Fig. 6
From: Cardioprotective role of SIRT1 activation on mitochondrial function in insulin-resistant H9c2 cells
Cellular alterations in palmitic acid (PA)-induced insulin resistance model in H9c2 cells. Insulin-resistance markedly increased the acetylation of lysine residues in peptide chains (Hyper K-Acetylation). Hyper K-Acetylation caused mitochondrial dysfunction which was reflected in mitochondrial fragmentation, lowered ATP production, and mitochondrial membrane (ΔΨm) depolarization. Parallelly K-acetylation increased cellular oxidative stress which affected the levels of ROS and RNS. Cellular ionic homeostasis was impaired. Intracellular free zinc ([Zn2+]i) and free calcium ([Ca2+]i) concentrations were increased. All these alterations caused increased apoptosis and impaired contractile function both of which are hallmarks of cardiac dysfunction. SIRT1 is one of the major regulators of intracellular K-acetylation levels. EX527 was used as an inhibitor, and SRT1720 as an activator of SIRT1