Rhizolutin, a Novel 7/10/6‐Tricyclic Dilactone, Dissociates Misfolded Protein Aggregates and Reduces Apoptosis/Inflammation Associated with Alzheimer's Disease

2020 ◽  
Vol 132 (51) ◽  
pp. 23194-23198
Author(s):  
Yun Kwon ◽  
Jisu Shin ◽  
Kwangho Nam ◽  
Joon Soo An ◽  
Seung‐Hoon Yang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregates ◽  
Misfolded Protein

Fundamentals of cross-seeding of amyloid proteins: an introduction

2019 ◽  
Vol 7 (46) ◽  
pp. 7267-7282 ◽  
Author(s):  
Baiping Ren ◽  
Yanxian Zhang ◽  
Mingzhen Zhang ◽  
Yonglan Liu ◽  
Dong Zhang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Type 2 Diabetes ◽  
Alzheimer's Disease ◽  
Protein Misfolding ◽  
Protein Aggregates ◽  
Misfolded Protein ◽  
Amyloid Proteins ◽  
Misfolding Diseases

Misfolded protein aggregates formed by the same (homologous) or different (heterologous/cross) sequences are the pathological hallmarks of many protein misfolding diseases (PMDs) including Alzheimer's disease (AD) and type 2 diabetes (T2D).

scholarly journals Imaging Alzheimer's disease-related protein aggregates in human cells using a selenium label

2010 ◽  
Vol 241 ◽  
pp. 012020 ◽  
Author(s):  
E K McGuire ◽  
M Motskin ◽  
T P J Knowles ◽  
C M Dobson ◽  
D W McComb ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregates ◽  
Human Cells ◽  
Related Protein

scholarly journals Loss of function of the mitochondrial peptidase PITRM1 induces proteotoxic stress and Alzheimer’s disease-like pathology in human cerebral organoids

2020 ◽  
Author(s):  
Dina Ivanyuk ◽  
María José Pérez ◽  
Vasiliki Panagiotakopoulou ◽  
Gabriele Di Napoli ◽  
Dario Brunetti ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Death ◽  
Cortical Neurons ◽  
Amyloid Β ◽  
Neuronal Cell ◽  
Protein Aggregates ◽  
Neuronal Cultures ◽  
Loss Of Function ◽  
Proteotoxic Stress

AbstractMutations in pitrilysin metallopeptidase 1 (PITRM1), a mitochondrial protease involved in mitochondrial precursor processing and degradation, result in a slow-progressive syndrome, characterized by cerebellar ataxia, psychotic episodes and obsessive behavior as well as cognitive decline. To investigate the pathogenetic mechanisms of mitochondrial presequence processing, we employed cortical neurons and cerebral organoids generated from PITRM1 knockout human induced pluripotent stem cells (iPSCs). PITRM1 deficiency strongly induced mitochondrial unfolded protein response (UPRmt) and enhanced mitochondrial clearance in iPSC-derived neurons. Furthermore, we observed increased levels of amyloid precursor protein and amyloid β in PITRM1 knockout neurons. However, neither cell death nor protein aggregates were observed in 2D iPSC-derived cortical neuronal cultures. On the contrary, cerebral organoids generated from PITRM1 knockout iPSCs spontaneously developed over time pathological features of Alzheimer’s disease (AD), including accumulation of protein aggregates, tau pathology, and neuronal cell death. Importantly, we provide evidence for a protective role of UPRmt and mitochondrial clearance against impaired mitochondrial presequence processing and proteotoxic stress. In summary, we propose a novel concept of PITRM1-linked neurological syndrome whereby defects of mitochondrial presequence processing induce an early activation of UPRmt that, in turn, modulates cytosolic quality control pathways. Thus our work supports a mechanistic link between mitochondrial function and common neurodegenerative proteinopathies.

P3-196: Detection of Abeta oligomers in Alzheimer's disease patient CSF with a novel misfolded protein assay

2010 ◽  
Vol 6 ◽  
pp. S508-S508
Author(s):  
Carol Man Gao ◽  
Joseph P Fedynyshyn ◽  
Erika Magdangal ◽  
Alice Yam ◽  
Kaj Blennow ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Disease Patient ◽  
Misfolded Protein ◽  
Protein Assay

Antibody 9D5 Recognizes Oligomeric Pyroglutamate Amyloid-β in a Fraction of Amyloid-β Deposits in Alzheimer's Disease without Cross-Reactivity with other Protein Aggregates

2012 ◽  
Vol 29 (2) ◽  
pp. 361-371 ◽  
Author(s):  
Vivek Venkataramani ◽  
Oliver Wirths ◽  
Herbert Budka ◽  
Wolfgang Härtig ◽  
Gabor G. Kovacs ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Protein Aggregates ◽  
Cross Reactivity

Transmission of pathogenic protein aggregates in Alzheimer’s disease

2017 ◽  
Vol 51 (3) ◽  
pp. 368-371 ◽  
Author(s):  
A. L. Schwarzman ◽  
S. V. Sarantseva
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregates
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