identified from in vitro studies. Insulin receptor tyrosine kinase is activated by insulin, which results in the tyrosine phosphorylation of insulin receptor substrate 1 (IRS-1). The serine–threonine kinase AKT is subsequently activated, which facilitates the movement of storage vesicles containing glucose transporter type 4 (GLUT4) to the cell membrane. The transmembrane protein, GLUT4, enables glucose to enter the cell. Tyrosine phosphorylated IRS-1 has binding sites for key signalling proteins, including the p85 and p110 subunits of phosphatidylinositol 3-kinase, which through activation of the AKT and protein kinase 3 (PKC) cascades has a major role in insulin function. Activated AKT induces glycogen synthesis through inhibition of glycogen synthase kinase 3β (GSK3β), protein synthesis and cell survival by inhibiting Bcl-2-associated death promoter (BAD; a proapoptotic factor), forkhead box protein O1 (FOXO1; a transcription factor) and GSK3β. P, phosphate group; PI, phosphatidylinositol. Reprinted from Banach, M. et al. Statin therapy and new-onset diabetes: molecular mechanisms and clinical relevance. Curr. Pharm. Des. 19, 4904–4912 (2013) © with permission from Bentham Science.
Betteridge, D. J. & Carmena, R. (2015) The diabetogenic action of statins — mechanisms and clinical implications
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