scholarly journals The common inhalation anesthetic isoflurane induces caspase activation and increases amyloid β-protein level in vivo

2008 ◽  
Vol 64 (6) ◽  
pp. 618-627 ◽  
Author(s):  
Zhongcong Xie ◽  
Deborah J. Culley ◽  
Yuanlin Dong ◽  
Guohua Zhang ◽  
Bin Zhang ◽  
...  
Keyword(s):  
Protein Level ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Caspase Activation ◽  
Inhalation Anesthetic ◽  
Β Protein ◽  
The Common

scholarly journals The Inhalation Anesthetic Desflurane Induces Caspase Activation and Increases Amyloid β-Protein Levels under Hypoxic Conditions

2008 ◽  
Vol 283 (18) ◽  
pp. 11866-11875 ◽  
Author(s):  
Bin Zhang ◽  
Yuanlin Dong ◽  
Guohua Zhang ◽  
Robert D. Moir ◽  
Weiming Xia ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Caspase Activation ◽  
Protein Levels ◽  
Hypoxic Conditions ◽  
Inhalation Anesthetic ◽  
Β Protein

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Nature ◽  
2002 ◽  
Vol 416 (6880) ◽  
pp. 535-539 ◽  
Author(s):  
Dominic M. Walsh ◽  
Igor Klyubin ◽  
Julia V. Fadeeva ◽  
William K. Cullen ◽  
Roger Anwyl ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Term Potentiation

scholarly journals Mutation of the Kunitz-type proteinase inhibitor domain in the amyloid β-protein precursor abolishes its anti-thrombotic properties in vivo

2017 ◽  
Vol 155 ◽  
pp. 58-64 ◽  
Author(s):  
Feng Xu ◽  
Judianne Davis ◽  
Michael Hoos ◽  
William E. Van Nostrand
Keyword(s):  
Proteinase Inhibitor ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein ◽  
Kunitz Type

scholarly journals Upregulation of Alzheimer’s Disease Amyloid-β Protein Precursor in Astrocytes Both in vitro and in vivo

2020 ◽  
pp. 1-12 ◽  
Author(s):  
Yingxia Liang ◽  
Frank Raven ◽  
Joseph F. Ward ◽  
Sherri Zhen ◽  
Siyi Zhang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein

271 Pharmacological manipulation of Alzheimer's amyloid β protein in vitro and in vivo

1996 ◽  
Vol 17 (4) ◽  
pp. S68
Author(s):  
C.B. Eckman ◽  
C.-M. Prada ◽  
A. Fauq ◽  
S.G. Younkin
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Pharmacological Manipulation ◽  
Β Protein

scholarly journals The molecular tweezer CLR01 improves behavioral deficits and reduces tau pathology in P301S-tau transgenic mice

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Jing Di ◽  
Ibrar Siddique ◽  
Zizheng Li ◽  
Ghattas Malki ◽  
Simon Hornung ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Muscle Strength ◽  
Mouse Model ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Tau Pathology ◽  
Behavioral Deficits ◽  
Β Protein

Abstract Background Molecular tweezers (MTs) are broad-spectrum inhibitors of abnormal protein aggregation. A lead MT, called CLR01, has been demonstrated to inhibit the aggregation and toxicity of multiple amyloidogenic proteins in vitro and in vivo. Previously, we evaluated the effect of CLR01 in the 3 × Tg mouse model of Alzheimer’s disease, which overexpresses mutant human presenilin 1, amyloid β-protein precursor, and tau and found that subcutaneous administration of the compound for 1 month led to a robust reduction of amyloid plaques, neurofibrillary tangles, and microgliosis. CLR01 also has been demonstrated to inhibit tau aggregation in vitro and tau seeding in cell culture, yet because in Alzheimer’s disease (AD) and in the 3 × Tg model, tau hyperphosphorylation and aggregation are thought to be downstream of Aβ insults, the study in this model left open the question whether CLR01 affected tau in vivo directly or indirectly. Methods To determine if CLR01 could ameliorate tau pathology directly in vivo, we tested the compound similarly using the P301S-tau (line PS19) mouse model. Mice were administered 0.3 or 1.0 mg/kg per day CLR01 and tested for muscle strength and behavioral deficits, including anxiety- and disinhibition-like behavior. Their brains then were analyzed by immunohistochemical and biochemical assays for pathological forms of tau, neurodegeneration, and glial pathology. Results CLR01 treatment ameliorated muscle-strength deterioration, anxiety-, and disinhibition-like behavior. Improved phenotype was associated with decreased levels of pathologic tau forms, suggesting that CLR01 exerts a direct effect on tau in vivo. Limitations of the study included a relatively short treatment period of the mice at an age in which full pathology is not yet developed. In addition, high variability in this model lowered the statistical significance of the findings of some outcome measures. Conclusions The findings suggest that CLR01 is a particularly attractive candidate for the treatment of AD because it targets simultaneously the two major pathogenic proteins instigating and propagating the disease, amyloid β-protein (Aβ), and tau, respectively. In addition, our study suggests that CLR01 can be used for the treatment of other tauopathies in the absence of amyloid pathology.

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