Dissociation of β-amyloid from lipoprotein in cerebrospinal fluid from Alzheimer's disease accelerates β-amyloid-42 assembly.
Identifieur interne : 002471 ( Main/Exploration ); précédent : 002470; suivant : 002472Dissociation of β-amyloid from lipoprotein in cerebrospinal fluid from Alzheimer's disease accelerates β-amyloid-42 assembly.
Auteurs : Ayumi Takamura [Japon] ; Takeshi Kawarabayashi ; Tatsuki Yokoseki ; Masao Shibata ; Maho Morishima-Kawashima ; Yuko Saito ; Shigeo Murayama ; Yasuo Ihara ; Koji Abe ; Mikio Shoji ; Makoto Michikawa ; Etsuro MatsubaraSource :
- Journal of neuroscience research [ 1097-4547 ] ; 2011.
Descripteurs français
- KwdFr :
- Adulte d'âge moyen, Analyse de variance, Encéphale (métabolisme), Femelle, Fragments peptidiques (), Humains, Lipoprotéines (métabolisme), Maladie d'Alzheimer (), Maladie d'Alzheimer (anatomopathologie), Mâle, Peptides bêta-amyloïdes (), Sujet âgé, Sujet âgé de 80 ans ou plus, Test ELISA (), Études cas-témoins.
- MESH :
- anatomopathologie : Maladie d'Alzheimer.
- métabolisme : Encéphale, Lipoprotéines.
- Adulte d'âge moyen, Analyse de variance, Femelle, Fragments peptidiques, Humains, Maladie d'Alzheimer, Mâle, Peptides bêta-amyloïdes, Sujet âgé, Sujet âgé de 80 ans ou plus, Test ELISA, Études cas-témoins.
English descriptors
- KwdEn :
- Aged, Aged, 80 and over, Alzheimer Disease (cerebrospinal fluid), Alzheimer Disease (pathology), Amyloid beta-Peptides (cerebrospinal fluid), Analysis of Variance, Brain (metabolism), Case-Control Studies, Enzyme-Linked Immunosorbent Assay (methods), Female, Humans, Lipoproteins (metabolism), Male, Middle Aged, Peptide Fragments (cerebrospinal fluid).
- MESH :
- chemical , cerebrospinal fluid : Amyloid beta-Peptides, Peptide Fragments.
- cerebrospinal fluid : Alzheimer Disease.
- metabolism : Brain, Lipoproteins.
- methods : Enzyme-Linked Immunosorbent Assay.
- pathology : Alzheimer Disease.
- Aged, Aged, 80 and over, Analysis of Variance, Case-Control Studies, Female, Humans, Male, Middle Aged.
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.
DOI: 10.1002/jnr.22615
PubMed: 21394760
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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