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High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease

Standard

High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease. / Dohler, Frank; Sepulveda-Falla, Diego; Krasemann, Susanne; Altmeppen, Hermann; Schlüter, Hartmut; Hildebrand, Diana; Zerr, Inga; Matschke, Jakob; Glatzel, Markus.

in: BRAIN, Jahrgang 137, Nr. Pt 3, 01.03.2014, S. 873-86.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Dohler, F, Sepulveda-Falla, D, Krasemann, S, Altmeppen, H, Schlüter, H, Hildebrand, D, Zerr, I, Matschke, J & Glatzel, M 2014, 'High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease', BRAIN, Jg. 137, Nr. Pt 3, S. 873-86. https://doi.org/10.1093/brain/awt375

APA

Dohler, F., Sepulveda-Falla, D., Krasemann, S., Altmeppen, H., Schlüter, H., Hildebrand, D., Zerr, I., Matschke, J., & Glatzel, M. (2014). High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease. BRAIN, 137(Pt 3), 873-86. https://doi.org/10.1093/brain/awt375

Vancouver

Dohler F, Sepulveda-Falla D, Krasemann S, Altmeppen H, Schlüter H, Hildebrand D et al. High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease. BRAIN. 2014 Mär 1;137(Pt 3):873-86. https://doi.org/10.1093/brain/awt375

Bibtex

@article{de022b8266e5459eb40f53d2a277c403,
title = "High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease",
abstract = "Alzheimer's disease is the most common form of dementia and the generation of oligomeric species of amyloid-β is causal to the initiation and progression of it. Amyloid-β oligomers bind to the N-terminus of plasma membrane-bound cellular prion protein (PrP(C)) initiating a series of events leading to synaptic degeneration. Composition of bound amyloid-β oligomers, binding regions within PrP(C), binding affinities and modifiers of this interaction have been almost exclusively studied in cell culture or murine models of Alzheimer's disease and our knowledge on PrP(C)-amyloid-β interaction in patients with Alzheimer's disease is limited regarding occurrence, binding regions in PrP(C), and size of bound amyloid-β oligomers. Here we employed a PrP(C)-amyloid-β binding assay and size exclusion chromatography on neuropathologically characterized Alzheimer's disease and non-demented control brains (n = 15, seven female, eight male, average age: 79.2 years for Alzheimer's disease and n = 10, three female, seven male, average age: 66.4 years for controls) to investigate amyloid-β-PrP(C) interaction. PrP(C)-amyloid-β binding always occurred in Alzheimer's disease brains and was never detected in non-demented controls. Neither expression level of PrP(C) nor known genetic modifiers of Alzheimer's disease, such as the PrP(C) codon 129 polymorphism, influenced this interaction. In Alzheimer's disease brains, binding of amyloid-β to PrP(C) occurred via the PrP(C) N-terminus. For synthetic amyloid-β42, small oligomeric species showed prominent binding to PrP(C), whereas in Alzheimer's disease brains larger protein assemblies containing amyloid-β42 bound efficiently to PrP(C). These data confirm Alzheimer's disease specificity of binding of amyloid-β to PrP(C) via its N-terminus in a large cohort of Alzheimer's disease/control brains. Differences in sizes of separated protein fractions between synthetic and brain-derived amyloid-β binding to PrP(C) suggest that larger assemblies of amyloid-β or additional non-amyloid-β components may play a role in binding of amyloid-β42 to PrP(C) in Alzheimer's disease.",
keywords = "Aged, Aged, 80 and over, Alzheimer Disease, Amyloid beta-Peptides, Chromatography, Gel, Cohort Studies, Female, Humans, Male, Middle Aged, Polymorphism, Genetic, PrPC Protein, Prefrontal Cortex, Prions, Protein Binding",
author = "Frank Dohler and Diego Sepulveda-Falla and Susanne Krasemann and Hermann Altmeppen and Hartmut Schl{\"u}ter and Diana Hildebrand and Inga Zerr and Jakob Matschke and Markus Glatzel",
year = "2014",
month = mar,
day = "1",
doi = "10.1093/brain/awt375",
language = "English",
volume = "137",
pages = "873--86",
journal = "BRAIN",
issn = "0006-8950",
publisher = "Oxford University Press",
number = "Pt 3",

}

RIS

TY - JOUR

T1 - High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease

AU - Dohler, Frank

AU - Sepulveda-Falla, Diego

AU - Krasemann, Susanne

AU - Altmeppen, Hermann

AU - Schlüter, Hartmut

AU - Hildebrand, Diana

AU - Zerr, Inga

AU - Matschke, Jakob

AU - Glatzel, Markus

PY - 2014/3/1

Y1 - 2014/3/1

N2 - Alzheimer's disease is the most common form of dementia and the generation of oligomeric species of amyloid-β is causal to the initiation and progression of it. Amyloid-β oligomers bind to the N-terminus of plasma membrane-bound cellular prion protein (PrP(C)) initiating a series of events leading to synaptic degeneration. Composition of bound amyloid-β oligomers, binding regions within PrP(C), binding affinities and modifiers of this interaction have been almost exclusively studied in cell culture or murine models of Alzheimer's disease and our knowledge on PrP(C)-amyloid-β interaction in patients with Alzheimer's disease is limited regarding occurrence, binding regions in PrP(C), and size of bound amyloid-β oligomers. Here we employed a PrP(C)-amyloid-β binding assay and size exclusion chromatography on neuropathologically characterized Alzheimer's disease and non-demented control brains (n = 15, seven female, eight male, average age: 79.2 years for Alzheimer's disease and n = 10, three female, seven male, average age: 66.4 years for controls) to investigate amyloid-β-PrP(C) interaction. PrP(C)-amyloid-β binding always occurred in Alzheimer's disease brains and was never detected in non-demented controls. Neither expression level of PrP(C) nor known genetic modifiers of Alzheimer's disease, such as the PrP(C) codon 129 polymorphism, influenced this interaction. In Alzheimer's disease brains, binding of amyloid-β to PrP(C) occurred via the PrP(C) N-terminus. For synthetic amyloid-β42, small oligomeric species showed prominent binding to PrP(C), whereas in Alzheimer's disease brains larger protein assemblies containing amyloid-β42 bound efficiently to PrP(C). These data confirm Alzheimer's disease specificity of binding of amyloid-β to PrP(C) via its N-terminus in a large cohort of Alzheimer's disease/control brains. Differences in sizes of separated protein fractions between synthetic and brain-derived amyloid-β binding to PrP(C) suggest that larger assemblies of amyloid-β or additional non-amyloid-β components may play a role in binding of amyloid-β42 to PrP(C) in Alzheimer's disease.

AB - Alzheimer's disease is the most common form of dementia and the generation of oligomeric species of amyloid-β is causal to the initiation and progression of it. Amyloid-β oligomers bind to the N-terminus of plasma membrane-bound cellular prion protein (PrP(C)) initiating a series of events leading to synaptic degeneration. Composition of bound amyloid-β oligomers, binding regions within PrP(C), binding affinities and modifiers of this interaction have been almost exclusively studied in cell culture or murine models of Alzheimer's disease and our knowledge on PrP(C)-amyloid-β interaction in patients with Alzheimer's disease is limited regarding occurrence, binding regions in PrP(C), and size of bound amyloid-β oligomers. Here we employed a PrP(C)-amyloid-β binding assay and size exclusion chromatography on neuropathologically characterized Alzheimer's disease and non-demented control brains (n = 15, seven female, eight male, average age: 79.2 years for Alzheimer's disease and n = 10, three female, seven male, average age: 66.4 years for controls) to investigate amyloid-β-PrP(C) interaction. PrP(C)-amyloid-β binding always occurred in Alzheimer's disease brains and was never detected in non-demented controls. Neither expression level of PrP(C) nor known genetic modifiers of Alzheimer's disease, such as the PrP(C) codon 129 polymorphism, influenced this interaction. In Alzheimer's disease brains, binding of amyloid-β to PrP(C) occurred via the PrP(C) N-terminus. For synthetic amyloid-β42, small oligomeric species showed prominent binding to PrP(C), whereas in Alzheimer's disease brains larger protein assemblies containing amyloid-β42 bound efficiently to PrP(C). These data confirm Alzheimer's disease specificity of binding of amyloid-β to PrP(C) via its N-terminus in a large cohort of Alzheimer's disease/control brains. Differences in sizes of separated protein fractions between synthetic and brain-derived amyloid-β binding to PrP(C) suggest that larger assemblies of amyloid-β or additional non-amyloid-β components may play a role in binding of amyloid-β42 to PrP(C) in Alzheimer's disease.

KW - Aged

KW - Aged, 80 and over

KW - Alzheimer Disease

KW - Amyloid beta-Peptides

KW - Chromatography, Gel

KW - Cohort Studies

KW - Female

KW - Humans

KW - Male

KW - Middle Aged

KW - Polymorphism, Genetic

KW - PrPC Protein

KW - Prefrontal Cortex

KW - Prions

KW - Protein Binding

U2 - 10.1093/brain/awt375

DO - 10.1093/brain/awt375

M3 - SCORING: Journal article

C2 - 24519981

VL - 137

SP - 873

EP - 886

JO - BRAIN

JF - BRAIN

SN - 0006-8950

IS - Pt 3

ER -