Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity.
Nuclear inclusion a (NIa) of turnip mosaic virus is a cytosolic protease that cleaves amyloid β (Aβ) when heterologously overexpressed. Lentivirus-mediated expression of NIa in the brains of APP(sw)/PS1 mice significantly reduces cerebral Aβ levels and plaque depositions, and improves behavioral def...
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doaj-aed34ca48cd7478cba5c7d54938ba1972020-11-25T01:27:14ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0196e9865010.1371/journal.pone.0098650Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity.Baehyun ShinHyejin OhSang Min ParkHye-Eun HanMichael YeWoo Keun SongWoo Jin ParkNuclear inclusion a (NIa) of turnip mosaic virus is a cytosolic protease that cleaves amyloid β (Aβ) when heterologously overexpressed. Lentivirus-mediated expression of NIa in the brains of APP(sw)/PS1 mice significantly reduces cerebral Aβ levels and plaque depositions, and improves behavioral deficits. Here, the effects of NIa and neprilysin (NEP), a well-known Aβ-cleaving protease, on oligomeric Aβ-induced cell death were evaluated. NIa cleaved monomeric and oligomeric Aβ at a similar rate, whereas NEP only cleaved monomeric Aβ. Oligomeric Aβ-induced cytotoxicity and mitochondrial dysfunction were significantly ameliorated by NIa, but not by NEP. Endocytosed fluorescently-labeled Aβ localized to mitochondria, and this was significantly reduced by NIa, but not by NEP. These data suggest that NIa may exerts its protective roles by degrading Aβ and thus preventing mitochondrial deposition of Aβ.http://europepmc.org/articles/PMC4051590?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Baehyun Shin Hyejin Oh Sang Min Park Hye-Eun Han Michael Ye Woo Keun Song Woo Jin Park |
spellingShingle |
Baehyun Shin Hyejin Oh Sang Min Park Hye-Eun Han Michael Ye Woo Keun Song Woo Jin Park Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. PLoS ONE |
author_facet |
Baehyun Shin Hyejin Oh Sang Min Park Hye-Eun Han Michael Ye Woo Keun Song Woo Jin Park |
author_sort |
Baehyun Shin |
title |
Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. |
title_short |
Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. |
title_full |
Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. |
title_fullStr |
Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. |
title_full_unstemmed |
Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity. |
title_sort |
intracellular cleavage of amyloid β by a viral protease nia prevents amyloid β-mediated cytotoxicity. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2014-01-01 |
description |
Nuclear inclusion a (NIa) of turnip mosaic virus is a cytosolic protease that cleaves amyloid β (Aβ) when heterologously overexpressed. Lentivirus-mediated expression of NIa in the brains of APP(sw)/PS1 mice significantly reduces cerebral Aβ levels and plaque depositions, and improves behavioral deficits. Here, the effects of NIa and neprilysin (NEP), a well-known Aβ-cleaving protease, on oligomeric Aβ-induced cell death were evaluated. NIa cleaved monomeric and oligomeric Aβ at a similar rate, whereas NEP only cleaved monomeric Aβ. Oligomeric Aβ-induced cytotoxicity and mitochondrial dysfunction were significantly ameliorated by NIa, but not by NEP. Endocytosed fluorescently-labeled Aβ localized to mitochondria, and this was significantly reduced by NIa, but not by NEP. These data suggest that NIa may exerts its protective roles by degrading Aβ and thus preventing mitochondrial deposition of Aβ. |
url |
http://europepmc.org/articles/PMC4051590?pdf=render |
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