Methods for Monitoring Endoplasmic Reticulum Stress and the Unfolded Protein Response. (19th January 2010)

• Record Type: Journal Article
• Authors: Samali, Afshin; FitzGerald, Una; Deegan, Shane; Gupta, Sanjeev
• Other Names: Hori Osamu Academic Editor.
• Is Part Of: International journal of cell biology. Volume 2010(2010)
• Publication Date: 2010-01-19
• Subjects: Cytology -- Periodicals; Cell Biology; Cytology; Periodicals; Electronic journals -- Sciences; Electronic journals -- Biology; Periodicals; 571.6
• DOI: 10.1155/2010/830307
• Languages: English
• ISSNs: 1687-8876

Abstract

Abstract : The endoplasmic reticulum (ER) is the site of folding of membrane and secreted proteins in the cell. Physiological or pathological processes that disturb protein folding in the endoplasmic reticulum cause ER stress and activate a set of signaling pathways termed the Unfolded Protein Response (UPR). The UPR can promote cellular repair and sustained survival by reducing the load of unfolded proteins through upregulation of chaperones and global attenuation of protein synthesis. Research into ER stress and the UPR continues to grow at a rapid rate as many new investigators are entering the field. There are also many researchers not working directly on ER stress, but who wish to determine whether this response is activated in the system they are studying: thus, it is important to list a standard set of criteria for monitoring UPR in different model systems. Here, we discuss approaches that can be used by researchers to plan and interpret experiments aimed at evaluating whether the UPR and related processes are activated. We would like to emphasize that no individual assay is guaranteed to be the most appropriate one in every situation and strongly recommend the use of multiple assays to verify UPR activation.