Protein Kinases and Growth Associated Proteins in Plaque Formation in Alzheimer's Disease

1992 ◽  
Vol 3 (2) ◽  
Author(s):  
Eliezer Masliah ◽  
Margaret Mallory ◽  
Niangfe Ge ◽  
Tsunao Saitoh
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Kinases ◽  
Plaque Formation ◽  
Associated Proteins

scholarly journals Commonalities between Copper Neurotoxicity and Alzheimer’s Disease

Toxics ◽  
2021 ◽  
Vol 9 (1) ◽  
pp. 4
Author(s):  
Roshni Patel ◽  
Michael Aschner
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Structural Changes ◽  
Copper Ion ◽  
Plaque Formation ◽  
Ion Concentration ◽  
Medical Community ◽  
Disease Etiology ◽  
Parent Protein ◽  
Lead Zinc

Alzheimer’s disease, a highly prevalent form of dementia, targets neuron function beginning from the hippocampal region and expanding outwards. Alzheimer’s disease is caused by elevated levels of heavy metals, such as lead, zinc, and copper. Copper is found in many areas of daily life, raising a concern as to how this metal and Alzheimer’s disease are related. Previous studies have not identified the common pathways between excess copper and Alzheimer’s disease etiology. Our review corroborates that both copper and Alzheimer’s disease target the hippocampus, cerebral cortex, cerebellum, and brainstem, affecting motor skills and critical thinking. Additionally, Aβ plaque formation was analyzed beginning from synthesis at the APP parent protein site until Aβ plaque formation was completed. Structural changes were also noted. Further analysis revealed a relationship between amyloid-beta plaques and copper ion concentration. As copper ion levels increased, it bound to the Aβ monomer, expediting the plaque formation process, and furthering neurodegeneration. These conclusions can be utilized in the medical community to further research on the etiology of Alzheimer’s disease and its relationships to copper and other metal-induced neurotoxicity.

scholarly journals Ube3a deficiency inhibits amyloid plaque formation in APPswe/PS1δE9 mouse model of Alzheimer’s disease

2017 ◽  
Vol 26 (20) ◽  
pp. 4042-4054 ◽  
Author(s):  
Brijesh Kumar Singh ◽  
Naman Vatsa ◽  
Vipendra Kumar ◽  
Shashi Shekhar ◽  
Ankit Sharma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Mouse Model ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Model Of Alzheimer’S Disease

Distribution of beta amyloid associated proteins in plaques in Alzheimer's disease and in the non-demented elderly

1995 ◽  
Vol 4 (3) ◽  
pp. 291-297 ◽  
Author(s):  
Shan-Shan Zhan ◽  
Robert Veerhuis ◽  
Wouter Kamphorst ◽  
Piet Eikelenboom
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Beta Amyloid ◽  
Associated Proteins

Tau protein kinases: Involvement in Alzheimer's disease

2013 ◽  
Vol 12 (1) ◽  
pp. 289-309 ◽  
Author(s):  
Ludovic Martin ◽  
Xenia Latypova ◽  
Cornelia M. Wilson ◽  
Amandine Magnaudeix ◽  
Marie-Laure Perrin ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Kinases ◽  
Tau Protein

P2-241: Focal demyelination associated with amyloid plaque formation in Alzheimer's disease

2010 ◽  
Vol 6 ◽  
pp. S385-S385
Author(s):  
James Vickers ◽  
Stan Mitew ◽  
Matthew Kirkcaldie ◽  
Jerome Staal ◽  
Tracey Dickson
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Focal Demyelination

scholarly journals Network Analysis of a Membrane-Enriched Brain Proteome across Stages of Alzheimer’s Disease

Proteomes ◽  
2019 ◽  
Vol 7 (3) ◽  
pp. 30 ◽  
Author(s):  
Lenora Higginbotham ◽  
Eric Dammer ◽  
Duc Duong ◽  
Erica Modeste ◽  
Thomas Montine ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Network Analysis ◽  
Proteomic Analysis ◽  
Expression Patterns ◽  
Label Free ◽  
Post Mortem Brain ◽  
Brain Proteome ◽  
Associated Proteins ◽  
Membrane Bound

Previous systems-based proteomic approaches have characterized alterations in protein co-expression networks of unfractionated asymptomatic (AsymAD) and symptomatic Alzheimer’s disease (AD) brains. However, it remains unclear how sample fractionation and sub-proteomic analysis influences the organization of these protein networks and their relationship to clinicopathological traits of disease. In this proof-of-concept study, we performed a systems-based sub-proteomic analysis of membrane-enriched post-mortem brain samples from pathology-free control, AsymAD, and AD brains (n = 6 per group). Label-free mass spectrometry based on peptide ion intensity was used to quantify the 18 membrane-enriched fractions. Differential expression and weighted protein co-expression network analysis (WPCNA) were then used to identify and characterize modules of co-expressed proteins most significantly altered between the groups. We identified a total of 27 modules of co-expressed membrane-associated proteins. In contrast to the unfractionated proteome, these networks did not map strongly to cell-type specific markers. Instead, these modules were principally organized by their associations with a wide variety of membrane-bound compartments and organelles. Of these, the mitochondrion was associated with the greatest number of modules, followed by modules linked to the cell surface compartment. In addition, we resolved networks with strong associations to the endoplasmic reticulum, Golgi apparatus, and other membrane-bound organelles. A total of 14 of the 27 modules demonstrated significant correlations with clinical and pathological AD phenotypes. These results revealed that the proteins within individual compartments feature a heterogeneous array of AD-associated expression patterns, particularly during the preclinical stages of disease. In conclusion, this systems-based analysis of the membrane-associated AsymAD brain proteome yielded a unique network organization highly linked to cellular compartmentalization. Further study of this membrane-associated proteome may reveal novel insight into the complex pathways governing the earliest stages of disease.

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