Cited by 448Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchGenetic Neurodegenerative Diseases

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Endoplasmic reticulum dysfunction in neurological disease

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Roussel, Benoit D, Kruppa, Antonina J, Miranda, Elena, Crowther, Damian C, Lomas, David A, Marciniak, Stefan J·2013·The Lancet Neurology

DOI 10.1016/s1474-4422(12)70238-7

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Abstract

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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Harding, 2003, An integrated stress response regulates amino acid metabolism and resistance to oxidative stress, Mol Cell, 11, 619, 10.1016/S1097-2765(03)00105-9 · DOI

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Authors: Roussel, B. D., Kruppa, A. J., Miranda, E., Crowther, D. C., Lomas, D. A., & Marciniak, S. J.
Affiliations: Inserm (FR)
University of Cambridge (GB)
Istituto Pasteur (IT)
Corresponding author: Marciniak, Stefan J
ORCID: Roussel, Benoit D
Kruppa, Antonina J
Miranda, Elena
Crowther, Damian C
Lomas, David A
Marciniak, Stefan J
Venue: The Lancet Neurology
Publisher: Elsevier BV
Published: 2013-01
Volume: 12
Issue: 1
Pages: 105-118
ISSN: 1474-4422 (ISSN-L)
DOI: 10.1016/s1474-4422(12)70238-7
OpenAlex: W2051661723
Cited by: 441
References: 137
Citations by year: 2026: 9 · 2025: 16 · 2024: 25 · 2023: 19 · 2022: 28 · 2021: 25 · 2020: 31 · 2019: 35 · 2018: 32 · 2017: 34 · 2016: 54 · 2015: 41 · 2014: 54 · 2013: 38
FWCI: 3.92
Type: journal article
Language: en
Open access: green
inserm.hal.science
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: The Lancet Neurology (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, cc-by)
HAL (submittedVersion)
UCL Discovery (University College London) (submittedVersion)
IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
Apollo
Funders: Wellcome Trust (G1002610, 089703/Z/09/Z, 100140, 089703, 100140/Z/12/Z)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: endoplasmic reticulum dysfunction, endoplasmic reticulum stress, unfolded protein response, neurodegenerative diseases, cerebral ischemia, stroke, sleep apnea, Alzheimer's disease, amyloid-beta, neuroserpin, multiple sclerosis, amyotrophic lateral sclerosis, prion disease, Parkinson's disease, Huntington's disease, protein misfolding
MeSH terms: Animals, Endoplasmic Reticulum, Humans, Nervous System Diseases, Signal Transduction, Amyloid beta-Peptides, Protein Folding, Unfolded Protein Response

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