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

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

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 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.

scholarly journals Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β

FEBS Letters ◽  
2004 ◽  
Vol 576 (1-2) ◽  
pp. 57-62 ◽  
Author(s):  
Sandor Boros ◽  
Bram Kamps ◽  
Lisa Wunderink ◽  
Willem de Bruijn ◽  
Wilfried W. de Jong ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Amyloid Β ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

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
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