Three ER transmembrane proteins, IRE1, PERK, and ATF6, sense ER stress in the ER lumen and become activated regulating a cascade of signaling pathways collectively termed the Unfolded Protein Response (UPR). Response categories of the Unfolded Protein Response. Studying ER stress and the UPR will help us understand the pathophysiology and develop novel therapeutic modalities for ER stress-related disorders. We will mainly focus on the tissue culture system. This chapter discusses the methods for measuring and quantifying ER stress levels, UPR activation and the subsequent downstream outcomes. Recent evidence further indicates that ER stress-mediated cell dysfunction and death is involved in pathogenesis of human chronic disorders including diabetes and neurodegeneraiton. However, if the UPR fails to reestablish the ER to normality, ER stress causes cell dysfunction and death. ER stress activates a complex signaling network referred as the Unfolded Protein response (UPR) to reduce ER stress and restore homeostasis. However, physiological and pathological stimuli can disrupt this ER homeostasis resulting to an accumulation of misfolded and unfolded proteins, a condition known as ER stress. In order for proteins to fold properly a balance between the ER protein load and the folding capacity to process this load must be established. The endoplasmic reticulum (ER) is a multifunctional organelle essential for the synthesis, folding, and processing of secretory and transmembrane proteins.
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