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New Insights Into An Old Interaction: Developing A Model For Pai-1:Vn Interactions, Letitia Nichole Puster
New Insights Into An Old Interaction: Developing A Model For Pai-1:Vn Interactions, Letitia Nichole Puster
Doctoral Dissertations
Active human Plasminogen Activator Inhibitor 1 (PAI-1) is most often found in complex with Vitronectin (VN), an ~62kDa glycoprotein. Research has shown PAI-1 and VN form higher order complexes in tissues, and our work indicates a 2:1 (PAI-1:VN) stoichiometry for these complexes. A logical model for PAI-1:VN interaction proposes that two PAI-1 molecules bind VN at separate sites. However, our small-angle neutron scattering (SANS) data suggest that there is a PAI-1: PAI-1:VN interaction, in which PAI-1 forms a dimer when in complex with VN. We tested this novel arrangement of PAI-1 within the complex by using a variety of biophysical …
From Loop To Strand: Characterization Of The Conformation And Dynamics Of The Human Plasminogen Activator Inhibitor-1 Reactive Center, Tihami Qureshi
From Loop To Strand: Characterization Of The Conformation And Dynamics Of The Human Plasminogen Activator Inhibitor-1 Reactive Center, Tihami Qureshi
Doctoral Dissertations
Plasminogen activator inhibitor-1 (PAI-1), with its cofactor vitronectin (VN), controls the rate of plasmin-mediated fibrin breakdown in blood clots by inhibiting tissue-plasminogen activator (tPA) and urokinase-plasminogen activator (uPA). The activity of PAI-1 is attributed to its reactive center loop (RCL), which is solvent-exposed in an active conformation, but inserts as an additional strand into its central β [beta]-sheet during transition to a latent state and during inhibition. VN slows the latency transition, and the rate at which PAI-1 inhibits the plasminogen activators (PAs) also differs. However, the steps during the latency transition, mechanism of VN stabilization, and basis for inhibitory …
Recombinant Production Of Vitronectin And Insights Into Its Structure And Role In Fibrinolysis, Cameron T. Landers
Recombinant Production Of Vitronectin And Insights Into Its Structure And Role In Fibrinolysis, Cameron T. Landers
Chancellor’s Honors Program Projects
No abstract provided.
Studies On The Role Of Vitronectin And Plasminogen-Activator Inhibitor-1 Complexes Beyond Inhibiting Proteases: Binding To The Extracellular Matrix, Cell Interactions And Pathogenesis, Sumit Goswami
Doctoral Dissertations
Plasminogen activator inhibitor-1 (PAI-1), a member of the serine protease inhibitor (serpin) superfamily of proteins, circulates in blood in a complex with vitronectin (VN). These two proteins are also found localized together in the extracellular matrix in many different pathophysiological conditions. Both of these proteins are involved with a number of physiologically important processes. Though PAI-1 is a well-known inhibitor of serine proteases, more emphasis is now geared towards its protease independent functions. VN, on the other hand, is a binding protein that exists in the circulation in a preferred monomeric conformation. However, in the extracellular matrix, VN exists as …