Endoplasmic reticulum dysfunction in neurological disease

Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin...

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Bibliographic Details
Published in:Lancet neurology Vol. 12; no. 1; pp. 105 - 118
Main Authors: Roussel, Benoit D, Kruppa, Antonina J, Miranda, Elena, Crowther, Damian C, Lomas, David A, Marciniak, Stefan J
Format: Journal Article
Language:English
Published: England Elsevier Ltd 01.01.2013
Elsevier Limited
Elsevier
Subjects:
Alzheimer's disease
Amyloid beta-Peptides
Amyloid beta-Peptides - genetics
Amyotrophic lateral sclerosis
Animals
Ataxia
beta -Amyloid
Cellular Biology
Cognitive ability
Disease
Endoplasmic Reticulum
Endoplasmic Reticulum - pathology
Endoplasmic Reticulum - physiology
Enzymes
Epilepsy
Humans
Inclusion bodies
Ischemia
Life Sciences
Movement disorders
Multiple sclerosis
Mutation
Nervous System Diseases
Nervous System Diseases - genetics
Nervous System Diseases - pathology
Nervous System Diseases - physiopathology
Neurodegenerative diseases
Neurological diseases
Neurology
neuroserpin
Prion protein
Protein Folding
Reperfusion
Signal Transduction
Signal Transduction - physiology
Sleep
Sleep disorders
Stress
Stroke
Unfolded Protein Response
Unfolded Protein Response - genetics
ISSN:1474-4422, 1474-4465, 1474-4465
Online Access:Get full text
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Summary:Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible.
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ISSN:1474-4422
1474-4465
1474-4465
DOI:10.1016/S1474-4422(12)70238-7