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Cytosolic amyloid-beta peptide 42 escaping from degradation induces cell death

Cited 13 time in Web of Science Cited 15 time in Scopus
Authors
Lee, Eun Kyung; Park, Yong Wook; Shin, Dong Yeon; Mook-Jung, Inhee; Yoo, Yung Joon
Issue Date
2006-04-25
Publisher
Elsevier
Citation
Biochem Biophys Res Commun. 2006 Jun 2;344(2):471-7. Epub 2006 Apr 4.
Keywords
Amyloid beta-Protein/*metabolism*ApoptosisCell Line, TumorCytosol/*metabolismHumansNeuroblastoma/*metabolism/*pathologyPeptide Fragments/*metabolism
Abstract
Accumulating evidence suggests that intracellular amyloid-beta (Abeta) peptide triggers the early pathological events in Alzheimer's disease (AD). However, little is known about the consequence of cytosolic Abeta. In this study, we ectopically expressed Abeta42 in the cytoplasm of SH-SY5Y neuroblastoma cells by expressing a fusion protein of GFP-tagged ubiquitin and Abeta42 (GFPUb-Abeta42). Although GFPUb and Abeta42 are stochastically produced with the same molar ratio in the cytoplasm, Abeta42 was completely degraded in more than 50% of the GFPUb-expressing cells. However, if Abeta42 was not degraded in their cytoplasm, then Abeta42-expressing cells underwent apoptosis. The number of Abeta42-expressing cells is significantly increased by the inhibition of proteasome with MG132. Cytosolic Abeta42 which has escaped degradation inhibits proteasome and thereby may accelerate the accumulation of Abeta42 and its detrimental effects. Our findings suggest that cells have the potential to degrade Abeta42 in their cytoplasm but if Abeta42 appears in the cytoplasm due to its incomplete degradation, it accumulates and may trigger the fatal cascade of pathology of AD.
ISSN
0006-291X (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16630565

http://hdl.handle.net/10371/27245
DOI
https://doi.org/10.1016/j.bbrc.2006.03.166
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Biochemistry & Molecular Biology (생화학교실)Journal Papers (저널논문_생화학교실)
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