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Advanced Glycation End Products Modulate Amyloidogenic APP Processing and Tau Phosphorylation: A Mechanistic Link between Glycation and the Development of Alzheimer’s Disease

  • Kedar Batkulwar
    Kedar Batkulwar
    Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India
    Academy of Scientific and Innovative Research (AcSIR), CSIR-National Chemical Laboratory, Pune-411008, India
  • Rashmi Godbole
    Rashmi Godbole
    Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India
  • Reema Banarjee
    Reema Banarjee
    Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India
    Academy of Scientific and Innovative Research (AcSIR), CSIR-National Chemical Laboratory, Pune-411008, India
  • Omar Kassaar
    Omar Kassaar
    Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
    More by Omar Kassaar
  • Robert J. Williams*
    Robert J. Williams
    Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
    *E-mail: [email protected]
  • , and 
  • Mahesh J. Kulkarni*
    Mahesh J. Kulkarni
    Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India
    Academy of Scientific and Innovative Research (AcSIR), CSIR-National Chemical Laboratory, Pune-411008, India
    *E-mail: [email protected]
Cite this: ACS Chem. Neurosci. 2018, 9, 5, 988–1000
Publication Date (Web):January 31, 2018
Copyright © 2018 American Chemical Society

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    Abstract Image

    Advanced glycation end products (AGEs) are implicated in the pathology of Alzheimer’s disease (AD), as they induce neurodegeneration following interaction with the receptor for AGE (RAGE). This study aimed to establish a mechanistic link between AGE-RAGE signaling and AD pathology. AGE-induced changes in the neuro2a proteome were monitored by SWATH-MS. Western blotting and cell-based reporter assays were used to investigate AGE-RAGE regulated APP processing and tau phosphorylation in primary cortical neurons. Selected protein expression was validated in brain samples affected by AD. The AGE-RAGE axis altered proteome included increased expression of cathepsin B and asparagine endopeptidase (AEP), which mediated an increase in Aβ1–42 formation and tau phosphorylation, respectively. Elevated cathepsin B, AEP, RAGE, and pTau levels were found in human AD brain, coincident with enhanced AGEs. This study demonstrates that the AGE-RAGE axis regulates Aβ1–42 formation and tau phosphorylation via increased cathepsin B and AEP, providing a new molecular link between AGEs and AD pathology.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acschemneuro.7b00410.

    • Supplemental methods and figures. Table S1. List of glycated peptides identified by high resolution accurate mass spectrometry. Table S3. List of differentially regulated proteins upon AGE induction. Table S4. Functional annotation of the GO process by DAVID analysis (PDF)

    • Table S2. List of identified proteins and peptides (XLSX)

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