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β‐amyloid peptide is internalized into chick retinal neurons and alters the distribution of myosin Vb
Author(s) -
Oliveira Leandro T.,
Matos Priscila A.,
Provance David William,
de Mello Fernando G.,
Andrade Leonardo R.,
Sorenson Martha M.,
Salerno Verônica P.
Publication year - 2012
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21007
Subject(s) - biology , internalization , microbiology and biotechnology , endocytic cycle , senile plaques , myosin , population , axon , amyloid (mycology) , p3 peptide , intracellular , retinal , neuroscience , alzheimer's disease , cell , amyloid precursor protein , biochemistry , endocytosis , pathology , disease , medicine , botany , demography , sociology
The most common neurodegenerative disorder afflicting the aging human population is Alzheimer's disease (AD). A major hallmark of AD is dementia from a loss of neuronal function, attributed to the presence and accumulation of β‐amyloid (Aβ) peptide into senile plaques. Preceding senile plaque formation, abnormalities in axons can be observed as changes in morphologies and intracellular trafficking. Recently, it has been recognized that Aβ also accumulates within neurons and this intraneuronal Aβ accumulation has been reported to be critical in the disruption of synapses and cognitive function. Here, we report on the internalization of a fluorescently labeled Aβ peptide into cultured chick retinal neurons. The pattern of Aβ distribution during the time course of incubation is reminiscent of the endocytic pathway. Furthermore, the distribution of the internalized Aβ peptide converges with that of myosin Vb and both relocalize from the axon to cell body. These observations are consistent with the hypothesis that AD proceeds as a result of an imbalance between Aβ production and Aβ clearance, suggesting a role for myosin Vb in this process. © 2012 Wiley Periodicals, Inc