Memory Loss and the Onset of Alzheimer’s Disease Could Be Under the Control of Extracellular Heat Shock Proteins

2018 ◽  
Vol 63 (3) ◽  
pp. 927-934 ◽  
Author(s):  
Nelson Arispe ◽  
Antonio De Maio
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Memory Loss ◽  
Shock Proteins

scholarly journals Quantitative phosphoproteomics of Alzheimer's disease reveals cross-talk between kinases and small heat shock proteins

PROTEOMICS ◽  
2014 ◽  
Vol 15 (2-3) ◽  
pp. 508-519 ◽  
Author(s):  
Eric B. Dammer ◽  
Andrew K. Lee ◽  
Duc M. Duong ◽  
Marla Gearing ◽  
James J. Lah ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cross Talk ◽  
Small Heat Shock Proteins ◽  
Shock Proteins ◽  
Quantitative Phosphoproteomics

scholarly journals Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018 ◽  
Vol 19 (9) ◽  
pp. 2603 ◽  
Author(s):  
Claudia Campanella ◽  
Andrea Pace ◽  
Celeste Caruso Bavisotto ◽  
Paola Marzullo ◽  
Antonella Marino Gammazza ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Protein Misfolding ◽  
Point Of View ◽  
Toxic Species ◽  
Shock Proteins

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60, Hsp70 and Hsp90. The role of these proteins in AD is highlighted from a biological point of view. Pharmacological targeting of such HSPs with inhibitors or regulators is also discussed.

scholarly journals Alzheimer Cells on Their Way to Derailment Show Selective Changes in Protein Quality Control Network

2020 ◽  
Vol 7 ◽  
Author(s):  
Margreet B. Koopman ◽  
Stefan G. D. Rüdiger
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Quality Control ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Brain Regions ◽  
Control Network ◽  
Shock Proteins

Alzheimer’s Disease is driven by protein aggregation and is characterized by accumulation of Tau protein into neurofibrillary tangles. In healthy neurons the cellular protein quality control is successfully in charge of protein folding, which raises the question to which extent this control is disturbed in disease. Here, we describe that brain cells in Alzheimer’s Disease show very specific derailment of the protein quality control network. We performed a meta-analysis on the Alzheimer’s Disease Proteome database, which provides a quantitative assessment of disease-related proteome changes in six brain regions in comparison to age-matched controls. We noted that levels of all paralogs of the conserved Hsp90 chaperone family are reduced, while most other chaperones – or their regulatory co-chaperones - do not change in disease. The notable exception is a select group consisting of the stress inducible HSP70, its nucleotide exchange factor BAG3 – which links the Hsp70 system to autophagy - and neuronal small heat shock proteins, which are upregulated in disease. They are all members of a cascade controlled in the stress response, channeling proteins towards a pathway of chaperone assisted selective autophagy. Together, our analysis reveals that in an Alzheimer’s brain, with exception of Hsp90, the players of the protein quality control are still present in full strength, even in brain regions most severely affected in disease. The specific upregulation of small heat shock proteins and HSP70:BAG3, ubiquitous in all brain areas analyzed, may represent a last, unsuccessful attempt to advert cell death.

Heat Shock Proteins, a Key Modulator of Neuroinflammation in Alzheimer’s Disease

2020 ◽  
Author(s):  
Komal Panchal ◽  
Vidhi Bhatt ◽  
Mahima Raval ◽  
Anand Krishna Tiwari
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

Expression of heat shock proteins in Alzheimer's disease

Neurology ◽  
1991 ◽  
Vol 41 (3) ◽  
pp. 345-345 ◽  
Author(s):  
J. E. Hamos ◽  
B. Oblas ◽  
D. Pulaski-Salo ◽  
W. J. Welch ◽  
D. G. Bole ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains

2006 ◽  
Vol 32 (2) ◽  
pp. 119-130 ◽  
Author(s):  
M. M. M. Wilhelmus ◽  
I. Otte-Holler ◽  
P. Wesseling ◽  
R. M. W. de Waal ◽  
W. C. Boelens ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Specific Association ◽  
Shock Proteins
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