6533b85bfe1ef96bd12ba1c5
RESEARCH PRODUCT
Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation
Francesco CappelloGiulio TaglialatelaClaudia MarinoClaudia MarinoBalaji Krishnansubject
chaperoninProtein ConformationPhysiologyAmyloid betaCognitive NeuroscienceBiochemistryCell LineMitochondrial ProteinsMice03 medical and health sciences0302 clinical medicinemedicineAnimalsHumanssynaptic toxicityCytotoxicity030304 developmental biology0303 health sciencesAmyloid-β oligomersynaptic plasticityAmyloid beta-PeptidesbiologyChemistryNeurotoxicityLong-term potentiationChaperonin 60Cell BiologyGeneral MedicineAlzheimer's diseaseHsp60medicine.diseaseCell biologyChaperone (protein)SynapsesToxicitySynaptic plasticitybiology.proteinHSP60030217 neurology & neurosurgeryProtein Bindingdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-05-15 | ACS Chemical Neuroscience |