scholarly journals Significance of cytosolic cathepsin D in Alzheimer's disease pathology: Protective cellular effects of PLGA nanoparticles against β‐amyloid‐toxicity

2020 ◽  
Vol 46 (7) ◽  
pp. 686-706 ◽  
Author(s):  
Y. Wang ◽  
Q. Wu ◽  
B. G. Anand ◽  
G. Karthivashan ◽  
G. Phukan ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cathepsin D ◽  
Plga Nanoparticles ◽  
Cellular Effects ◽  
Amyloid Toxicity ◽  
Β Amyloid

PLGA-Based Curcumin Delivery System: An Interesting Therapeutic Approach in Treatment of Alzheimer’s Disease

2021 ◽  
Vol 19 ◽  
Author(s):  
Sanaz Keshavarz Shahbaz ◽  
Khadijeh Koushki ◽  
Thozhukat Sathyapalan ◽  
Muhammed Majeed ◽  
Amirhossein Sahebkar
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neurological Disorders ◽  
Neurodegenerative Disorder ◽  
Aqueous Solubility ◽  
Plga Nanoparticles ◽  
Progressive Degeneration ◽  
Hyperphosphorylated Tau Protein ◽  
Amyloid Aβ ◽  
Β Amyloid

: Progressive degeneration and dysfunction of the nervous system because of oxidative stress, aggregations of misfolded proteins, and neuroinflammation are the key pathological features of neurodegenerative diseases. Alzheimer's disease is a chronic neurodegenerative disorder driven by uncontrolled extracellular deposition of β-amyloid (Aβ) in the amyloid plaques and intracellular accumulation of hyperphosphorylated tau protein. Curcumin is a hydrophobic polyphenol with noticeable neuroprotective and anti-inflammatory effects that can cross the blood-brain barrier. Therefore, it is widely studied for the alleviation of inflammatory and neurological disorders. However, the clinical application of curcumin is limited due to its low aqueous solubility and bioavailability. Recently, nano-based curcumin delivery systems are developed to overcome these limitations effectively. This review article discusses the effects and potential mechanisms of curcumin-loaded PLGA nanoparticles in Alzheimer’s disease.

scholarly journals P2-306: Puromycin-sensitive aminopeptidase rescues β-amyloid toxicity in Alzheimer's disease

2011 ◽  
Vol 7 ◽  
pp. S408-S408
Author(s):  
Antonina Kruppa ◽  
Dhia Chandraratna ◽  
James Irving ◽  
Stefan Marciniak ◽  
Matthew Townsend ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Toxicity ◽  
Β Amyloid

scholarly journals Involvement of glutaredoxin-1 and thioredoxin-1 in β-amyloid toxicity and Alzheimer's disease

2005 ◽  
Vol 13 (9) ◽  
pp. 1454-1465 ◽  
Author(s):  
S Akterin ◽  
R F Cowburn ◽  
A Miranda-Vizuete ◽  
A Jiménez ◽  
N Bogdanovic ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Toxicity ◽  
Thioredoxin 1 ◽  
Β Amyloid

scholarly journals Alternative pathways for production of β-amyloid peptides of Alzheimer's disease

2008 ◽  
Vol 389 (8) ◽  
Author(s):  
Vivian Hook ◽  
Israel Schechter ◽  
Hans-Ulrich Demuth ◽  
Gregory Hook
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Posttranslational Modifications ◽  
Cathepsin B ◽  
Cathepsin D ◽  
General Meeting ◽  
Glutaminyl Cyclase ◽  
Alternative Pathways ◽  
Β Amyloid ◽  
Bace 1

Abstract This highlight article describes three Alzheimer's disease (AD) studies presented at the 5th General Meeting of the International Proteolysis Society that address enzymatic mechanisms for producing neurotoxic β-amyloid (Aβ) peptides. One group described the poor kinetics of BACE 1 for cleaving the wild-type (WT) β-secretase site of APP found in most AD patients. They showed that cathepsin D displays BACE 1-like specificity and cathepsin D is 280-fold more abundant in human brain than BACE 1. Nevertheless, as BACE 1 and cathepsin D show poor activity towards the WT β-secretase site, they suggested continuing the search for additional β-secretase(s). The second group reported cathepsin B as an alternative β-secretase possessing excellent kinetic efficiency and specificity for the WT β-secretase site. Significantly, inhibitors of cathepsin B improved memory, with reduced amyloid plaques and decreased Aβ(40/42) in brains of AD animal models expressing amyloid precursor protein containing the WT β-secretase site. The third group addressed isoaspartate and pyroglutamate (pGlu) posttranslational modifications of Aβ. Results showed that cathepsin B, but not BACE 1, efficiently cleaves the WT β-secretase isoaspartate site. Furthermore, cyclization of N-terminal Glu by glutaminyl cyclase generates highly amyloidogenic pGluAβ(3–40/42). These presentations suggest cathepsin B and glutaminyl cyclase as potential new AD therapeutic targets.

Аnticholinesterase and antioxidant activity of new binary conjugates of (с)-carbolines

2019 ◽  
Vol 484 (1) ◽  
pp. 104-108
Author(s):  
G. F. Makhaeva ◽  
E. F. Shevtsova ◽  
N. P. Boltneva ◽  
N. V. Kovaleva ◽  
E. V. Rudakova ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Antioxidant Activity ◽  
Anticholinesterase Activity ◽  
Amyloid Aggregation ◽  
Varying Length ◽  
Β Amyloid ◽  
New Compounds

This study presents the synthesis of binary tetrohydro-γ-carbolines with ditriazol spacers of varying length, which exhibit anticholinesterase and antioxidant activity, as compared to the original Dimebon prototype. Anticholinesterase activity suggests the potential ability of the new compounds to block β-amyloid aggregation induced by anticholinesterase, making them promising candidates for further research preparations for the treatment of Alzheimer's disease. Particular attention should be paid to the conjugate with an intertriazol hexamethylene spacer, which can be regarded as the leading compound in this series.

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