Necroptotic neuronal cell death in amyotrophic lateral sclerosis: A relevant hypothesis with potential therapeutic implication?

2020 ◽  
Vol 144 ◽  
pp. 110295
Author(s):  
Mathilde Chevin ◽  
Guillaume Sébire ◽  
Paul Deltenre ◽  
Hazim Kadhim
Keyword(s):  
Cell Death ◽  
Amyotrophic Lateral Sclerosis ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Therapeutic Implication ◽  
Lateral Sclerosis

Celastrol Blocks Neuronal Cell Death and Extends Life in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis

2005 ◽  
Vol 2 (5) ◽  
pp. 246-254 ◽  
Author(s):  
Mahmoud Kiaei ◽  
Khatuna Kipiani ◽  
Susanne Petri ◽  
Junyu Chen ◽  
Noel Y. Calingasan ◽  
...  
Keyword(s):  
Cell Death ◽  
Amyotrophic Lateral Sclerosis ◽  
Mouse Model ◽  
Transgenic Mouse ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Transgenic Mouse Model ◽  
Lateral Sclerosis

N-acetyl-l -tryptophan, but not N-acetyl-d -tryptophan, rescues neuronal cell death in models of amyotrophic lateral sclerosis

2015 ◽  
Vol 134 (5) ◽  
pp. 956-968 ◽  
Author(s):  
Ana C. Sirianni ◽  
Jiying Jiang ◽  
Jiang Zeng ◽  
Lilly L. Mao ◽  
Shuanhu Zhou ◽  
...  
Keyword(s):  
Cell Death ◽  
Amyotrophic Lateral Sclerosis ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Lateral Sclerosis

scholarly journals Structural properties and neuronal toxicity of amyotrophic lateral sclerosis–associated Cu/Zn superoxide dismutase 1 aggregates

2005 ◽  
Vol 171 (1) ◽  
pp. 75-85 ◽  
Author(s):  
Gen Matsumoto ◽  
Aleksandar Stojanovic ◽  
Carina I. Holmberg ◽  
Soojin Kim ◽  
Richard I. Morimoto
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Superoxide Dismutase ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Dependent Manner ◽  
Superoxide Dismutase 1 ◽  
Aggregate Structure ◽  
Mutant Sod1 ◽  
Aggregate Structures ◽  
Lateral Sclerosis

The appearance of protein aggregates is a characteristic of protein misfolding disorders including familial amyotrophic lateral sclerosis, a neurodegenerative disease caused by inherited mutations in Cu/Zn superoxide dismutase 1 (SOD1). Here, we use live cell imaging of neuronal and nonneuronal cells to show that SOD1 mutants (G85R and G93A) form an aggregate structure consisting of immobile scaffolds, through which noninteracting cellular proteins can diffuse. Hsp70 transiently interacts, in a chaperone activity-dependent manner, with these mutant SOD1 aggregate structures. In contrast, the proteasome is sequestered within the aggregate structure, an event associated with decreased degradation of a proteasomal substrate. Through the use of time-lapse microscopy of individual cells, we show that nearly all (90%) aggregate-containing cells express higher levels of mutant SOD1 and died within 48 h, whereas 70% of cells expressing a soluble mutant SOD1 survived. Our results demonstrate that SOD1 G85R and G93A mutants form a distinct class of aggregate structures in cells destined for neuronal cell death.

scholarly journals Brief Review of the Role of Glycogen Synthase Kinase-3β in Amyotrophic Lateral Sclerosis

2011 ◽  
Vol 2011 ◽  
pp. 1-5 ◽  
Author(s):  
Seong-Ho Koh ◽  
Wonki Baek ◽  
Seung H. Kim
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Therapeutic Strategy ◽  
Glycogen Synthase ◽  
Neuronal Cell Death ◽  
Neuronal Cell ◽  
Glycogen Synthase Kinase ◽  
Diverse Range ◽  
Symptom Progression ◽  
Lateral Sclerosis

Glycogen synthase kinase-3β(GSK-3β) is known to affect a diverse range of biological functions controlling gene expression, cellular architecture, and apoptosis. GSK-3βhas recently been identified as one of the important pathogenic mechanisms in motor neuronal death related to amyotrophic lateral sclerosis (ALS). Therefore, the development of methods to control GSK-3βcould be helpful in postponing the symptom progression of ALS. Here we discuss the known roles of GSK-3βin motor neuronal cell death in ALS and the possibility of employing GSK-3βmodulators as a new therapeutic strategy.

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