Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls.

ABSTRACT: Neurodegenerative diseases are distinguished by characteristic protein aggregates initiated by disease-specific 'seed' proteins; however, roles of other co-aggregated proteins remain largely unexplored. Compact hippocampal aggregates were purified from Alzheimer's and control-subject pools using magnetic-bead immunoaffinity pulldowns. Their components were fractionated by electrophoretic mobility and analyzed by high-resolution proteomics. Although total detergent-insoluble aggregates from Alzheimer's and controls had similar protein content, within the fractions isolated by tau or Aβ1-42 pulldown, the protein constituents of Alzheimer-derived aggregates were more abundant, diverse, and post-translationally modified than those from controls. Tau- and Aβ-containing aggregates were distingui

SUBMITTER: Ayyadevara S 

PROVIDER: S-EPMC5013017 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature