ArticleJournal of neurochemistry2011
Decreased activity of the 20S proteasome in the brain white matter and gray matter of patients with multiple sclerosis.
Article in Journal of neurochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- The role of autophagy in the pathogenesis and treatment of multiple sclerosis.Autophagy reports · 2025Review
- Oxidative Stress Markers in Multiple Sclerosis.International journal of molecular sciences · 2024Review
- A novelFrontiers in cellular neuroscience · 2024Article
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- An Overview of Recent Advances in the Neuroprotective Potentials of Fisetin against Diverse Insults in Neurological Diseases and the Underlying Signaling Pathways.Biomedicines · 2023Review
- Bisphenol-A (BPA) Impairs Hippocampal Neurogenesis via Inhibiting Regulation of the Ubiquitin Proteasomal System.Molecular neurobiology · 2023Article
- Molecular alteration of the proteasome contributes to AD-like pathology in the brain of HFD-STZ diabetic rats.Metabolic brain disease · 2023Article
- RNA-binding proteins as a common ground for neurodegeneration and inflammation in amyotrophic lateral sclerosis and multiple sclerosis.Frontiers in molecular neuroscience · 2023Review
- Genetic variations in theExperimental and therapeutic medicine · 2021Article
- The impact of regional astrocyte interferon-γ signaling during chronic autoimmunity: a novel role for the immunoproteasome.Journal of neuroinflammation · 2020Article
- The role of PSMB5 in sodium arsenite-induced oxidative stress in L-02 cells.Cell stress & chaperones · 2020Article
- Decreased levels of constitutive proteasomes in experimental autoimmune encephalomyelitis may be caused by a combination of subunit displacement and reduced Nfe2l1 expression.Journal of neurochemistry · 2020Article
- Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019Review
- A Sentinel in the Crosstalk Between the Nervous and Immune System: The (Immuno)-Proteasome.Frontiers in immunology · 2019Review
- Effects of a novel orally administered calpain inhibitor SNJ-1945 on immunomodulation and neurodegeneration in a murine model of multiple sclerosis.Journal of neurochemistry · 2014Article
- NQO1 gene rs1800566 variant is not associated with risk for multiple sclerosis.BMC neurology · 2014Article
- Detection of protein aggregates in brain and cerebrospinal fluid derived from multiple sclerosis patients.Frontiers in neurology · 2014Review
- Current understanding on the role of standard and immunoproteasomes in inflammatory/immunological pathways of multiple sclerosis.Autoimmune diseases · 2014Review
- Increased carbonylation, protein aggregation and apoptosis in the spinal cord of mice with experimental autoimmune encephalomyelitis.ASN neuro · 2013Article
- Inhibitors of the immunoproteasome: current status and future directions.Current pharmaceutical design · 2013Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Carbonylated (oxidized) proteins are known to accumulate in the cerebral white matter (WM) and gray matter (GM) of patients with multiple sclerosis (MS). Although oxidative stress is necessary for carbonyl generation, it is the failure of the degradation systems that ultimately leads to the build-up of carbonylated proteins within tissues. In this study, we measured the activity of the 20S proteasome and other proteolytic systems in the cerebral WM and GM of 13 MS patients and 13 controls. We report that the activities of the three peptidases of the 20S proteasome (i.e. chymotrypsin-like, caspase-like and trypsin-like) in both MS-WM and MS-GM are greatly reduced. Interestingly, neither the amount of proteasome nor the levels of the catalytic subunits (β1, β2, and β5) are diminished in this disease. Proteins containing Lys-48 poly-ubiquitin also accumulate in MS tissues, indicating failure of the 26S proteasome as well. Levels of the regulatory caps 11S α and 19S are also lower in MS than in controls, suggesting that the activity of the more complex proteasomes may be reduced further. Finally, the activities of other proteases that might also remove oxidized proteins (calpain, cathepsin B, mitochondrial LonP) are not lessened in MS. Together, these studies suggest that direct inactivation of proteolytic centers in the 20S particle and/or the presence of specific inhibitors is the underlying cause of proteasomal dysfunction in MS.
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Registered trials
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