@article {44385,
	title = {Advanced glycation end products modulate amyloidogenic APP processing and tau phosphorylation: a mechanistic link between glycation and the development of alzheimer{\textquoteright}s disease},
	journal = {ACS Chemical Neuroscience},
	volume = {9},
	year = {2018},
	month = {MAY},
	pages = {988-1000},
	abstract = {Advanced glycation end products (AGEs) are implicated in the pathology of Alzheimer{\textquoteright}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 A beta(1-)(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 A beta(1-)(42) formation and tau phosphorylation via increased cathepsin B and AEP, providing a new molecular link between AGEs and AD pathology.},
	doi = {10.1021/acschemneuro.7b00410},
	author = {Batkulwar, Kedar and Godbole, Rashmi and Banarjee, Reema and Kassaar, Omar and Williams, Robert J. and Kulkarni, Mahesh J.}
}
