Measuring ER stress and the unfolded protein response using mammalian tissue culture system

Christine M. Oslowski, Fumihiko Urano

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

527 Scopus citations

Abstract

The endoplasmic reticulum (ER) functions to properly fold and process secreted and transmembrane proteins. Environmental and genetic factors that disrupt ER function cause an accumulation of misfolded and unfolded proteins in the ER lumen, a condition termed ER stress. ER stress activates a signaling network called the Unfolded Protein Response (UPR) to alleviate this stress and restore ER homeostasis, promoting cell survival and adaptation. However, under unresolvable ER stress conditions, the UPR promotes apoptosis. Here, we discuss the current methods to measure ER stress levels, UPR activation, and subsequent pathways in mammalian cells. These methods will assist us in understanding the UPR and its contribution to ER stress-related disorders such as diabetes and neurodegeneration.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages71-92
Number of pages22
EditionC
DOIs
StatePublished - 2011

Publication series

NameMethods in Enzymology
NumberC
Volume490
ISSN (Print)0076-6879

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