Abstract
Alzheimer's disease (AD) is the leading cause of dementia worldwide. While the etiology of AD remains uncertain, neurotoxic effects of amyloid beta oligomers (Aβo) on synaptic function, a well-established early event in AD, is an attractive area for the development of novel strategies to modify or cease the disease's progression. In this work, we tested the protective action of the mitochondrial chaperone Hsp60 against Aβo neurotoxicity, by determining the direct effect of Hsp60 in changing Aβo toxic conformations and thus reducing their dysfunctional synaptic binding and consequent suppression of long-term potentiation. Our data suggest that Hsp60 has a direct impact on Aβo, resulting in a reduction of cytotoxicity and rescue of Aβo-driven synaptic damage, thus proposing Hsp60 as an attractive therapeutic target candidate.
| Original language | English (US) |
|---|---|
| Journal | ACS Chemical Neuroscience |
| DOIs | |
| State | Published - Jan 1 2019 |
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Keywords
- Alzheimer's disease
- Amyloid-β oligomers
- chaperonin
- Hsp60
- synaptic plasticity
- synaptic toxicity
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Cognitive Neuroscience
- Cell Biology
Cite this
Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation. / Marino, Claudia; Krishnan, Balaji; Cappello, Francesco; Taglialatela, Giulio.
In: ACS Chemical Neuroscience, 01.01.2019.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation
AU - Marino, Claudia
AU - Krishnan, Balaji
AU - Cappello, Francesco
AU - Taglialatela, Giulio
PY - 2019/1/1
Y1 - 2019/1/1
N2 - Alzheimer's disease (AD) is the leading cause of dementia worldwide. While the etiology of AD remains uncertain, neurotoxic effects of amyloid beta oligomers (Aβo) on synaptic function, a well-established early event in AD, is an attractive area for the development of novel strategies to modify or cease the disease's progression. In this work, we tested the protective action of the mitochondrial chaperone Hsp60 against Aβo neurotoxicity, by determining the direct effect of Hsp60 in changing Aβo toxic conformations and thus reducing their dysfunctional synaptic binding and consequent suppression of long-term potentiation. Our data suggest that Hsp60 has a direct impact on Aβo, resulting in a reduction of cytotoxicity and rescue of Aβo-driven synaptic damage, thus proposing Hsp60 as an attractive therapeutic target candidate.
AB - Alzheimer's disease (AD) is the leading cause of dementia worldwide. While the etiology of AD remains uncertain, neurotoxic effects of amyloid beta oligomers (Aβo) on synaptic function, a well-established early event in AD, is an attractive area for the development of novel strategies to modify or cease the disease's progression. In this work, we tested the protective action of the mitochondrial chaperone Hsp60 against Aβo neurotoxicity, by determining the direct effect of Hsp60 in changing Aβo toxic conformations and thus reducing their dysfunctional synaptic binding and consequent suppression of long-term potentiation. Our data suggest that Hsp60 has a direct impact on Aβo, resulting in a reduction of cytotoxicity and rescue of Aβo-driven synaptic damage, thus proposing Hsp60 as an attractive therapeutic target candidate.
KW - Alzheimer's disease
KW - Amyloid-β oligomers
KW - chaperonin
KW - Hsp60
KW - synaptic plasticity
KW - synaptic toxicity
UR - http://www.scopus.com/inward/record.url?scp=85066443435&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85066443435&partnerID=8YFLogxK
U2 - 10.1021/acschemneuro.9b00086
DO - 10.1021/acschemneuro.9b00086
M3 - Article
C2 - 31091411
AN - SCOPUS:85066443435
JO - ACS Chemical Neuroscience
JF - ACS Chemical Neuroscience
SN - 1948-7193
ER -