ArticleJournal of molecular neuroscience : MN2015
C-Reactive Protein Induces Tau Hyperphosphorylation via GSK3β Signaling Pathway in SH-SY5Y Cells.
Article in Journal of molecular neuroscience : MN, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Inflammatory proteins associated with Alzheimer's disease reduced by a GLP1 receptor agonist: a post hoc analysis of the EXSCEL randomized placebo controlled trial.Alzheimer's research & therapy · 2024Trial
- Monoclonal antibodies and small molecules: on the cutting edge of Alzheimer's disease therapy.Frontiers in cell and developmental biology · 2026Review
- From Better Diagnostics to Earlier Treatment: The Rapidly Evolving Alzheimer's Disease Landscape.Medicina (Kaunas, Lithuania) · 2025Review
- Dementia after Ischemic Stroke, from Molecular Biomarkers to Therapeutic Options.International journal of molecular sciences · 2024Review
- GSK3: A potential target and pending issues for treatment of Alzheimer's disease.CNS neuroscience & therapeutics · 2024Review
- Early Life Stress and Epigenetics in Late-onset Alzheimer's Dementia: A Systematic Review.Current genomics · 2018Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
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Abstract
Amyloid plaques and neurofibrillary tangles are the key pathological features of Alzheimer's disease (AD). Studies have shown that C-reactive protein (CRP) increases during inflammatory reactions and, therefore, has been associated with AD. However, there is no published report relating the impact of CRP to the regulation of tau phosphorylation. In the present study, we investigated the effects of CRP on the phosphorylation of tau protein in SH-SY5Y cells. Treatment of cells with CRP (5, 10, 20 μg/ml) resulted in neurotoxicity and apoptosis, as was observed by MTT assay and Hoechst staining, respectively. Western blot analysis showed that CRP, in a time- and concentration-dependent manner, induced the phosphorylation of tau at Ser202 and ser396 in SH-SY5Y cells. Phosphorylation of Akt (Ser473) and GSK3β (Ser9) were decreased by CRP treatment, whereas phosphorylation of ERK and p38 were not affected. Pharmacological inhibition of GSK3β reversed the effects induced by CRP, viz., cytotoxicity, apoptosis, and tau phosphorylation. Herein, we present a novel mechanism of cell death following CRP insult, which activates tau hyperphosphorylation by regulating GSK3β activity. CRP could potentially be used as an important pathological factor for the therapeutic intervention of AD.
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