Premium
Amyloid‐beta oligomers increase the localization of prion protein at the cell surface
Author(s) -
Caetano Fabiana A.,
Beraldo Flavio H.,
Hajj Glaucia N. M.,
Guimaraes Andre L.,
Jürgensen Sofia,
WasilewskaSampaio Ana Paula,
Hirata Pedro H. F.,
Souza Ivana,
Machado Cleiton F.,
Wong Daisy Y.L.,
De Felice Fernanda G.,
Ferreira Sergio T.,
Prado Vania F.,
Rylett R. Jane,
Martins Vilma R.,
Prado Marco A. M.
Publication year - 2011
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2011.07225.x
Subject(s) - microbiology and biotechnology , cell , endocytosis , oligomer , biotinylation , cell culture , confocal microscopy , receptor , flow cytometry , chemistry , biophysics , biology , biochemistry , organic chemistry , genetics
J. Neurochem. (2011) 117 , 538–553. Abstract In Alzheimer’s disease, the amyloid‐β peptide (Aβ) interacts with distinct proteins at the cell surface to interfere with synaptic communication. Recent data have implicated the prion protein (PrP C ) as a putative receptor for Aβ. We show here that Aβ oligomers signal in cells in a PrP C ‐dependent manner, as might be expected if Aβ oligomers use PrP C as a receptor. Immunofluorescence, flow cytometry and cell surface protein biotinylation experiments indicated that treatment with Aβ oligomers, but not monomers, increased the localization of PrP C at the cell surface in cell lines. These results were reproduced in hippocampal neuronal cultures by labeling cell surface PrP C . In order to understand possible mechanisms involved with this effect of Aβ oligomers, we used live cell confocal and total internal reflection microscopy in cell lines. Aβ oligomers inhibited the constitutive endocytosis of PrP C , but we also found that after Aβ oligomer‐treatment PrP C formed more clusters at the cell surface, suggesting the possibility of multiple effects of Aβ oligomers. Our experiments show for the first time that Aβ oligomers signal in a PrP C ‐dependent way and that they can affect PrP C trafficking, increasing its localization at the cell surface.