Diego Pajares Herrera
Pronouns: He/His/Him
Research Mentor(s): Matthew Holding
Research Mentor School/College/Department: Life Sciences Institute/EEB / Other
Program:
Authors: Diego Pajares Herrera, Matthew Holding, Laura Haynes, David Ginsburg
Session: Session 4: 1:40 pm – 2:30 pm
Poster: 66
Abstract
Regulation of blood clotting is important to avoid excessive bleeding or clotting. Plasminogen activator inhibitor (PAI-1) is a protein that belongs to the family of serine protease inhibitors (SERPINs). These proteins inhibit plasminogen activators that start fibrinolysis, a process that dissolves blood clots. Additionally, these proteins are believed to coevolve specificity with their target proteases, leading to the prediction of differential specificity in PAI-1 between different animal species. The primary aim of this study is to enhance our understanding of the coevolution between PAI-1 and plasminogen activators by testing the specificity of 9 species’ PAI-1 proteins to different two proteases. This study uses PAI-1 samples from lemur, pangolin, echidna, ermine, rabbit, sheep, tarsier, shrew, and human. By comparing the inhibition of the proteases Coagulation Factor XIIa and uPA, we assess which inhibitor is best at human uPA. If coevolution occurred, it is anticipated that species more distantly related to humans will exhibit poorer inhibition of human uPA compared to human PAI-1. We expect to see reciprocal specificity if we alter the species’ origin of the uPA protease. It is expected that rabbit and ermine PAI-1 will exhibit higher inhibition against their respective uPA. This would highlight how molecular traits coevolve and diverge over time.
