Amyloid Accumulation Drives Proteome-wide Alterations in Mouse Models of Alzheimer’s Disease-like Pathology | Zendy

Jeffrey N. Savas | Zendy; Yizhi Wang | Zendy; Laura A. DeNardo | Zendy; Salvador MartínezBartolomé | Zendy; Daniel B. McClatchy | Zendy; Timothy J. Hark | Zendy; Natalie F. Shanks | Zendy; Kira Cozzolino | Zendy; Mathieu LavalléeAdam | Zendy; Samuel N. Smukowski | Zendy; Sung Kyu Park | Zendy; Jeffery W. Kelly | Zendy; Edward H. Koo | Zendy; Terunaga Nakagawa | Zendy; Eliezer Masliah | Zendy; Anirvan Ghosh | Zendy; John R. Yates | Zendy

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Amyloid Accumulation Drives Proteome-wide Alterations in Mouse Models of Alzheimer’s Disease-like Pathology

Author(s) -

Jeffrey N. Savas,

Yizhi Wang,

Laura A. DeNardo,

Salvador MartínezBartolomé,

Daniel B. McClatchy,

Timothy J. Hark,

Natalie F. Shanks,

Kira Cozzolino,

Mathieu LavalléeAdam,

Samuel N. Smukowski,

Sung Kyu Park,

Jeffery W. Kelly,

Edward H. Koo,

Terunaga Nakagawa,

Eliezer Masliah,

Anirvan Ghosh,

John R. Yates

Publication year - 2017

Publication title -

cell reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.264

H-Index - 154

eISSN - 2639-1856

pISSN - 2211-1247

DOI - 10.1016/j.celrep.2017.11.009

Subject(s) - ampa receptor , proteome , genetically modified mouse , apolipoprotein e , biology , neuroscience , amyloid (mycology) , neurodegeneration , transgene , amyloid precursor protein , amyloid beta , disease , microbiology and biotechnology , alzheimer's disease , receptor , pathology , glutamate receptor , medicine , bioinformatics , gene , biochemistry

Amyloid beta (Aβ) peptides impair multiple cellular pathways and play a causative role in Alzheimer's disease (AD) pathology, but how the brain proteome is remodeled by this process is unknown. To identify protein networks associated with AD-like pathology, we performed global quantitative proteomic analysis in three mouse models at young and old ages. Our analysis revealed a robust increase in Apolipoprotein E (ApoE) levels in nearly all brain regions with increased Aβ levels. Taken together with prior findings on ApoE driving Aβ accumulation, this analysis points to a pathological dysregulation of the ApoE-Aβ axis. We also found dysregulation of protein networks involved in excitatory synaptic transmission. Analysis of the AMPA receptor (AMPAR) complex revealed specific loss of TARPγ-2, a key AMPAR-trafficking protein. Expression of TARPγ-2 in hAPP transgenic mice restored AMPA currents. This proteomic database represents a resource for the identification of protein alterations responsible for AD.

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