Modulation of Autophagic Activity for the Treatment of Alzheimer’s Disease
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".
Deadline for manuscript submissions: closed (31 January 2021) | Viewed by 9884
Special Issue Editor
Interests: Alzheimer’s disease; aggregation; tau oligomer
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
As neurons age, their survival depends on eliminating a growing burden of damaged, potentially toxic proteins and organelles. This capability declines with aging and disorders. There are two proteolytic systems, the proteasome system and the autophagic–lysosomal system. Senile plaques consist of amyloid β protein (Aβ) and neurofibrillary tangles (NFTs) which, composed of highly phosphorylated tau protein, are pathological hallmarks of Alzheimer's disease (AD).
Autophagy is considered to be one of the main Aβ-eliminating pathways under normal conditions. The ubiquitin proteasomal system may be the primary mechanism to degrade endogenous tau, while aggregated tau does not undergo degradation by the proteasome. Autophagy is involved in the clearance of soluble and aggregated tau and NFT in the cell. Moreover, autophagy activation can reduce the secretion of tau and tau propagation. These facts imply that autophagy activation can be beneficial for the AD via clearance of Aβ or tau. In fact, several therapeutic studies have been performed by modulating autophagy, including mTORC1-dependent and -independent autophagy inducers, other autophagy-inducing drugs, and gene therapy including micro RNA. However, it has been reported that Aβ can be produced in autophagy, and Aβ secretion can also be done by autophagy. This Special Issue will give us precious information about autophagy and Aβ or tau. Additionally, it may shed light on whether autophagy activation is beneficial or not for AD treatment.
Dr. Tadanori Hamano
Guest Editor
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Keywords
- Alzheimer’s disease
- tau protein
- amyloid protein
- autophagy
- LC3
- P62
- rapamycin
- mTORC1
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