ArticleInternational journal of molecular sciences2019
Epitope Mapping Immunoassay Analysis of the Interaction between β-Amyloid and Fibrinogen.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Multimer Detection System: A Universal Assay System for Differentiating Protein Oligomers from Monomers.International journal of molecular sciences · 2025Review
- Fibrin-Targeting Immunotherapy for Dementia.The journal of prevention of Alzheimer's disease · 2023Article
- Application of Next-Generation Sequencing in Neurodegenerative Diseases: Opportunities and Challenges.Neuromolecular medicine · 2021Review
- Neuroblastoma SH-SY5Y cytotoxicity, anti-amyloidogenic activity and cyclooxygenase inhibition of3 Biotech · 2020Article
- Advance in Plasma AD Core Biomarker Development: Current Findings from Immunomagnetic Reduction-Based SQUID Technology.Neurology and therapy · 2019Review
- Anti-Amyloidogenic and Cyclooxygenase Inhibitory Activity ofMolecules (Basel, Switzerland) · 2019Article
- Potential Fluid Biomarkers for the Diagnosis of Mild Cognitive Impairment.International journal of molecular sciences · 2019Review
- Genetic analyses of early-onset Alzheimer's disease using next generation sequencing.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vast majority of patients with Alzheimer's disease (AD) suffer from impaired cerebral circulation. Substantial evidence indicates that fibrinogen (Fbg) and fibrin clot formation play an important role in this circulatory dysfunction in AD. Fbg interacts with β-amyloid (1-42) (Aβ), forming plasmin-resistant abnormal blood clots, and increased fibrin deposition has been discovered in the brains of AD patients and mouse models. In this study, biochemical approaches and the epitope mapping immunoassay were employed to characterize binding epitopes within the Fbg and complementary epitopes in Aβ. We discovered the Aβ5⁻25 peptide as the most critical region for the interaction, which can be inhibited by specific monoclonal and polyclonal antibodies against the central region of Aβ. Aβ binding to Fbg may block plasmin-mediated fibrin cleavage at this site, resulting in the generation of increased levels of plasmin-resistant fibrin degradation fragments. Our study elucidates the Aβ⁻Fbg interaction that may involve the mechanism by which Aβ⁻Fbg binding delays fibrinolysis by plasmin, providing valuable information in the development of therapeutic approaches for AD.
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Registered trials
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