TASTPM Mice Expressing Amyloid Precursor Protein and Presenilin-1 Mutant Transgenes Are Sensitive to γ-Secretase Modulation and Amyloid-β42 Lowering by GSM-10h

2011 ◽  
Vol 8 (1-2) ◽  
pp. 15-24 ◽  
Author(s):  
Ishrut Hussain ◽  
David C. Harrison ◽  
Julie Hawkins ◽  
Trevor Chapman ◽  
Ian Marshall ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Presenilin 1

Presenilin 1 Regulates the Processing of β-Amyloid Precursor Protein C-Terminal Fragments and the Generation of Amyloid β-Protein in Endoplasmic Reticulum and Golgi†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16465-16471 ◽  
Author(s):  
Weiming Xia ◽  
Jimin Zhang ◽  
Beth L. Ostaszewski ◽  
William Taylor Kimberly ◽  
Peter Seubert ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Amyloid Precursor Protein ◽  
Protein C ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Presenilin 1 ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Β Amyloid

scholarly journals Oral Treponema denticola infection induces Aβ1-40 and Aβ1-42 accumulation in the hippocampus of C57BL/6 mice

2021 ◽  
Author(s):  
Xinyi Su ◽  
Zhiqun Tang ◽  
Yuqiu Liu ◽  
Wanzhi He ◽  
Jiapei Jiang ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Porphyromonas Gingivalis ◽  
Neuronal Cells ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Presenilin 1 ◽  
Central Component ◽  
Treponema Denticola ◽  
Periodontal Pathogens ◽  
The Brain

Abstract Accumulation of amyloid-β (Aβ) in the brain is a central component of pathology in Alzheimer’s disease. A growing number of evidences demonstrate close associations between periodontal pathogens including Porphyromonas gingivalis (P. gingivalis) and Treponema denticola (T. denticola) and AD. However, the effect and mechanisms of T. denticola on accumulation of Aβ remain to be unclear. In this study, we demonstrated that T. denticola was able to enter brain and act directly on nerve cells resulting in intra and extracellular Aβ1−40 and Aβ1−42 accumulation in the hippocampus of C57BL/6 mice by selectively activating both β-secretase and γ-secretase. Furthermore, both KMI1303, an inhibitor of β- secretase, as well as DAPT, an inhibitor of γ- secretase were found to be able to inhibit the effect of T. denticola on Aβ accumulation in N2a neuronal cells. Overall, it is concluded that T. denticola increases the expression of Aβ1−42 and Aβ1−40 by its regulation on beta-site amyloid precursor protein cleaving enzyme-1 and Presenilin 1.

scholarly journals The Role of Presenilin-1 in the γ-Secretase Cleavage of the Amyloid Precursor Protein of Alzheimer's Disease

2000 ◽  
Vol 275 (3) ◽  
pp. 1525-1528 ◽  
Author(s):  
Jean-Noël Octave ◽  
Rachid Essalmani ◽  
Bernadette Tasiaux ◽  
Jean Menager ◽  
Christian Czech ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Presenilin 1

A Numerical Study of Sensitivity Coefficients for a Model of Amyloid Precursor Protein and Tubulin-Associated Unit Protein Transport and Agglomeration in Neurons at the Onset of Alzheimer's Disease

2019 ◽  
Vol 141 (3) ◽  
Author(s):  
I. A. Kuznetsov ◽  
A. V. Kuznetsov
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Precursor Protein ◽  
Tau Protein ◽  
Protein Transport ◽  
Numerical Study ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Model Parameters ◽  
In The Beginning

Modeling of intracellular processes occurring during the development of Alzheimer's disease (AD) can be instrumental in understanding the disease and can potentially contribute to finding treatments for the disease. The model of intracellular processes in AD, which we previously developed, contains a large number of parameters. To distinguish between more important and less important parameters, we performed a local sensitivity analysis of this model around the values of parameters that give the best fit with published experimental results. We show that the influence of model parameters on the total concentrations of amyloid precursor protein (APP) and tubulin-associated unit (tau) protein in the axon is reciprocal to the influence of the same parameters on the average velocities of the same proteins during their transport in the axon. The results of our analysis also suggest that in the beginning of AD the aggregation of amyloid-β and misfolded tau protein have little effect on transport of APP and tau in the axon, which suggests that early damage in AD may be reversible.

scholarly journals Amyloid-β Peptide Exacerbates the Memory Deficit Caused by Amyloid Precursor Protein Loss-of-Function in Drosophila

PLoS ONE ◽  
2015 ◽  
Vol 10 (8) ◽  
pp. e0135741 ◽  
Author(s):  
Isabelle Bourdet ◽  
Aurélie Lampin-Saint-Amaux ◽  
Thomas Preat ◽  
Valérie Goguel
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Memory Deficit ◽  
Precursor Protein ◽  
Amyloid Β Peptide ◽  
Loss Of Function ◽  
Protein Loss

scholarly journals P3-385: Presenilin 1 is involved in the maturation of beta-site amyloid precursor protein-cleaving enzyme 1(BACE1)

2006 ◽  
Vol 2 ◽  
pp. S489-S489
Author(s):  
Akira Kuzuya ◽  
Kengo Uemura ◽  
Ayae Kinoshita ◽  
Shun Shimohama
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Presenilin 1
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