University of Washington
NW-120 Health Sciences Building
Laboratory Medicine, Box 357110
Seattle, WA 98195-7110
Phone: (206) 598-6131
FAX: (206) 598-6189
Laboratory Medicine Site
Tait Research Lab Site
Dr. Tait's laboratory works on the annexin family of calcium-dependent phospholipid binding proteins. The long-range goal of this research is to understand how annexins interact with cell membranes, and to develop better means to diagnose and treat disorders related to thrombosis and apoptosis. The interaction of annexin V with phospholipids, platelets, leukocytes, and erythrocytes has been characterized quantitatively. These results show that annexin V is an excellent probe for detection and functional inhibition of cellular procoagulant phospholipid (primarily phosphatidylserine). Currently, the structural requirements for membrane binding are being investigated, and annexin V is being developed as a means to image apoptotic cells in vivo in clinical areas such as organ transplant rejection, cancer chemotherapy, myocardial infarction, and stroke. .
Investigator: Dr. Tait is Professor of Laboratory Medicine and Adjunct Professor of Pathology and Medicine/Medical Genetics. He also directs the clinical molecular genetics laboratory in Laboratory Medicine at the University of Washington Medical Center, which provides DNA-based clinical testing for genetic diseases.
Tait JF, Gibson D, Fujikawa K. Phospholipid binding properties of human placental anticoagulant protein I, a member of the lipocortin family. J Biol Chem 1989; 264:7944-7949.
Thiagarajan P, Tait JF. Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets. J Biol Chem 1990; 265:17420-17423.
Stratton JR, Dewhurst TA, Kasina S, Reno JM, Cerqueira MD, Baskin DG, Tait JF. Selective uptake of radiolabeled annexin V on acute porcine left atrial thrombi. Circulation 1995; 92:3113-21.
Wood BL, Gibson DF, Tait JF. Increased phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations. Blood 1996; 88:1873-80.
Blankenberg FG, Katsikis PD, Tait JF, Davis RE, Naumovski L, Ohtsuki K, Kopiwada S, Abrams MJ, Darkes M, Robbins RC, Maecker HT, Strauss HW. In vivo detection and imaging of phosphatidylserine expression during programmed cell death. Proc Natl Acad Sci USA 1998; 95:6349-6354.
Tait JF, Smith C, Wood BL. Measurement of phosphatidylserine exposure in leukocytes and platelets by whole-blood flow cytometry with annexin V. Blood Cells Molec Dis 1999; 25:271-278.
Tait JF, Brown DS, Gibson DF, Blankenberg FG, Strauss HW. Development and characterization of annexin V mutants with endogenous chelation sites for 99mTc. Bioconjugate Chemistry 2000; 11:918-925.
Tait JF, Gibson DF, Smith C. Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy. Analytical Biochemistry 2004; 329:112-9.
Jin M, Smith C, Hsieh HY, Gibson DF, Tait JF. Essential role of B-helix calcium binding sites in annexin V-membrane binding. J Biol Chem 2004; 279:40351-57.
Tait JF, Smith C, Blankenberg FG. Structural requirements for in vivo detection of cell death with 99mTc-annexin V. J Nucl Med 2005; 46:807-815.
Tait JF, Smith C, Levashova Z, Patel B, Blankenberg FG, Vanderheyden J-L. Improved detection of cell death in vivo with annexin V radiolabeled by site-specific methods. J Nucl Med 2006; 47:1546-1553.
Jeppesen B, Smith C, Gibson DF, Tait JF. Entropic and enthalpic contributions to annexin V-membrane binding. A comprehensive quantitative model. J Biol Chem 2008; 283: 6126-6135.
Smith C, Gibson DF, Tait JF. Transmembrane voltage regulates binding of annexin V and lactadherin to cells with exposed phosphatidylserine. BMC Biochem 2009; 10(1): 5. Available at: http://www.biomedcentral.com/1471-2091/10/5