Abstract:
:Monoclonal 2C3 specific to β-amyloid (Aβ) oligomers (AβOs) enabled us to test our hypothesis that the alteration of lipoprotein-Aβ interaction in the central nervous system (CNS) initiates and/or accelerates the cascade favoring Aβ assembly. Immunoprecipitation of frontal cortex employing 2C3 unequivocally detected soluble 4-, 8-, and 12-mers in Alzheimer's disease (AD) brains. Immunoblot analysis of the entorhinal cortex employing 2C3 revealed that the accumulation of soluble 12-mers precedes the appearance of neuronal loss or cognitive impairment and is enhanced as the Braak neurofibrially tangle (NFT) stages progress. The dissociation of soluble Aβ from lipoprotein particles occurs in cerebrospinal fluid (CSF), and the presence of lipoprotein-free oligomeric 2C3 conformers (4- to 35-mers) was evident, which mimic CNS environments. Such CNS environments may strongly affect conformation of soluble Aβ peptides, resulting in the conversion of soluble Aβ(42) monomers into soluble Aβ(42) assembly. The findings suggest that functionally declined lipoproteins may accelerate the generation of metabolic conditions leading to higher levels of soluble Aβ(42) assembly in the CNS.
journal_name
J Neurosci Resjournal_title
Journal of neuroscience researchauthors
Takamura A,Kawarabayashi T,Yokoseki T,Shibata M,Morishima-Kawashima M,Saito Y,Murayama S,Ihara Y,Abe K,Shoji M,Michikawa M,Matsubara Edoi
10.1002/jnr.22615subject
Has Abstractpub_date
2011-06-01 00:00:00pages
815-21issue
6eissn
0360-4012issn
1097-4547journal_volume
89pub_type
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