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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2007-11-5
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pubmed:abstractText |
Alzheimer's disease (AD) is characterized by the aggregation of misfolded proteins. Previously we reported activation of the unfolded protein response (UPR) in AD neurons. A potential source for UPR activation in AD neurons may be the increased levels of beta-amyloid (Abeta). In this study, we used preparations enriched in oligomeric or fibrillar Abeta (1-42) to investigate the role of the conformational state of Abeta in UPR activation in differentiated neuroblastoma cells. Both oligomeric and fibrillar Abeta (1-42) do not induce BiP expression to the extent that it can be detected in a pool of cells. However, using a fluorescent UPR reporter cell line that allows analysis of individual cells, we demonstrated mild activation of the UPR by oligomeric but not fibrillar Abeta (1-42). We showed that oligomeric Abeta (1-42) is significantly more toxic to cells primed for UPR than is fibrillar Abeta (1-42), indicating that activation of the UPR contributes to oligomer-specific Abeta (1-42) toxicity. Because UPR activation is observed in AD brain at a stage that precedes the massive fibrillar Abeta deposition and tangle formation, this may indicate a role for nonfibrillar Abeta in the induction of the UPR in AD neurons.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Dimethyl Sulfoxide,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Formazans,
http://linkedlifedata.com/resource/pubmed/chemical/MTT formazan,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrazolium Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-42),
http://linkedlifedata.com/resource/pubmed/chemical/thioflavin T
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1523-0864
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2245-54
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17979527-Amyloid beta-Peptides,
pubmed-meshheading:17979527-Calnexin,
pubmed-meshheading:17979527-Cell Differentiation,
pubmed-meshheading:17979527-Cell Line,
pubmed-meshheading:17979527-Cell Survival,
pubmed-meshheading:17979527-Dimethyl Sulfoxide,
pubmed-meshheading:17979527-Dose-Response Relationship, Drug,
pubmed-meshheading:17979527-Endoplasmic Reticulum,
pubmed-meshheading:17979527-Fluorescent Dyes,
pubmed-meshheading:17979527-Formazans,
pubmed-meshheading:17979527-Humans,
pubmed-meshheading:17979527-In Situ Nick-End Labeling,
pubmed-meshheading:17979527-Neuroblastoma,
pubmed-meshheading:17979527-Peptide Fragments,
pubmed-meshheading:17979527-Protein Conformation,
pubmed-meshheading:17979527-Stress, Physiological,
pubmed-meshheading:17979527-Temperature,
pubmed-meshheading:17979527-Tetrazolium Salts,
pubmed-meshheading:17979527-Thiazoles,
pubmed-meshheading:17979527-Time Factors,
pubmed-meshheading:17979527-Transfection,
pubmed-meshheading:17979527-Tunicamycin
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pubmed:year |
2007
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pubmed:articleTitle |
Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner.
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pubmed:affiliation |
Neurogenetics Laboratory, University of Amsterdam, Amsterdam, The Netherlands.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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