Methods for monitoring endoplasmic reticulum stress and the unfolded protein response.

Hdl Handle:
http://hdl.handle.net/10147/93853
Title:
Methods for monitoring endoplasmic reticulum stress and the unfolded protein response.
Authors:
Samali, Afshin; Fitzgerald, Una; Deegan, Shane; Gupta, Sanjeev
Affiliation:
Department of Biochemistry, National University of Ireland, Galway, Galway, Ireland.
Citation:
Methods for monitoring endoplasmic reticulum stress and the unfolded protein response. 2010, 2010:830307 Int J Cell Biol
Journal:
International journal of cell biology
Issue Date:
2010
URI:
http://hdl.handle.net/10147/93853
DOI:
10.1155/2010/830307
PubMed ID:
20169136
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.
Language:
en
ISSN:
1687-8884

Full metadata record

DC FieldValue Language
dc.contributor.authorSamali, Afshinen
dc.contributor.authorFitzgerald, Unaen
dc.contributor.authorDeegan, Shaneen
dc.contributor.authorGupta, Sanjeeven
dc.date.accessioned2010-03-08T13:14:16Z-
dc.date.available2010-03-08T13:14:16Z-
dc.date.issued2010-
dc.identifier.citationMethods for monitoring endoplasmic reticulum stress and the unfolded protein response. 2010, 2010:830307 Int J Cell Biolen
dc.identifier.issn1687-8884-
dc.identifier.pmid20169136-
dc.identifier.doi10.1155/2010/830307-
dc.identifier.urihttp://hdl.handle.net/10147/93853-
dc.description.abstractThe 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.-
dc.language.isoenen
dc.titleMethods for monitoring endoplasmic reticulum stress and the unfolded protein response.en
dc.contributor.departmentDepartment of Biochemistry, National University of Ireland, Galway, Galway, Ireland.en
dc.identifier.journalInternational journal of cell biologyen

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