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Fibrinogen Mitigates Prion-Mediated Platelet Activation and Neuronal Cell Toxicity
Deepa Gautam1,2, Jyotsna Kailashiya1, Arundhati Tiwari1
1Center for Advanced Research on Platelet Signaling and Thrombosis Biology, Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi, India.
Frontiers in Cell and Developmental Biology
|April 7, 2022
Summary
Prion peptide (PrP) interacts with fibrinogen, reducing neuronal toxicity and platelet pro-thrombotic responses. This novel interaction may offer therapeutic strategies for prion diseases.
Area of Science:
- Neuroscience
- Biochemistry
- Hematology
Background:
- Prion diseases involve misfolded prion protein (PrP) forming amyloid fibrils.
- Prion peptide (PrP) sequence 106-126 is amyloidogenic and linked to prion pathologies.
- PrP is associated with pro-thrombotic effects and neuronal toxicity.
Purpose of the Study:
- To investigate the interaction between PrP(106-126) and fibrinogen.
- To determine the effect of this interaction on platelet responses and neuronal toxicity.
- To explore the impact of PrP on fibrin clot formation and stability.
Main Methods:
- Studied the interaction between PrP(106-126) and fibrinogen.
- Assessed PrP-fibrinogen effects on platelet cytosolic calcium, calpain activation, and extracellular vesicle shedding.
- Evaluated the impact of PrP-fibrinogen on neuronal cell cytotoxicity.
- Analyzed PrP's effect on fibrin clot formation and resistance to plasmin-mediated fibrinolysis.
Main Results:
- Fibrinogen mitigated PrP-induced increases in platelet cytosolic calcium, calpain activation, and extracellular vesicle shedding.
- Fibrinogen exposure averted PrP-induced neuronal cell toxicity.
- PrP accelerated fibrin clot formation, resulting in clots resistant to fibrinolysis.
- These findings suggest enhanced thrombus stability due to PrP.
Conclusions:
- The interaction between PrP and fibrinogen can mitigate PrP-induced cellular toxicity and pro-thrombotic responses.
- This interaction may be clinically relevant for managing prion-related disorders.
- Developing molecules that mimic PrP-binding sites on fibrinogen could be a therapeutic strategy.
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