Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation

2021 ◽  
Author(s):  
Joana S. Cristóvão ◽  
Guilherme G. Moreira ◽  
Filipe E. P. Rodrigues ◽  
Ana P. Carapeto ◽  
Mário S. Rodrigues ◽  
...  

A mechanism of chemical regulation of the S100B chaperone via Cu2+ induced assembly of S100B cross-linked oligomers with enhanced anti-amyloid aggregation activity.

2020 ◽  
Vol 9 (6) ◽  
pp. 1713 ◽  
Author(s):  
Gabriela Dumitrita Stanciu ◽  
Veronica Bild ◽  
Daniela Carmen Ababei ◽  
Razvan Nicolae Rusu ◽  
Alina Cobzaru ◽  
...  

Diabetes and Alzheimer’s disease are two highly prevalent diseases among the aging population and have become major public health concerns in the 21st century, with a significant risk to each other. Both of these diseases are increasingly recognized to be multifactorial conditions. The terms “diabetes type 3” or “brain diabetes” have been proposed in recent years to provide a complete view of the potential common pathogenic mechanisms between these diseases. While insulin resistance or deficiency remains the salient hallmarks of diabetes, cognitive decline and non-cognitive abnormalities such as impairments in visuospatial function, attention, cognitive flexibility, and psychomotor speed are also present. Furthermore, amyloid aggregation and deposition may also be drivers for diabetes pathology. Here, we offer a brief appraisal of social impact and economic burden of these chronic diseases and provide insight into amyloidogenesis through considering recent advances of amyloid-β aggregates on diabetes pathology and islet amyloid polypeptide on Alzheimer’s disease. Exploring the detailed knowledge of molecular interaction between these two amyloidogenic proteins opens new opportunities for therapies and biomarker development.


Author(s):  
Tahmina Akter ◽  
Hitoshi Nakamoto

Abstract In contrast to Escherichia coli, cyanobacteria have multiple GroELs, the bacterial homologues of chaperonin/Hsp60. We have shown that cyanobacterial GroELs are mutually distinct and different from E. coli GroEL with which the paradigm for chaperonin structure/function has been established. However, little is known about regulation of cyanobacterial GroELs. This study investigated effect of pH (varied from 7.0 to 8.5) on chaperone activity of GroEL1 and GroEL2 from the cyanobacterium Synechococcus elongatus PCC7942 and E. coli GroEL. GroEL1 and GroEL2 showed pH dependency in suppression of aggregation of heat-denatured malate dehydrogenase, lactate dehydrogenase and citrate synthase. They exhibited higher anti-aggregation activity at more alkaline pHs. Escherichia coli GroEL showed a similar pH-dependence in suppressing aggregation of heat-denatured lactate dehydrogenase. No pH dependence was observed in all the GroELs when urea-denatured lactate dehydrogenase was used for anti-aggregation assay, suggesting that the pH-dependence is related to some denatured structures. There was no significant influence of pH on the chaperone activity of all the GroELs to promote refolding of heat-denatured malate dehydrogenase. It is known that pH in cyanobacterial cytoplasm increases by one pH unit following a shift from darkness to light, suggesting that the pH-change modulates chaperone activity of cyanobacterial GroEL1 and GroEL2.


2011 ◽  
Vol 119 (1) ◽  
pp. 220-230 ◽  
Author(s):  
Peter J. Crouch ◽  
Maria S. Savva ◽  
Lin W. Hung ◽  
Paul S. Donnelly ◽  
Alexandra I. Mot ◽  
...  

2018 ◽  
Vol 54 (16) ◽  
pp. 2000-2003 ◽  
Author(s):  
Jian Wang ◽  
Tomoya Yamamoto ◽  
Jia Bai ◽  
Sarah J. Cox ◽  
Kyle J. Korshavn ◽  
...  

Magic-angle-spinning NMR for monitoring amyloid aggregation reveals that mechanical rotation of Aβ1–40 monomers increases the rate of aggregation.


2018 ◽  
Vol 76 ◽  
pp. 228-236 ◽  
Author(s):  
Zhenhua Wu ◽  
Wenxia Liao ◽  
Kelin Chen ◽  
Jingfang Qin ◽  
Huang Tang

2017 ◽  
Vol 13 (8) ◽  
pp. 1545-1551 ◽  
Author(s):  
Elaheh Jamasbi ◽  
Frances Separovic ◽  
Mohammed Akhter Hossain ◽  
Giuseppe Donato Ciccotosto

Phosphorylation of Aβ42 promotes the formation of amyloid plaques in the brain, which lack the neurotoxic properties associated with oligomeric species causing pathogenesis in Alzheimer's disease.


2017 ◽  
Vol 8 (2) ◽  
pp. 1295-1302 ◽  
Author(s):  
S. Pellegrino ◽  
N. Tonali ◽  
E. Erba ◽  
J. Kaffy ◽  
M. Taverna ◽  
...  

Acyclic β-hairpins designed on oligomeric and fibril structures of Aβ1–42 disrupt protein–protein interactions mediating amyloid β-peptide aggregation.


2018 ◽  
Vol 34 (4) ◽  
pp. 456-463 ◽  
Author(s):  
Yu-Xi Wang ◽  
Bin Lin ◽  
Le Zhou ◽  
Zhi-Yang Yan ◽  
Han Zhang ◽  
...  

Biochemistry ◽  
2014 ◽  
Vol 53 (40) ◽  
pp. 6323-6331 ◽  
Author(s):  
Kanchan Garai ◽  
Philip B. Verghese ◽  
Berevan Baban ◽  
David M. Holtzman ◽  
Carl Frieden

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