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Quaternary Structure Defines a Large Class of Amyloid-ß Oligomers Neutralized by Sequestration.
Liu, Peng; Reed, Miranda N; Kotilinek, Linda A; Grant, Marianne K O; Forster, Colleen L; Qiang, Wei; Shapiro, Samantha L; Reichl, John H; Chiang, Angie C A; Jankowsky, Joanna L; Wilmot, Carrie M; Cleary, James P; Zahs, Kathleen R; Ashe, Karen H.
Afiliação
  • Liu P; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Reed MN; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Kotilinek LA; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Grant MK; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Forster CL; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA; UMN Academic Health Center Biological Materials Procurement Network, University of Minnesota, Minneapolis, MN 55455, USA.
  • Qiang W; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
  • Shapiro SL; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Reichl JH; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Chiang AC; Departments of Neuroscience, Neurology and Neurosurgery, Huffington Center on Aging, Baylor College of Medicine, Houston, TX 77030, USA.
  • Jankowsky JL; Departments of Neuroscience, Neurology and Neurosurgery, Huffington Center on Aging, Baylor College of Medicine, Houston, TX 77030, USA.
  • Wilmot CM; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • Cleary JP; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA; Geriatric Research, Education and Clinical Center (GRECC), VA Medical Center, Minneapolis, MN 55417, USA.
  • Zahs KR; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA.
  • Ashe KH; Department of Neurology, University of Minnesota, Minneapolis, MN 55455, USA; N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455, USA; Department of Neuroscience, University of Minnesota, Minneapolis, MN 55455, USA; Geriatric Research, Education and C
Cell Rep ; 11(11): 1760-71, 2015 Jun 23.
Article em En | MEDLINE | ID: mdl-26051935
ABSTRACT
The accumulation of amyloid-ß (Aß) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in the living brain. Here we show that Aß oligomers can be assigned to one of at least two classes (type 1 and type 2) based on their temporal, spatial, and structural relationships to amyloid fibrils. The type 2 oligomers are related to amyloid fibrils and represent the majority of oligomers generated in vivo, but they remain confined to the vicinity of amyloid plaques and do not impair cognition at levels relevant to AD. Type 1 oligomers are unrelated to amyloid fibrils and may have greater potential to cause global neural dysfunction in AD because they are dispersed. These results refine our understanding of the pathogenicity of Aß oligomers in vivo.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos beta-Amiloides / Placa Amiloide / Estrutura Quaternária de Proteína / Doença de Alzheimer / Agregação Patológica de Proteínas Limite: Animals / Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos beta-Amiloides / Placa Amiloide / Estrutura Quaternária de Proteína / Doença de Alzheimer / Agregação Patológica de Proteínas Limite: Animals / Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article