scholarly journals Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis

2013 ◽  
Vol 129 (1) ◽  
pp. 190-204 ◽  
Author(s):  
Julie D. Atkin ◽  
Manal A. Farg ◽  
Kai Ying Soo ◽  
Adam K. Walker ◽  
Mark Halloran ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Mutant Sod1 ◽  
Golgi Transport ◽  
Lateral Sclerosis

Unraveling the Complexity of Amyotrophic Lateral Sclerosis: Recent Advances from the Transgenic Mutant SOD1 Mice

2010 ◽  
Vol 9 (4) ◽  
pp. 491-503 ◽  
Author(s):  
M. Peviani ◽  
I. Caron ◽  
C. Pizzasegola ◽  
F. Gensano ◽  
M. Tortarolo ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Mutant Sod1 ◽  
Recent Advances ◽  
Lateral Sclerosis

Differential effect of oxidative or excitotoxic stress on the transcriptional profile of amyotrophic lateral sclerosis-linked mutant SOD1 cultured neurons

2011 ◽  
Vol 89 (9) ◽  
pp. 1439-1450 ◽  
Author(s):  
Nadia Boutahar ◽  
Anne Wierinckx ◽  
Jean Philippe Camdessanche ◽  
Jean-Christophe Antoine ◽  
Evelyne Reynaud ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Differential Effect ◽  
Transcriptional Profile ◽  
Cultured Neurons ◽  
Mutant Sod1 ◽  
Lateral Sclerosis

scholarly journals Lack of TNF-alpha receptor type 2 protects motor neurons in a cellular model of amyotrophic lateral sclerosis and in mutant SOD1 mice but does not affect disease progression

2015 ◽  
Vol 135 (1) ◽  
pp. 109-124 ◽  
Author(s):  
Massimo Tortarolo ◽  
Antonio Vallarola ◽  
Dario Lidonnici ◽  
Elisa Battaglia ◽  
Francesco Gensano ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Disease Progression ◽  
Motor Neurons ◽  
Receptor Type ◽  
Tnf Alpha ◽  
Cellular Model ◽  
Mutant Sod1 ◽  
Lateral Sclerosis

scholarly journals Endogenous Cu in the central nervous system fails to satiate the elevated requirement for Cu in a mutant SOD1 mouse model of ALS

Metallomics ◽  
2016 ◽  
Vol 8 (9) ◽  
pp. 1002-1011 ◽  
Author(s):  
J. B. Hilton ◽  
A. R. White ◽  
P. J. Crouch
Keyword(s):  
Central Nervous System ◽  
Amyotrophic Lateral Sclerosis ◽  
Nervous System ◽  
Mouse Model ◽  
Limited Capacity ◽  
Mutant Sod1 ◽  
The Central Nervous System ◽  
Sod1 Mouse ◽  
Lateral Sclerosis

It is unclear why ubiquitous expression of mutant SOD1 selectively affects the central nervous system in amyotrophic lateral sclerosis. Here we hypothesise that the central nervous system is primarily affected because, unlike other tissues, it has relatively limited capacity to satiate an increased requirement for Cu.

scholarly journals Fully Metallated S134N Cu,Zn-Superoxide Dismutase Displays Abnormal Mobility and Intermolecular Contacts in Solution

2005 ◽  
Vol 280 (43) ◽  
pp. 35815-35821 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Nicola D'Amelio ◽  
Elena Gaggelli ◽  
Elisa Libralesso ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Superoxide Dismutase ◽  
Familial Amyotrophic Lateral Sclerosis ◽  
Wild Type ◽  
Mutant Sod1 ◽  
Copper Zinc Superoxide Dismutase ◽  
Intermolecular Contacts ◽  
Nmr Methods ◽  
The Individual ◽  
Lateral Sclerosis

S134N copper-zinc superoxide dismutase (SOD1) is one of the many mutant SOD1 proteins known to cause familial amyotrophic lateral sclerosis. Earlier studies demonstrated that partially metal-deficient S134N SOD1 crystallized in filament-like arrays with abnormal contacts between the individual protein molecules. Because protein aggregation is implicated in SOD1-linked familial amyotrophic lateral sclerosis, abnormal intermolecular interactions between mutant SOD1 proteins could be relevant to the mechanism of pathogenesis in the disease. We have therefore applied NMR methods to ascertain whether abnormal contacts also form between S134N SOD1 molecules in solution and whether Cys-6 or Cys-111 plays any role in the aggregation. Our studies demonstrate that the behavior of fully metallated S134N SOD1 is dramatically different from that of fully metallated wild type SOD1 with a region of subnanosecond mobility located close to the site of the mutation. Such a high degree of mobility is usually seen only in the apo form of wild type SOD1, because binding of zinc to the zinc site normally immobilizes that region. In addition, concentration-dependent chemical shift differences were observed for S134N SOD1 that were not observed for wild type SOD1, indicative of abnormal intermolecular contacts in solution. We have here also established that the two free cysteines (6 and 111) do not play a role in this behavior.

scholarly journals Gonadectomy and dehydroepiandrosterone (DHEA) do not modulate disease progression in the G93A mutant SOD1 rat model of amyotrophic lateral sclerosis

2012 ◽  
Vol 13 (3) ◽  
pp. 311-314 ◽  
Author(s):  
Antonio Hayes-Punzo ◽  
Patrick Mulcrone ◽  
Michael Meyer ◽  
Jacalyn Mchugh ◽  
Clive N. Svendsen ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Disease Progression ◽  
Rat Model ◽  
Mutant Sod1 ◽  
Lateral Sclerosis

scholarly journals Insoluble Mutant SOD1 Is Partly Oligoubiquitinated in Amyotrophic Lateral Sclerosis Mice

2006 ◽  
Vol 281 (44) ◽  
pp. 33325-33335 ◽  
Author(s):  
Manuela Basso ◽  
Tania Massignan ◽  
Giuseppina Samengo ◽  
Cristina Cheroni ◽  
Silvia De Biasi ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Mutant Sod1 ◽  
Lateral Sclerosis
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