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Autophagic dysfunction in Alzheimer’s disease: Cellular and molecular mechanistic approaches to halt Alzheimer’s pathogenesis

dc.contributor.authorUddin M.S.
dc.contributor.authorMamun A.A.
dc.contributor.authorLabu Z.K.
dc.contributor.authorHidalgo-Lanussa O.
dc.contributor.authorBarreto G.E.
dc.contributor.authorAshraf G.M.
dc.date.accessioned2020-09-02T22:29:29Z
dc.date.available2020-09-02T22:29:29Z
dc.date.issued2019
dc.identifier10.1002/jcp.27588
dc.identifier.citation234, 6, 8094-8112
dc.identifier.issn00219541
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6466
dc.descriptionAutophagy is a preserved cytoplasmic self-degradation process and endorses recycling of intracellular constituents into bioenergetics for the controlling of cellular homeostasis. Functional autophagy process is essential in eliminating cytoplasmic waste components and helps in the recycling of some of its constituents. Studies have revealed that neurodegenerative disorders may be caused by mutations in autophagy-related genes and alterations of autophagic flux. Alzheimer’s disease (AD) is an irrevocable deleterious neurodegenerative disorder characterized by the formation of senile plaques and neurofibrillary tangles (NFTs) in the hippocampus and cortex. In the central nervous system of healthy people, there is no accretion of amyloid β (Aβ) peptides due to the balance between generation and degradation of Aβ. However, for AD patients, the generation of Aβ peptides is higher than lysis that causes accretion of Aβ. Likewise, the maturation of autophagolysosomes and inhibition of their retrograde transport creates favorable conditions for Aβ accumulation. Furthermore, increasing mammalian target of rapamycin (mTOR) signaling raises tau levels as well as phosphorylation. Alteration of mTOR activity occurs in the early stage of AD. In addition, copious evidence links autophagic/lysosomal dysfunction in AD. Compromised mitophagy is also accountable for dysfunctional mitochondria that raises Alzheimer’s pathology. Therefore, autophagic dysfunction might lead to the deposit of atypical proteins in the AD brain and manipulation of autophagy could be considered as an emerging therapeutic target. This review highlights the critical linkage of autophagy in the pathogenesis of AD, and avows a new insight to search for therapeutic target for blocking Alzheimer’s pathogenesis. © 2018 Wiley Periodicals, Inc.
dc.language.isoen
dc.publisherWiley-Liss Inc.
dc.subjectAlzheimer’s disease
dc.subjectamyloid β
dc.subjectautophagy
dc.subjectlysosomal dysfunction
dc.subjectmitophagy
dc.subjectneurofibrillary tangles
dc.subjectsenile plaques
dc.subjectamyloid beta protein
dc.subjectcarbamazepine
dc.subjectdimebon
dc.subjectlithium
dc.subjectmammalian target of rapamycin
dc.subjectmetformin
dc.subjectminoxidil
dc.subjectnicotinamide
dc.subjectnootropic agent
dc.subjectpeptidomimetic agent
dc.subjectrapamycin
dc.subjectresveratrol
dc.subjectsmer 28
dc.subjecttau protein
dc.subjecttrehalose
dc.subjectunclassified drug
dc.subjectMTOR protein, human
dc.subjecttarget of rapamycin kinase
dc.subjectaging
dc.subjectAlzheimer disease
dc.subjectautolysosome
dc.subjectautophagosome
dc.subjectautophagy
dc.subjectbioenergy
dc.subjectbrain cortex
dc.subjectbrain mitochondrion
dc.subjectcell death
dc.subjectcentral nervous system
dc.subjectdrug effect
dc.subjectdrug mechanism
dc.subjectdrug targeting
dc.subjectgene mutation
dc.subjecthippocampus
dc.subjecthomeostasis
dc.subjecthousekeeping gene
dc.subjecthuman
dc.subjectlysosome
dc.subjectmitophagy
dc.subjectmTOR signaling
dc.subjectnerve degeneration
dc.subjectneurofibrillary tangle
dc.subjectneuropathology
dc.subjectnonhuman
dc.subjectpathogenesis
dc.subjectpathophysiology
dc.subjectpriority journal
dc.subjectprotein degradation
dc.subjectprotein phosphorylation
dc.subjectReview
dc.subjectsenile plaque
dc.subjectxenophagy
dc.subjectAlzheimer disease
dc.subjectautophagy
dc.subjectcytoplasm
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectmitochondrion
dc.subjectpathology
dc.subjectsignal transduction
dc.subjectAlzheimer Disease
dc.subjectAmyloid beta-Peptides
dc.subjectAutophagosomes
dc.subjectAutophagy
dc.subjectCytoplasm
dc.subjectHumans
dc.subjectMitochondria
dc.subjectMitophagy
dc.subjectProteolysis
dc.subjectSignal Transduction
dc.subjectTOR Serine-Threonine Kinases
dc.titleAutophagic dysfunction in Alzheimer’s disease: Cellular and molecular mechanistic approaches to halt Alzheimer’s pathogenesis
dc.typeReview


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