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HNE-modified proteins in Down syndrome: Involvement in development of Alzheimer disease neuropathology

dc.contributor.authorBarone E.
dc.contributor.authorHead E.
dc.contributor.authorButterfield D.A.
dc.contributor.authorPerluigi M.
dc.date.accessioned2020-09-02T22:12:59Z
dc.date.available2020-09-02T22:12:59Z
dc.date.issued2017
dc.identifier10.1016/j.freeradbiomed.2016.10.508
dc.identifier.citation111, , 262-269
dc.identifier.issn08915849
dc.identifier.urihttps://hdl.handle.net/20.500.12728/3683
dc.descriptionDown syndrome (DS), trisomy of chromosome 21, is the most common genetic form of intellectual disability. The neuropathology of DS involves multiple molecular mechanisms, similar to AD, including the deposition of beta-amyloid (Aβ) into senile plaques and tau hyperphosphorylationg in neurofibrillary tangles. Interestingly, many genes encoded by chromosome 21, in addition to being primarily linked to amyloid-beta peptide (Aβ) pathology, are responsible for increased oxidative stress (OS) conditions that also result as a consequence of reduced antioxidant system efficiency. However, redox homeostasis is disturbed by overproduction of Aβ, which accumulates into plaques across the lifespan in DS as well as in AD, thus generating a vicious cycle that amplifies OS-induced intracellular changes. The present review describes the current literature that demonstrates the accumulation of oxidative damage in DS with a focus on the lipid peroxidation by-product, 4-hydroxy-2-nonenal (HNE). HNE reacts with proteins and can irreversibly impair their functions. We suggest that among different post-translational modifications, HNE-adducts on proteins accumulate in DS brain and play a crucial role in causing the impairment of glucose metabolism, neuronal trafficking, protein quality control and antioxidant response. We hypothesize that dysfunction of these specific pathways contribute to accelerated neurodegeneration associated with AD neuropathology. © 2017 Elsevier Inc.
dc.language.isoen
dc.publisherElsevier Inc.
dc.subject4-hydroxy-2-nonenal
dc.subjectAlzheimer disease
dc.subjectDown syndrome
dc.subjectLipid peroxidation
dc.subjectProtein oxidation
dc.subjectRedox proteomics
dc.subject4 hydroxynonenal
dc.subjectglucose
dc.subjectprotein
dc.subject4-hydroxy-2-nonenal
dc.subjectaldehyde
dc.subjectamyloid beta protein
dc.subjectglucose
dc.subjectMAPT protein, human
dc.subjecttau protein
dc.subjectAlzheimer disease
dc.subjectDown syndrome
dc.subjectglucose metabolism
dc.subjecthuman
dc.subjectlipid peroxidation
dc.subjectmolecular pathology
dc.subjectnerve degeneration
dc.subjectneuropathology
dc.subjectnonhuman
dc.subjectoxidation reduction reaction
dc.subjectoxidative stress
dc.subjectpriority journal
dc.subjectprotein modification
dc.subjectprotein processing
dc.subjectprotein quality
dc.subjectproteomics
dc.subjectReview
dc.subjectAlzheimer disease
dc.subjectamyloid plaque
dc.subjectDown syndrome
dc.subjectgenetics
dc.subjectlipid peroxidation
dc.subjectmetabolism
dc.subjectmitochondrion
dc.subjectnerve cell
dc.subjectneurofibrillary tangle
dc.subjectoxidative stress
dc.subjectpathology
dc.subjectprotein processing
dc.subjectAldehydes
dc.subjectAlzheimer Disease
dc.subjectAmyloid beta-Peptides
dc.subjectDown Syndrome
dc.subjectGlucose
dc.subjectHumans
dc.subjectLipid Peroxidation
dc.subjectMitochondria
dc.subjectNeurofibrillary Tangles
dc.subjectNeurons
dc.subjectOxidative Stress
dc.subjectPlaque, Amyloid
dc.subjectProtein Processing, Post-Translational
dc.subjecttau Proteins
dc.titleHNE-modified proteins in Down syndrome: Involvement in development of Alzheimer disease neuropathology
dc.typeReview


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