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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Vydané v:	Lancet neurology Ročník 12; číslo 1; s. 105 - 118
Hlavní autori:	Roussel, Benoit D, Kruppa, Antonina J, Miranda, Elena, Crowther, Damian C, Lomas, David A, Marciniak, Stefan J
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England Elsevier Ltd 01.01.2013 Elsevier Limited Elsevier
Predmet:	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
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Popis
Shrnutí:	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.
Bibliografia:	SourceType-Scholarly Journals-1 content type line 14 ObjectType-Feature-4 ObjectType-Undefined-1 ObjectType-Review-2 ObjectType-Article-3 ObjectType-Article-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 ObjectType-Article-2 ObjectType-Feature-1
ISSN:	1474-4422 1474-4465 1474-4465
DOI:	10.1016/S1474-4422(12)70238-7