Characterization of prekallikrein antibodies and proteomic identification of FXIa substrates on endothelial cells

My research investigates how components of the contact activation system regulate endothelial function. First, I characterized the molecular mechanism of prekallikrein (PK) activation on endothelial cells, identifying the critical roles of the A1–A3 apple domains and validating domain-specific monoclonal antibodies as mechanistic tools and therapeutic candidates. Second, I used label-free quantitative proteomics to reveal how coagulation factor XIa (FXIa) reprograms the endothelial proteome and secretome, suppressing barrier integrity and angiogenesis while promoting immune activation and extracellular matrix remodeling. Together, these studies highlight novel mechanisms linking coagulation factors to vascular inflammation and identify potential therapeutic targets for thromboinflammatory disease