scholarly journals Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease

2019 ◽  
Vol 10 ◽  
Author(s):  
Jack M. Webster ◽  
April L. Darling ◽  
Vladimir N. Uversky ◽  
Laura J. Blair
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Aggregation ◽  
Neurodegenerative Disease ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Small heat shock proteins, protein degradation and protein aggregation diseases

Autophagy ◽  
2011 ◽  
Vol 7 (1) ◽  
pp. 101-103 ◽  
Author(s):  
Michel J. Vos ◽  
Marianne P. Zijlstra ◽  
Serena Carra ◽  
Ody C.M. Sibon ◽  
Harm H. Kampinga
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Aggregation ◽  
Protein Degradation ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal-like cells

2020 ◽  
Author(s):  
R. San Gil ◽  
D. Cox ◽  
L. McAlary ◽  
T. Berg ◽  
A. K. Walker ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Diseases ◽  
Protein Aggregation ◽  
Neurodegenerative Disease ◽  
Heat Shock Response ◽  
Flow Cytometric Analysis ◽  
Protein Aggregates ◽  
Shock Response ◽  
Shock Proteins

AbstractProtein aggregation that results in the formation of inclusions is strongly correlated with neuronal death and is a pathological hallmark common to many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Huntington’s disease. Cells are thought to dramatically up-regulate the levels of heat shock proteins during periods of cellular stress via induction of the heat shock response (HSR). Heat shock proteins are well-characterised molecular chaperones that interact with aggregation-prone proteins to either stabilise, refold, or traffic protein for degradation. The reason why heat shock proteins are unable to maintain the solubility of particular proteins in neurodegenerative disease is unknown. We sought to determine whether neurodegenerative disease-associated protein aggregates can induce the HSR. Here, we generated a neuroblastoma cell line that expresses a fluorescent reporter under conditions of HSR induction, for example heat shock. Using these cells, we show that the HSR is not induced by exogenous treatment with aggregated forms of Parkinson’s disease-associated α-synuclein or the ALS-associated G93A mutant of superoxide dismutase-1 (SOD1G93A). Furthermore, flow cytometric analysis revealed that intracellular expression of SOD1G93A or a pathogenic form of polyQ-expanded huntingtin (Htt72Q), similarly, results in no or low induction of the HSR. In contrast, expression of a non-pathogenic but aggregation-prone form of firefly luciferase (Fluc) did induce an HSR in a significantly greater proportion of cells. Finally, we show that HSR induction is dependent on the intracellular levels of the aggregation-prone proteins, but the pathogenic proteins (SOD1G93A and Htt72Q) elicit a significantly lower HSR compared to the non-pathogenic proteins (Fluc). These results suggest that pathogenic proteins either evade detection or impair induction of the HSR in neuronal-like cells. Therefore, defective HSR induction may facilitate the initiation of protein aggregation leading to inclusion formation in neurodegenerative diseases.

scholarly journals Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

2003 ◽  
Vol 50 (2) ◽  
pp. 585-595 ◽  
Author(s):  
Axel Mogk ◽  
Elke Deuerling ◽  
Sonja Vorderwülbecke ◽  
Elizabeth Vierling ◽  
Bernd Bukau
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Aggregation ◽  
Small Heat Shock Proteins ◽  
System Form ◽  
Shock Proteins

scholarly journals O-GlcNAcylation of small heat shock proteins enhances their anti-amyloid chaperone activity

2019 ◽  
Author(s):  
Aaron T. Balana ◽  
Paul M. Levine ◽  
Somnath Mukherjee ◽  
Nichole J. Pedowitz ◽  
Stuart P. Moon ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Diseases ◽  
Protein Aggregation ◽  
Posttranslational Modification ◽  
Small Heat Shock Proteins ◽  
Amyloid Formation ◽  
Protein Chemistry ◽  
Synthetic Protein ◽  
Shock Proteins

AbstractA major role for the intracellular posttranslational modification O-GlcNAc appears to be the inhibition of protein aggregation. Most of the previous studies in this area have focused on O-GlcNAcylation of the amyloid-forming proteins themselves. Here, we use synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically. More specifically, we find that O-GlcNAcylation increases the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ. Mechanistically, we show that O-GlcNAc near the sHSP IXI-domain prevents its ability to intramolecularly compete with substrate binding. Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.

Small heat shock proteins inhibit amyloid-β protein aggregation and cerebrovascular amyloid-β protein toxicity

2006 ◽  
Vol 1089 (1) ◽  
pp. 67-78 ◽  
Author(s):  
Micha M.M. Wilhelmus ◽  
Wilbert C. Boelens ◽  
Irene Otte-Höller ◽  
Bram Kamps ◽  
Robert M.W. de Waal ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Aggregation ◽  
Amyloid Β ◽  
Small Heat Shock Proteins ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Shock Proteins ◽  
Protein Toxicity ◽  
Cerebrovascular Amyloid

P1-178 Small heat shock proteins affect amyloid-β protein aggregation and inhibit cerebrovascular amyloid-β protein toxicity

2004 ◽  
Vol 25 ◽  
pp. S146
Author(s):  
Micha M.M. Wilhelmus ◽  
Wilbert C. Boelens ◽  
Irene Otte-Höller ◽  
Bram Kamps ◽  
Frank de Lange ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Aggregation ◽  
Amyloid Β ◽  
Small Heat Shock Proteins ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Shock Proteins ◽  
Protein Toxicity ◽  
Cerebrovascular Amyloid

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

The Small Heat-shock Proteins IbpA and IbpB in E. coli: The Small Ones With a Big Role

2016 ◽  
Vol 9 (2) ◽  
pp. 84-96
Author(s):  
Sanchari Bhattacharjee ◽  
Rakhi Dasgupta ◽  
Angshuman Bagchi
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Shock Proteins
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