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Peter N. Walsh, MD, PhD
Professor Emeritus, Medicine Professor, Sol Sherry Thrombosis Research Center Professor, Fels Institute for Cancer Research and Molecular Biology Professor, Biochemistry Telephone: 215-707-4375 Fax: 215-707-3005 Email: pnw@temple.edu
Sol Sherry Thrombosis Research CenterFels Institute of Cancer Research and Molecular BiologyDepartment of Biochemistry
Molecular and Cellular Interactions of Blood Coagulation Proteins.
Research focuses on the characterization, intermolecular interactions and structure-function relationships of coagulation proteins and their interactions with platelets, and includes four specific NIH-funded projects, as follows:
Molecular Interactions of Factor XI. Recent observations resulting in the recognition of the essential role of FXI in hemostasis concern the relationship of its domain structure to its biological function, the molecular genetics of FXI, its molecular and cellular interactions, the elucidation of newly discovered pathways for activation of FXI, and the expression and regulation of its enzymatic activity. The long-term goals of this project are to elucidate the molecular mechanisms involved in the interaction of FXI with protein and cell surface ligands involved in its activation and in the expression and regulation of FXIa enzymatic activity.
Exosite Function in the Catalytic Domain of Coagulation Factor XIa. The long-term goals of this project are to elucidate the molecular mechanisms involved in the interaction of FXIa with its substrate, its cellular (platelet) receptor(s) and its regulators, including the platelet-secreted Kunitz inhibitor, protease nexin-2 and to define the structural biology mediating the exposure of exosites within the catalytic domain that result from the conversion of the zymogen to the protease.
Platelet Receptor-Mediated Factor X Activation. Platelets promote the catalysis FX activation by a complex of FIXa and FVIIIa by a receptor-mediated complex assembled on activated platelets, involving specific, high-affinity, saturable binding sites for FIXa, FVIII and FX, occupancy of which is closely correlated with rates of F-X activation on the platelet surface. The purpose of our studies is to examine the validity of this three-receptor hypothesis and to determine the structural components on the platelet surface and on the enzyme (FIXa) required for the assembly of this important coagulation complex.
Platelet Factor XI. Studies from our laboratory have focused on a novel but poorly understood unique protein, platelet FXI. The objectives of this project are to accomplish a structural and functional characterization of platelet FXI both at the genomic and protein levels, to determine the molecular basis for the presence of platelet FXI in patients with plasma FXI deficiency, to determine the mechanism of association of platelet FXI with the platelet plasma membrane, and to ascertain the mechanisms of its activation and the expression of its enzymatic activity.
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