A possible role of glycation in the regulation of amyloid β precursor protein processing leading to amyloid β accumulation

2020 ◽  
Vol 142 ◽  
pp. 109799
Author(s):  
Gouri V. Patil ◽  
Rakesh S. Joshi ◽  
Rubina S. Kazi ◽  
Shabda E. Kulsange ◽  
Mahesh J. Kulkarni
Keyword(s):  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein

scholarly journals Effects of Huanglian-Jie-Du-Tang and Its Modified Formula on the Modulation of Amyloid-β Precursor Protein Processing in Alzheimer's Disease Models

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e92954 ◽  
Author(s):  
Siva Sundara Kumar Durairajan ◽  
Ying-Yu Huang ◽  
Pui-Yee Yuen ◽  
Lei-Lei Chen ◽  
Ka-Yan Kwok ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Disease Models ◽  
Modified Formula

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

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.

Role of acetylcholinesterase inhibitors in pharmacological regulation of amyloid precursor protein processing

2006 ◽  
Vol 18 (2) ◽  
pp. 149-152 ◽  
Author(s):  
Marco Racchi ◽  
Emanuela Porrello ◽  
Cristina Lanni ◽  
Silvia Carolina Lenzken ◽  
Michela Mazzucchelli ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Acetylcholinesterase Inhibitors ◽  
Protein Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Pharmacological Regulation

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

Novel heparan sulphate analogues: inhibition of β-secretase cleavage of amyloid precursor protein

2005 ◽  
Vol 33 (5) ◽  
pp. 1116-1118 ◽  
Author(s):  
S.J. Patey ◽  
E.A. Yates ◽  
J.E. Turnbull
Keyword(s):  
Amyloid Precursor Protein ◽  
Heparan Sulphate ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Amyloid Β Peptide ◽  
Neuritic Plaques ◽  
Rate Limiting Step ◽  
Aβ Amyloid ◽  
Ad Alzheimer’S Disease

The role of HS (heparan sulphate) in the pathology of AD (Alzheimer's disease) is multifaceted. HS and other glycosaminoglycans have been widely reported to be associated with neuritic plaques. HS has also been shown to promote the aggregation of Aβ (amyloid β-peptide), the proteinaceous component of neuritic plaques. Recently, we described a novel and contrasting role for HS in the pathology of AD: HS can inhibit the formation of Aβ, by directly interacting with the protease BACE1 (β-site amyloid precursor protein cleaving enzyme 1; β-secretase 1), that cleaves the amyloid precursor protein and is the rate limiting step in the generation of Aβ. Here, we review the current roles of HS and the potential for HS-derivatives in the treatment of AD.

Sign in / Sign up

Export Citation Format

Share Document