scholarly journals Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer’s disease

2013 ◽  
Vol 5 (6) ◽  
pp. 61 ◽  
Author(s):  
Nathalie Jurisch-Yaksi ◽  
Wim Annaert
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Quality Control ◽  
Secretory Pathway ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Early Secretory Pathway

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.

scholarly journals Roles and Mechanisms of the Protein Quality Control System in Alzheimer’s Disease

2021 ◽  
Vol 23 (1) ◽  
pp. 345
Author(s):  
Yaping Liu ◽  
Runrong Ding ◽  
Ze Xu ◽  
Yuan Xue ◽  
Dongdong Zhang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Quality Control ◽  
Control System ◽  
Protein Quality ◽  
Early Stage ◽  
Senile Plaques ◽  
Protein Quality Control ◽  
Quality Control System ◽  
Protein Quality Control System

Alzheimer’s disease (AD) is characterized by the deposition of senile plaques (SPs) and the formation of neurofibrillary tangles (NTFs), as well as neuronal dysfunctions in the brain, but in fact, patients have shown a sustained disease progression for at least 10 to 15 years before these pathologic biomarkers can be detected. Consequently, as the most common chronic neurological disease in the elderly, the challenge of AD treatment is that it is short of effective biomarkers for early diagnosis. The protein quality control system is a collection of cellular pathways that can recognize damaged proteins and thereby modulate their turnover. Abundant evidence indicates that the accumulation of abnormal proteins in AD is closely related to the dysfunction of the protein quality control system. In particular, it is the synthesis, degradation, and removal of essential biological components that have already changed in the early stage of AD, which further encourages us to pay more attention to the protein quality control system. The review mainly focuses on the endoplasmic reticulum system (ERS), autophagy–lysosome system (ALS) and the ubiquitin–proteasome system (UPS), and deeply discusses the relationship between the protein quality control system and the abnormal proteins of AD, which can not only help us to understand how and why the complex regulatory system becomes malfunctional during AD progression, but also provide more novel therapeutic strategies to prevent the development of AD.

scholarly journals Protein quality control in the early secretory pathway

2008 ◽  
Vol 27 (2) ◽  
pp. 315-327 ◽  
Author(s):  
Tiziana Anelli ◽  
Roberto Sitia
Keyword(s):  
Quality Control ◽  
Secretory Pathway ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Early Secretory Pathway

scholarly journals Zinc regulates ERp44-dependent protein quality control in the early secretory pathway

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Satoshi Watanabe ◽  
Yuta Amagai ◽  
Sara Sannino ◽  
Tiziana Tempio ◽  
Tiziana Anelli ◽  
...  
Keyword(s):  
Quality Control ◽  
Secretory Pathway ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Early Secretory Pathway ◽  
Dependent Protein

scholarly journals Alzheimer cells on their way to derailment show selective changes in protein quality control network

2020 ◽  
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 characterised 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 Proteasome database, which provides a quantitative assessment of disease-related proteome changes in six brain regions in comparison with age-matched controls. We noted that levels of all paralogues 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, channelling 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 analysed, may represent a last, unsuccessful attempt to advert neuronal cell death.

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