الفهرس 
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Abstract
Insulin is a powerful anabolic hormone that exerts a diversity of effects on many types of cells. Most metabolic actions of insulin are enhancing of glucose uptake in adipocytes and skeletal muscles, activating glycogen synthesis in skeletal muscles, suppressing hepatic glucose production, and inhibiting lipolysis in adipocytes (Janus et al., 2016). After ingestion, insulin is secreted from the pancreas and provokes the uptake of circulating glucose in its target tissues by binding to an insulin receptor. This binding activates receptor autophosphorylation, which activates a downstream signaling cascade through the phosphorylation of tyrosine residues of the insulin receptor substrates (IRS-1 or IRS-2), followed by phosphorylation of phosphatidylinositol 3-kinase (PI3K), phosphoinositide dependent kinase-1, Protein kinase B (PKB, aslo known as AKT), protein kinase C (PKC) and mammalian target of rapamycin (mTOR), as well as ribosomal protein S6 kinase beta 1 (S6K1) (Janus et al., 2016). These actions result in an increased translocation of the glucose transporter 4 (GLUT4) to the membrane, thus facilitating glucose uptake (Bogan, 2012). After uptake, glucose 6-phosphate is produced by phosphorylation of glucose and subsequently enters different metabolic pathways (Zimmer, 1996).