“…Interfering with ER function activates the unfolded protein response (UPR), known as the ER stress response, which is a signal to recover ER function (Ma and Hendershot, 2004;Zhang and Kaufman, 2006;Rasheva and Domingos, 2009;White-Gilbertson et al, 2013). During ER stress, multiple signaling pathways are activated, including double-stranded RNA-activated protein kinase (PKR), the PKR-like ER kinase (PERK) and eukaryotic translation initiation factor 2 alpha (eIF2α), which suppress protein synthesis (Prostko et al, 1993;Teske et al, 2011). The UPR also activates synthesis of glucose-regulated protein 78 (GRP78), one of the endoplasmic reticulum chaperone molecules that can bind unfolded proteins and degrade misfolded proteins (Laitusis et al, 1999), and activation of transcription factors such as activating transcription factor (ATF6), inositol-requiring enzyme 1α (IRE1α), C/EBP homologous protein (CHOP), and caspase-12 (Urano et al, 2000;Yoshida et al, 2001;Lee et al, 2002;Back et al, 2006;Chung et al, 2011;.…”