scholarly journals Protein aggregation linked to Alzheimer's disease revealed by saturation transfer MRI

NeuroImage ◽  
2019 ◽  
Vol 188 ◽  
pp. 380-390 ◽  
Author(s):  
Lin Chen ◽  
Zhiliang Wei ◽  
Kannie W.Y. Chan ◽  
Shuhui Cai ◽  
Guanshu Liu ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregation ◽  
Saturation Transfer

Does protein aggregation drive postmitotic tissue degeneration?

2021 ◽  
Vol 13 (577) ◽  
pp. eaax0914 ◽  
Author(s):  
Jeffery W. Kelly
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Clinical Trials ◽  
Protein Aggregation ◽  
Protein Aggregate ◽  
Tissue Degeneration ◽  
Disease Modifying Therapies ◽  
Disease Modifying ◽  
Amyloid Diseases ◽  
Aggregate Structures

Pharmacological evidence, from clinical trials where patients with systemic amyloid diseases are treated with disease-modifying therapies, supports the notion that protein aggregation drives tissue degeneration in these disorders. The protein aggregate structures driving tissue pathology and the commonalities in etiology between these diseases and Alzheimer’s disease are under investigation.

scholarly journals A Novel Microtubule-Binding Drug Attenuates and Reverses Protein Aggregation in Animal Models of Alzheimer’s Disease

2019 ◽  
Vol 12 ◽  
Author(s):  
Samuel Kakraba ◽  
Srinivas Ayyadevara ◽  
Narsimha Reddy Penthala ◽  
Meenakshisundaram Balasubramaniam ◽  
Akshatha Ganne ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Animal Models ◽  
Protein Aggregation ◽  
Microtubule Binding

scholarly journals Monitoring protein aggregation and toxicity in Alzheimer’s disease mouse models using in vivo imaging

Methods ◽  
2011 ◽  
Vol 53 (3) ◽  
pp. 201-207 ◽  
Author(s):  
Tara L. Spires-Jones ◽  
Alix de Calignon ◽  
Melanie Meyer-Luehmann ◽  
Brian J. Bacskai ◽  
Bradley T. Hyman
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregation ◽  
Mouse Models ◽  
In Vivo Imaging

P2-092: MRI ANALYSIS BY CHEMICAL EXCHANGE SATURATION TRANSFER SHOWS LOW CEREBRAL 2-DEOXY-D-GLUCOSE UPTAKE IN A MODEL OF ALZHEIMER'S DISEASE

2006 ◽  
Vol 14 (7S_Part_13) ◽  
pp. P703-P703
Author(s):  
Daniele Tolomeo ◽  
Edoardo Micotti ◽  
Sonia Colombo Serra ◽  
Anniina Snellman ◽  
Michael Chappel ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Glucose Uptake ◽  
Chemical Exchange ◽  
Chemical Exchange Saturation Transfer ◽  
Saturation Transfer ◽  
Model Of Alzheimer’S Disease

scholarly journals In SilicoInsight into Potent of Anthocyanin Regulation of FKBP52 to Prevent Alzheimer’s Disease

2014 ◽  
Vol 2014 ◽  
pp. 1-20 ◽  
Author(s):  
Tzu-Chieh Hung ◽  
Tung-Ti Chang ◽  
Ming-Jen Fan ◽  
Cheng-Chun Lee ◽  
Calvin Yu-Chian Chen
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amino Acids ◽  
Protein Aggregation ◽  
Tau Protein ◽  
Hydrophobic Interactions ◽  
Dynamics Simulation ◽  
Binding Potential ◽  
Ligand Interaction ◽  
Structure Variation

Alzheimer’s disease (AD) is caused by the hyperphosphorylation of Tau protein aggregation. FKBP52 (FK506 binding protein 52) has been found to inhibit Tau protein aggregation. This study found six different kinds of anthocyanins that have high binding potential. After analyzing the docking positions, hydrophobic interactions, and hydrogen bond interactions, several amino acids were identified that play important roles in protein and ligand interaction. The proteins’ variation is described using eigenvectors and the distance between the amino acids during a molecular dynamics simulation (MD). This study investigates the three loops based around Glu85, Tyr113, and Lys121—all of which are important in inducing FKBP52 activation. By performing a molecular dynamic simulation process between unbound proteins and the protein complex with FK506, it was found that ligand targets that docked onto the FK1 domain will decrease the distance between Glu85/Tyr113 and Glu85/Lys121. The FKBP52 structure variation may induce FKBP52 activation and inhibit Tau protein aggregation. The results indicate that anthocyanins might change the conformation of FKBP52 during binding. In addition, the purple anthocyanins, such as cyanidin-3-glucoside and malvidin-3-glucoside, might be better than FK506 in regulating FKBP52 and treating Alzheimer’s disease.

scholarly journals Rivastigmine attenuates the Alzheimer's disease related protein degradation and apoptotic neuronal death signaling

2021 ◽  
Author(s):  
Parul Gupta ◽  
Shubhangini Tiwari ◽  
Abhishek Singh ◽  
Amit Pal ◽  
Amit Mishra ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregation ◽  
Er Stress ◽  
Protein Degradation ◽  
Acetylcholinesterase Activity ◽  
Inhibitory Effect ◽  
Proteasome Activity ◽  
Amyloid Aggregation ◽  
Biochemical Alterations

Rivastigmine is clinical drug for patients of Alzheimer’s disease (AD) exerting its inhibitory effect on acetylcholinesterase activity however, its effect on other disease related pathological mechanisms are not yet known. This study was conducted to evaluate the effect of rivastigmine on protein aggregation and degradation related mechanisms employing streptozotocin (STZ) induced experimental rat model. The known inhibitory effect of rivastigmine on cognition and acetylcholinesterase activity was observed in both cortex and hippocampus and further its effect on tau level, amyloid aggregation, biochemical alterations, endoplasmic reticulum (ER) stress, calcium homeostasis, proteasome activity and apoptosis was estimated. STZ administration in rat brain caused significant cognitive impairment, augmented acetylcholinesterase activity, tau phosphorylation and amyloid aggregation which were significantly inhibited with rivastigmine treatment. STZ also caused significant biochemical alterations which were attenuated with rivastigmine treatment. Since AD pathology is related to protein aggregation and we have found disease related amyloid aggregation, further the investigation was done to decipher the ER functionality and apoptotic signalling. STZ caused significantly altered level of ER stress related markers (GRP78, GADD153 and caspase-12) which were significantly inhibited with rivastigmine treatment. Further the effect of rivastigmine was estimated on proteasome activity in both regions. Rivastigmine treatment significantly enhances the proteasome activity and may contributes in removal of amyloid aggregation. In conclusion, findings suggested that along with inhibitory effect of rivastigmine on acetylcholinesterase activity and up to some extent on cognition, it has significant effect on disease related biochemical alterations, ER functionality, protein degradation machinery and neuronal apoptosis.

Sign in / Sign up

Export Citation Format

Share Document