Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease

M.J. Guerrero-Muñoz; D.L. Castillo-Carranza; S. Krishnamurthy; A.A. Paulucci-Holthauzen; U. Sengupta; C.A. Lasagna-Reeves; Y. Ahmad; G.R. Jackson; R. Kayed

doi:10.1016/j.nbd.2014.08.008

Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease

M.J. Guerrero-Muñoz, D.L. Castillo-Carranza, S. Krishnamurthy, A.A. Paulucci-Holthauzen, U. Sengupta, C.A. Lasagna-Reeves, Y. Ahmad, G.R. Jackson, R. Kayed

Research output: Contribution to journal › Article › peer-review

58 Citations (Scopus)

Abstract

Alzheimer's disease is a complex disease characterized by overlapping phenotypes with different neurodegenerative disorders. Oligomers are considered the most toxic species in amyloid pathologies. We examined human AD brain samples using an anti-oligomer antibody generated in our laboratory and detected potential hybrid oligomers composed of amyloid-β, prion protein, α-synuclein, and TDP-43 phosphorylated at serines 409 and 410. These data and in vitro results suggest that Aβ oligomer seeds act as a template for the aggregation of other proteins and generate an overlapping phenotype with other neuronal disorders. Furthermore, these results could explain why anti-amyloid-β therapy has been unsuccessful.

Original language	English
Pages (from-to)	14-23
Number of pages	10
Journal	Neurobiology of Disease
Volume	71
DOIs	https://doi.org/10.1016/j.nbd.2014.08.008
Publication status	Published - Nov 2014
Externally published	Yes

Bibliographical note

Funding Information:
We are grateful to Malika Farhed for excellent technical assistance, Julia Gerson for assistance with manuscript preparation and data analysis, and Lindsay Reese and Jennifer Deger for editorial assistance. We also thank Dr. Kelly T. Dineley and Dr. Yogesh Wairkar for their helpful suggestions. This work was supported by the Mitchell Center for Neurodegenerative Diseases and the Cullen Family Trust for Health Care .

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

All Science Journal Classification (ASJC) codes

Neurology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.nbd.2014.08.008

Cite this

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title = "Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease",

abstract = "Alzheimer's disease is a complex disease characterized by overlapping phenotypes with different neurodegenerative disorders. Oligomers are considered the most toxic species in amyloid pathologies. We examined human AD brain samples using an anti-oligomer antibody generated in our laboratory and detected potential hybrid oligomers composed of amyloid-β, prion protein, α-synuclein, and TDP-43 phosphorylated at serines 409 and 410. These data and in vitro results suggest that Aβ oligomer seeds act as a template for the aggregation of other proteins and generate an overlapping phenotype with other neuronal disorders. Furthermore, these results could explain why anti-amyloid-β therapy has been unsuccessful.",

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note = "Funding Information: We are grateful to Malika Farhed for excellent technical assistance, Julia Gerson for assistance with manuscript preparation and data analysis, and Lindsay Reese and Jennifer Deger for editorial assistance. We also thank Dr. Kelly T. Dineley and Dr. Yogesh Wairkar for their helpful suggestions. This work was supported by the Mitchell Center for Neurodegenerative Diseases and the Cullen Family Trust for Health Care . Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "2014",

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doi = "10.1016/j.nbd.2014.08.008",

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AU - Guerrero-Muñoz, M.J.

AU - Castillo-Carranza, D.L.

AU - Krishnamurthy, S.

AU - Paulucci-Holthauzen, A.A.

AU - Sengupta, U.

AU - Lasagna-Reeves, C.A.

AU - Ahmad, Y.

AU - Jackson, G.R.

AU - Kayed, R.

N1 - Funding Information: We are grateful to Malika Farhed for excellent technical assistance, Julia Gerson for assistance with manuscript preparation and data analysis, and Lindsay Reese and Jennifer Deger for editorial assistance. We also thank Dr. Kelly T. Dineley and Dr. Yogesh Wairkar for their helpful suggestions. This work was supported by the Mitchell Center for Neurodegenerative Diseases and the Cullen Family Trust for Health Care . Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 2014/11

Y1 - 2014/11

N2 - Alzheimer's disease is a complex disease characterized by overlapping phenotypes with different neurodegenerative disorders. Oligomers are considered the most toxic species in amyloid pathologies. We examined human AD brain samples using an anti-oligomer antibody generated in our laboratory and detected potential hybrid oligomers composed of amyloid-β, prion protein, α-synuclein, and TDP-43 phosphorylated at serines 409 and 410. These data and in vitro results suggest that Aβ oligomer seeds act as a template for the aggregation of other proteins and generate an overlapping phenotype with other neuronal disorders. Furthermore, these results could explain why anti-amyloid-β therapy has been unsuccessful.

AB - Alzheimer's disease is a complex disease characterized by overlapping phenotypes with different neurodegenerative disorders. Oligomers are considered the most toxic species in amyloid pathologies. We examined human AD brain samples using an anti-oligomer antibody generated in our laboratory and detected potential hybrid oligomers composed of amyloid-β, prion protein, α-synuclein, and TDP-43 phosphorylated at serines 409 and 410. These data and in vitro results suggest that Aβ oligomer seeds act as a template for the aggregation of other proteins and generate an overlapping phenotype with other neuronal disorders. Furthermore, these results could explain why anti-amyloid-β therapy has been unsuccessful.

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ER -

Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

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