β-amyloid peptide is internalized into chick retinal neurons and alters the distribution of myosin Vb

Authors

  • Leandro T. Oliveira,

    1. Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
    2. Departamento de Biociências da Atividade Física, Escola da Educação Física e Desportos, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
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  • Priscila A. Matos,

    1. Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
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  • David William Provance Jr.,

    1. Centro de Desenvolvimento Tecnológico em Saúde, Fundação Oswaldo Cruz, Rio de Janeiro, Brazil
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  • Fernando G. de Mello,

    1. Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
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  • Leonardo R. Andrade,

    1. Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
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  • Martha M. Sorenson,

    1. Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
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  • Verônica P. Salerno

    Corresponding author
    1. Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
    2. Departamento de Biociências da Atividade Física, Escola da Educação Física e Desportos, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
    • Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil
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  • Monitoring Editor: Makoto Kinoshita

Abstract

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

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