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oai:www.ideals.illinois.edu:2142/14739 2023-07-10 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Morrissey, James H. Morrissey, James H. Schwartz, Bradford S. Sligar, Stephen G. Tajkhorshid, Emad Pureza, Vincent S. 2010-01-06T17:48:33Z 2010-01-06T17:48:33Z 2012-01-07T11:00:11Z 2010-01-06T17:48:33Z Blood coagulation requires the assembly of several membrane-bound protein complexes composed of regulatory and catalytic subunits. The biomembranes involved in these reactions not only provide a platform for these procoagulant proteins, but can also affect their function. Increased exposure of acidic phospholipids on the outer leaflet of the plasma membrane can dramatically modulate the catalytic efficiencies of such membrane-bound enzymes. Under physiologic conditions, however, these phospholipids spontaneously cluster into a patchwork of membrane microdomains upon which membrane binding proteins may preferentially assemble. As a result, the membrane composition surrounding these proteins is largely unknown. Through the development and use of a nanometer-scale bilayer system that provides rigorous control of the phospholipid membrane environment, I investigated the role of phosphatidylserine, an acidic phospholipid, in the direct vicinity (within nanometers) of two critical membrane-bound procoagulant protein complexes and their respective natural substrates. Here, I present how the assembly and function of the tissue factor·factor VIIa and factor Va·factor Xa complexes, the first and final cofactor·enzyme complexes of the blood clotting cascade, respectively, are mediated by changes in their immediate phospholipid environments. Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2009-11-10T21:40:28Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 1 Pureza_Vincent.pdf: 4965433 bytes, checksum: f9aa99a8a02e55387a241c32fa524436 (MD5) Made available in DSpace on 2010-01-06T17:48:33Z (GMT). No. of bitstreams: 2 license.txt: 4063 bytes, checksum: 004c55426054805cd3bf0fa876a12e05 (MD5) Pureza_Vincent.pdf: 4965433 bytes, checksum: f9aa99a8a02e55387a241c32fa524436 (MD5) Item marked as restricted to the 'Administrator' Group (id=1) by William Ingram (wingram2@illinois.edu) on 2010-01-06T17:49:44Z Item is restricted until 2012-01-06T17:49:44Z Item reinstated by Sarah Shreeves (sshreeve@illinois.edu) on 2012-01-07T11:00:11Z Item was in collections: University of Illinois Dissertations and Theses (ID: 204) Dissertations and Theses - Biochemistry (ID: 679) No. of bitstreams: 3 Pureza_Vincent.pdf.txt: 168147 bytes, checksum: f3865e0c215cf0692521ea8359109123 (MD5) license.txt: 4063 bytes, checksum: 004c55426054805cd3bf0fa876a12e05 (MD5) Pureza_Vincent.pdf: 4965433 bytes, checksum: f9aa99a8a02e55387a241c32fa524436 (MD5) Item released from any restrictions by Sarah Shreeves (sshreeve@illinois.edu) on 2012-01-07T11:00:11Z http://hdl.handle.net/2142/14739 en Copyright 2009 Vincent S. Pureza blood coagulation clotting tissue factor prothrombin prothrombinase thrombin tenase intrinsic extrinsic factor VIIa nanotechnology Nanodiscs phospholipids membranes anionic hemostasis thrombosis heart disease hemostatic agent Blood coagulation reactions on nanoscale membrane surfaces 2009-12 Biochemistry 1438 Biochemistry 0318 University of Illinois at Urbana-Champaign Dissertation Ph.D. PHD:Biochemistry -UIUC 10KS0318PHD