Measuring ER stress and the unfolded protein response using mammalian tissue culture system
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Document Type
Book ChapterPublication Date
2011-01-27Keywords
Endoplasmic ReticulumUnfolded Protein Response
Stress, Physiological
Tissue Culture Techniques
Genetics and Genomics
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Show full item recordAbstract
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.Source
Methods Enzymol. 2011;490:71-92. Link to article on publisher's siteDOI
10.1016/B978-0-12-385114-7.00004-0Permanent Link to this Item
http://hdl.handle.net/20.500.14038/44058PubMed ID
21266244Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/B978-0-12-385114-7.00004-0