Cited by 358Amyotrophic Lateral Sclerosis ResearchEndoplasmic Reticulum Stress and DiseaseGenetic Neurodegenerative Diseases

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Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis

Ilieva, E. V., Ayala, V., Jove, M., Dalfo, E., Cacabelos, D., Povedano, M., Bellmunt, M. J., Ferrer, I., Pamplona, R., Portero-Otin, M.·2007·Brain

DOI 10.1093/brain/awm190

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Abstract

The occurrence of endoplasmic reticulum (ER) stress in the sporadic form of amyotrophic lateral sclerosis (ALS) is unknown, despite it has been recently documented in experimental models of the familial form. Here we show that spinal cord from patients with sporadic ALS showed signs of ER stress, such as increased levels of ER chaperones such as protein-disulfide isomerase, and increased phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha). Among the potential causes of such ER stress proteasomal impairment was confirmed in the same samples by demonstrating increased ubiquitin immunoreactivity and increased protein lipoxidative (125%), glycoxidative (55%) and direct oxidative damage (62%) over control values, as evidenced by mass-spectrometry and immunological methods. We found that protein oxidative damage was strongly associated to ALS-specific changes in fatty acid concentrations, specifically of n-3 series (as docosahexaenoic acid), and in the amount of mitochondrial components as respiratory complexes I and III, suggesting a mitochondrial dysfunction leading to increased free radical production. Oxidative stress was also evidenced in frontal cortex, suggesting that this region is affected early in ALS. As those events were partially reproduced by threohydroxyaspartate exposure in organotypic spinal cord cultures, we concluded that changes in fatty acid composition, mitochondrial function and proteasome activity, which may be driven by excitotoxicity, lead to oxidative stress and finally contribute to ER stress in sporadic ALS.

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Induction of the Unfolded Protein Response in Familial Amyotrophic Lateral Sclerosis and Association of Protein-disulfide Isomerase with Superoxide Dismutase 1
Atkin, J. D., Farg, M. A., Turner, B. J., Tomas, D., Lysaght, J. A., Nunan, J., Rembach, A., Nagley, P., Beart, P. M., Cheema, S. S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603393200 · Cited by 289
Retracted
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616
ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors
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Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
Obeng, E. A., Carlson, L. M., Gutman, D. M., Harrington, W. J., Lee, K. P., & Boise, L. (2006) · Blood · doi:10.1182/blood-2005-08-3531 · Cited by 1,176
Novel Docosatrienes and 17S-Resolvins Generated from Docosahexaenoic Acid in Murine Brain, Human Blood, and Glial Cells
Hong, S., Gronert, K., Devchand, P. R., Moussignac, R.-L., & Serhan, C. N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300218200 · Cited by 1,000
Endoplasmic Reticulum Stress Signaling in Disease
Marciniak, S. J., & Ron, D. (2006) · Physiological Reviews · doi:10.1152/physrev.00015.2006 · Cited by 951
ER stress and neurodegenerative diseases
Lindholm, D., Wootz, H., & Korhonen, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401778 · Cited by 882
Evidence of Increased Oxidative Damage in Both Sporadic and Familial Amyotrophic Lateral Sclerosis
Ferrante, R. J., Browne, S. E., Shinobu, L. A., Bowling, A. C., Baik, M. J., MacGarvey, U. M., Kowall, N. W., Brown, R. H., & Beal, M. F. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052064.x · Cited by 808
Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species
Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 711
Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and ‘aggresomes’ during oxidative stress, aging, and disease
Grune, T., Jung, T., Merker, K., & Davies, K. J. A. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.04.020 · Cited by 666

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Authors: Ilieva, E. V., Ayala, V., Jove, M., Dalfo, E., Cacabelos, D., Povedano, M., Bellmunt, M. J., Ferrer, I., Pamplona, R., & Portero-Otin, M.
Affiliations: Universitat de Lleida (ES)
ORCID: Ilieva, E. V.
Ayala, V.
Povedano, M.
Ferrer, I.
Pamplona, R.
Venue: Brain
Publisher: Oxford University Press (OUP)
Published: 2007-05-03
Volume: 130
Issue: 12
Pages: 3111-3123
ISSN: 0006-8950 (ISSN-L)
1460-2156
DOI: 10.1093/brain/awm190
OpenAlex: W2105174553
Cited by: 358
References: 72
Citations by year: 2026: 12 · 2025: 12 · 2024: 21 · 2023: 15 · 2022: 17 · 2021: 14 · 2020: 17 · 2019: 20 · 2018: 13 · 2017: 23 · 2016: 15 · 2015: 26 · 2014: 23 · 2013: 21 · 2012: 28
FWCI: 13.37
Type: journal article
Language: en
Open access: closed
Locations: Brain (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: sporadic ALS, endoplasmic reticulum stress, oxidative stress, protein oxidation, protein disulfide isomerase, eIF2α phosphorylation, proteasome impairment, ubiquitin, docosahexaenoic acid, omega-3 fatty acids, mitochondrial dysfunction, respiratory chain complexes, frontal cortex, excitotoxicity, spinal cord
MeSH terms: Adult, Aged, Amyotrophic Lateral Sclerosis, Endoplasmic Reticulum, Fatty Acids, Female, Frontal Lobe, Humans, Male, Middle Aged, Mitochondria, Nerve Tissue Proteins, Organ Culture Techniques, Oxidation-Reduction, Spinal Cord, Oxidative Stress, Ubiquitin, Proteasome Endopeptidase Complex

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Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis

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