Premium
A potential function for neuronal exosomes: Sequestering intracerebral amyloid‐β peptide
Author(s) -
Yuyama Kohei,
Sun Hui,
Usuki Seigo,
Sakai Shota,
Hanamatsu Hisatoshi,
Mioka Tetsuo,
Kimura Nobuyuki,
Okada Megumi,
Tahara Hidetoshi,
Furukawa Jun-ichi,
Fujitani Naoki,
Shinohara Yasuro,
Igarashi Yasuyuki
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.027
Subject(s) - microvesicles , exosome , downregulation and upregulation , cerebrospinal fluid , genetically modified mouse , transgene , amyloid (mycology) , pathogenesis , alzheimer's disease , amyloid precursor protein , microbiology and biotechnology , neurodegeneration , biology , chemistry , neuroscience , medicine , pathology , immunology , disease , microrna , biochemistry , gene
Elevated amyloid‐β peptide (Aβ) in brain contributes to Alzheimer's disease (AD) pathogenesis. We demonstrated the presence of exosome‐associated Aβ in the cerebrospinal fluid (CSF) of cynomolgus monkeys and APP transgenic mice. The levels of exosome‐associated Aβ notably decreased in the CSF of aging animals. We also determined that neuronal exosomes, but not glial exosomes, had abundant glycosphingolipids and could capture Aβ. Infusion of neuronal exosomes into brains of APP transgenic mice decreased Aβ and amyloid depositions, similarly to what reported previously on neuroblastoma‐derived exosomes. These findings highlight the role of neuronal exosomes in Aβ clearance, and suggest that their downregulation might relate to Aβ accumulation and, ultimately, the development of AD pathology.