GSK-3 is a serine/threonine protein kinase that phosphorylate either threonine or serine, and this phosphorylation controls a variety of biological activities, such as glycogen metabolism, cell signaling, cellular transport, and others. GS inhibition by GSK-3β leads to a decrease in glycogen synthesis in the liver and muscles, along with increased blood glucose or hyperglycemia. This is why GSK-3β is associated with the pathogenesis and progression of many diseases, such as diabetes, obesity, cancer, and Alzheimer's disease. It is active in resting cells and is inhibited by several hormones such as insulin, endothelial growth factor, and platelet-derived growth factor. Insulin inactivates it by phosphorylation of the specific serine residues Ser21 and Ser9 in GSK-3 isoforms α and β, respectively. In a phosphatidylinositol 3-kinase-dependent way.