4.8 Article

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

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CELL REPORTS
卷 21, 期 9, 页码 2614-2627

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CELL PRESS
DOI: 10.1016/j.celrep.2017.11.009

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  1. NIH [F32AG039127, R00DC013805, R01MH067880, P41GM103533, P30CA060553]
  2. Fonds de Recherche du Quebec-Nature et Technologies fellowship

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Amyloid beta (A beta) 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 Ab levels. Taken together with prior findings on ApoE driving Ab accumulation, this analysis points to a pathological dysregulation of the ApoE-Ab axis. We also found dysregulation of protein networks involved in excitatory synaptic transmission. Analysis of the AMPA receptor (AMPAR) complex revealed specific loss of TARPg-2, a key AMPAR-trafficking protein. Expression of TARPg-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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