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Publication: Protein tyrosine phosphatase PTPN22 negatively modulates platelet function and thrombus formation

In platelets, engagement of platelet surface receptors glycoprotein VI (GPVI) or GPIb-IX-IV by their respective ligands collagen or von Willebrand factor exposed from the subendothelial matrix at the site of vascular injury triggers the phosphorylation of several proteins, leading to activation and transduction of intraplatelet signaling pathway. In this study, a BioFlux shear flow system was used to examine platelet adhesion and aggregation to fibrillar collagen in mepacrine-labeled whole blood to assess adhesive mechanisms. The investigators used a BioFlux to help determine that PTPN22 inhibition enhanced aggregation, spreading, and clot retraction, revealing a novel role of PTPN22 in platelet function and arterial thrombosis.

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