scholarly journals Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production

2017 ◽  
Vol 292 (9) ◽  
pp. 3751-3767 ◽  
Author(s):  
Hermeto Gerber ◽  
Fang Wu ◽  
Mitko Dimitrov ◽  
Guillermo M. Garcia Osuna ◽  
Patrick C. Fraering
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Amyloid Β Peptide

scholarly journals A cellular model of amyloid precursor protein processing and amyloid-β peptide production

2014 ◽  
Vol 223 ◽  
pp. 114-122 ◽  
Author(s):  
MiMi P. Macias ◽  
Amanda M. Gonzales ◽  
Ashley L. Siniard ◽  
Aaron W. Walker ◽  
Jason J. Corneveaux ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Amyloid Β Peptide ◽  
Cellular Model

Impact of Vitamin D on Amyloid Precursor Protein Processing and Amyloid-β Peptide Degradation in Alzheimer's Disease

2013 ◽  
Vol 13 (2-3) ◽  
pp. 75-81 ◽  
Author(s):  
Marcus O.W. Grimm ◽  
Johannes Lehmann ◽  
Janine Mett ◽  
Valerie C. Zimmer ◽  
Sven Grösgen ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Vitamin D ◽  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Amyloid Β Peptide ◽  
Peptide Degradation

Fe65 Ser228 is phosphorylated by ATM/ATR and inhibits Fe65–APP-mediated gene transcription

2015 ◽  
Vol 465 (3) ◽  
pp. 413-421 ◽  
Author(s):  
Paul A. Jowsey ◽  
Peter G. Blain
Keyword(s):  
Amyloid Precursor Protein ◽  
Gene Transcription ◽  
Transcriptional Activity ◽  
Phosphorylation Site ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Protein Fragment ◽  
Active Protein

APP (amyloid precursor protein) processing generates cytotoxic amyloid β-peptides (Aβ) and a transcriptionally active protein fragment (AICD). In the present study, we identify a novel ATM/ATR phosphorylation site in the APP-binding protein Fe65. Phosphorylation of this site decreases the transcriptional activity of the Fe65–APP complex.

TUDCA, a Bile Acid, Attenuates Amyloid Precursor Protein Processing and Amyloid-β Deposition in APP/PS1 Mice

2012 ◽  
Vol 45 (3) ◽  
pp. 440-454 ◽  
Author(s):  
Ana F. Nunes ◽  
Joana D. Amaral ◽  
Adrian C. Lo ◽  
Maria B. Fonseca ◽  
Ricardo J. S. Viana ◽  
...  
Keyword(s):  
Bile Acid ◽  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing

scholarly journals Erratum: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production

Nature ◽  
2007 ◽  
Vol 446 (7133) ◽  
pp. 342-342 ◽  
Author(s):  
L. Pastorino ◽  
A. Sun ◽  
P.-J. Lu ◽  
X. Z. Zhou ◽  
M. Balastik ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Prolyl Isomerase

scholarly journals AMPA Receptor Activation Promotes Non-Amyloidogenic Amyloid Precursor Protein Processing and Suppresses Neuronal Amyloid-β Production

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e78155 ◽  
Author(s):  
Sarah E. Hoey ◽  
Federica Buonocore ◽  
Carla J. Cox ◽  
Victoria J. Hammond ◽  
Michael S. Perkinton ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Ampa Receptor ◽  
Amyloid Β ◽  
Receptor Activation ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing

The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production

Nature ◽  
2006 ◽  
Vol 440 (7083) ◽  
pp. 528-534 ◽  
Author(s):  
Lucia Pastorino ◽  
Anyang Sun ◽  
Pei-Jung Lu ◽  
Xiao Zhen Zhou ◽  
Martin Balastik ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Prolyl Isomerase

scholarly journals Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing

2008 ◽  
Vol 183 (2) ◽  
pp. 339-352 ◽  
Author(s):  
Takashi Sakurai ◽  
Kumi Kaneko ◽  
Misako Okuno ◽  
Koji Wada ◽  
Taku Kashiyama ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Molecular Mechanisms ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Amyloid Β Peptide ◽  
Dependent Manner ◽  
App Processing ◽  
Membrane Microdomain ◽  
Activity Dependent

Neuronal activity has an impact on β cleavage of amyloid precursor protein (APP) by BACE1 to generate amyloid-β peptide (Aβ). However, the molecular mechanisms underlying this effect remain to be elucidated. Cholesterol dependency of β cleavage prompted us to analyze immunoisolated APP-containing detergent-resistant membranes from rodent brains. We found syntaxin 1 as a key molecule for activity-dependent regulation of APP processing in cholesterol-dependent microdomains. In living cells, APP associates with syntaxin 1–containing microdomains through X11–Munc18, which inhibits the APP–BACE1 interaction and β cleavage via microdomain segregation. Phosphorylation of Munc18 by cdk5 causes a shift of APP to BACE1-containing microdomains. Neuronal hyperactivity, implicated in Aβ overproduction, promotes the switching of APP microdomain association as well as β cleavage in a partially cdk5-dependent manner. We propose that microdomain switching is a mechanism of cholesterol- and activity-dependent regulation of APP processing in neurons.

Sign in / Sign up

Export Citation Format

Share Document