Publications by authors named "Nima Mazinani"
Article Synopsis
- - The study investigates the role of amyloid β precursor protein (APP) in platelets, highlighting that APP moves to the platelet surface during activation and gets processed into metabolites like amyloid β and soluble APP.
- - Researchers found that activated coagulation factor XIII (FXIII-A*) binds to APP and enhances its processing, with further activation leading to significant increases in this binding.
- - Inhibition of FXIII-A* improved the breakdown of APP, suggesting that manipulating APP processing could be a potential therapeutic strategy for treating Alzheimer's disease.
Bleeding is increased in amyloid precursor protein knockout mouse.
Res Pract Thromb Haemost
July 2020
Article Synopsis
- APP plays a significant role in hemostasis, with its absence leading to increased bleeding in mice models, particularly during tail transections.
- Blood loss was comparable in APP knockout (KO) and wild-type (WT) mice for liver lacerations, but APP KO mice bled more in tail transections, especially when treated with specific medications.
- Analysis of blood from APP KO mice showed longer clotting times and weaker clots, highlighting the importance of platelet-derived APP and Aβ peptides in blood clotting and overall hemostasis.
Article Synopsis
- * Research found that while FXII is activated by nonbiological surfaces like soil, it does not significantly affect bleeding in clean wounds, indicating its unique role in more contaminated situations.
- * In experiments with wild-type and FXII-knocked out mice, soil reduced blood loss and sped up clotting in FXII-dependent manner, supporting the idea that FXII is crucial for managing bleeding in dirtier environments, unlike clean injuries.
Article Synopsis
- In cerebral amyloid angiopathy (CAA) and Alzheimer's disease (AD), amyloid β (Aβ) peptides accumulate around blood vessels, causing damage to surrounding tissues.
- Activated coagulation factor XIIIa (FXIIIa) plays a role in linking proteins, but its interaction with Aβ wasn't previously established.
- New experiments demonstrated that FXIIIa can covalently cross-link Aβ40 into larger structures and increase the stiffness of blood clots, indicating a potential role for FXIIIa in the formation of Aβ deposits in these diseases.
Article Synopsis
- Short-chain polyphosphate (polyP) is released from activated platelets, but its role in thrombosis is unclear.
- Numerical simulations and in vitro tests showed that localized synthetic polyP significantly speeds up clotting in flowing blood, especially at low shear rates typical of thrombotic conditions.
- While localized polyP can accelerate clotting at very low concentrations, the biological reasons for its localization on platelet or vascular surfaces are still unknown.
Article Synopsis
- Coagulation factor XIIIa (FXIIIa) is crucial for stabilizing blood clots by cross-linking fibrin and other proteins, but its inactivation mechanism is not well understood.
- This study reveals that plasmin, an enzyme involved in blood clot breakdown, can effectively cleave and inactivate FXIIIa, showing a high catalytic efficiency in both purified systems and blood.
- The research found that FXIIIa is particularly susceptible to plasmin during clot lysis, and its inactivation is influenced by the presence of fibrinogen and tissue plasminogen activator.