Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis

Research output: Contribution to journalReview articleResearchpeer-review

Abstract

Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterised by the progressive loss of motor neurons, leading to paralysis and death within several years of onset. Although protein misfolding is a key feature of ALS, the upstream triggers of disease remain elusive. Recently, endoplasmic reticulum (ER) stress was identified as an early and central feature in ALS diseasemodels as well as in human patient tissues, indicating that ER stress could be an important process in disease pathogenesis. One important chaperone induced by ER stress is protein disulphide isomerase (PDI), which is both upregulated and posttranslationally inhibited by S-nitrosylation in ALS. In this paper, we present evidence from studies of genetics, model organisms, and patient tissues which indicate an active role for PDI and ER stress in ALS disease processes.

LanguageEnglish
Article number317340
Pages1-7
Number of pages7
JournalNeurology Research International
Volume2011
DOIs
Publication statusPublished - Feb 2011
Externally publishedYes

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Protein Disulfide-Isomerases
Amyotrophic Lateral Sclerosis
Endoplasmic Reticulum Stress
Genetic Models
Motor Neurons
Heat-Shock Proteins
Paralysis
Neurodegenerative Diseases
Neuroprotection
Proteins

Cite this

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title = "Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis",
abstract = "Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterised by the progressive loss of motor neurons, leading to paralysis and death within several years of onset. Although protein misfolding is a key feature of ALS, the upstream triggers of disease remain elusive. Recently, endoplasmic reticulum (ER) stress was identified as an early and central feature in ALS diseasemodels as well as in human patient tissues, indicating that ER stress could be an important process in disease pathogenesis. One important chaperone induced by ER stress is protein disulphide isomerase (PDI), which is both upregulated and posttranslationally inhibited by S-nitrosylation in ALS. In this paper, we present evidence from studies of genetics, model organisms, and patient tissues which indicate an active role for PDI and ER stress in ALS disease processes.",
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Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis. / Walker, Adam K.; Atkin, Julie D.

In: Neurology Research International, Vol. 2011, 317340, 02.2011, p. 1-7.

Research output: Contribution to journalReview articleResearchpeer-review

TY - JOUR

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AB - Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterised by the progressive loss of motor neurons, leading to paralysis and death within several years of onset. Although protein misfolding is a key feature of ALS, the upstream triggers of disease remain elusive. Recently, endoplasmic reticulum (ER) stress was identified as an early and central feature in ALS diseasemodels as well as in human patient tissues, indicating that ER stress could be an important process in disease pathogenesis. One important chaperone induced by ER stress is protein disulphide isomerase (PDI), which is both upregulated and posttranslationally inhibited by S-nitrosylation in ALS. In this paper, we present evidence from studies of genetics, model organisms, and patient tissues which indicate an active role for PDI and ER stress in ALS disease processes.

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