About Dr. Thompson

About Me...

I am an assistant professor here at Middle Tennessee State University in the Department of Biology. Before I came here, I was previously an adjunct professor at Southeastern Career College in Nashville and the University of Phoenix in Nashville. Prior to that, I served as a postdoctoral fellow in the Department of Pathology at Vanderbilt University as a part of the Vascular Biology program, where I studied plasminogen activation and the activation of Factor V.

My primary teaching responsibilities include Genetics, Anatomy & Physiology, and Exploring Life (non-majors biology), but I do teach other courses from time to time as needed.  My laboratory research studies inflammation, primarily through zinc metallopeptidases, such as leukotriene A₄ hydrolase, puromycin-sensitive aminopeptidase, and matrix metalloproteinase-2 (MMP-2), that create and/or inactivate various inflammatory mediators.

Education

B.S., 1993, Zoology and Chemistry, University of Louisville, Louisville, KY
Ph.D., 2000, Biochemistry, University of Kentucky, Lexington, KY
Postdoctoral Fellow, 2000-2004, Pathology, Vanderbilt University, Nashville, TN

Publications

Peer-Reviewed Publications

1. Thompson, M.W., Archer, E.D., Romer, C.E., and Seipelt, R.L. (2006).  A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A₄ hydrolase stabilizes the transition state of the peptidase activity.  Peptides 27, 1701-1709.
2. Thompson, M.W., Govindaswami, M., and Hersh, L.B. (2003). Mutation of active site residues of the puromycin-sensitive aminopeptidase: conversion of the enzyme into a catalytically inactive binding protein. Archives of Biochemistry and Biophysics 413, 236-242.
3. Thompson, M.W. and Hersh, L.B. (2003). Analysis of conserved residues of the human puromycin-sensitive aminopeptidase. Peptides 24, 1359-1365.
4. Ma, Z., Daquin, A., Yao, J., Rodgers, D., Thompson, M.W. and Hersh, L.B. (2003). Proteolytic cleavage of the puromycin sensitive aminopeptidase generates a substrate binding domain. Archives of Biochemistry and Biophysics 415, 80-86.
5. Stoltze, L., Schirle, M., Schwarz, G., Schroter, C., Thompson, M.W., Hersh, L.B., Kalbacher, H., Stevanovic, S., Rammensee, H.G., and Schild, H. (2000). Two new proteases in the MHC class I processing pathway. Nature Immunology 1, 413-418.
6. Thompson, M.W., Tobler, A.R., Fontana, A., and Hersh, L.B. (1999). Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase. Biochemistry and Biophysics Research Communications 258, 234-240.

Invited Publications

1. Csuhai, E., Safavi, A., Thompson, M.W., and Hersh, L.B. (1998). Proteolytic inactivation of secreted neuropeptides. In V. Y. H. Hook (Ed.), Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing (173-189). Austin, TX: Landes.
2. Thompson, M.W. and Hersh, L.B. (2004). The puromycin-sensitive aminopeptidase: its role in neurological, reproductive, immunological, and proliferative disorders. In N.M. Hooper and U. Lendeckel (Eds.), Aminopeptidases in Biology and Disease (1-15). New York: Kluwer.

Abstracts

1. Thompson, M.W., Romer, C. E., and Seipelt, R.L. Two conserved tyrosine residues are essential for the peptidase activity of Saccharomyces cerevisiae leukotriene A₄ hydrolase. IUPS/ Experimental Biology 2005 Conference (ASBMB), San Diego, CA, April 2005.
2. Thompson, M.W., Tobler, A., Fontana, A., and Hersh, L.B. Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase. International Neuropeptide Society's 2000 Summer Neuropeptide Conference, Sainte-Adele, Quebec, Canada, 2000.
3. Romer, C., Dorset, D., Meyer, C., Thompson, M.W., and Seipelt, R.L. Cloning and Characterization of Yeast Leukotriene A₄ Hydrolase. Association of Southeastern Biologists Conference, Memphis, TN, 2004.
4. Romer, C., Dorset, D., Meyer, C., Thompson, M.W., and Seipelt, R.L. Cloning and Characterization of Yeast Leukotriene A₄ Hydrolase. Tennessee Academy of Science/Tennessee Science Teachers Association Meeting, Franklin, TN, 2004.
5. Thompson, M. W., Romer, C. E., and Seipelt, R. L. Tyrosine 244 Stabilizes the Transition State of the Peptidase Reaction of Saccharomyces cerevisiae Leukotriene A₄ Hydrolase. Tennessee Academy of Science Meeting, Martin, TN, 2005.
6. Archer, E. D., Seipelt, R. L., and Thompson, M. W. A Conserved Tryptophan Residue With an Altered pKa Is Essential for the Peptidase Reaction of Saccharomyces cerevisiae Leukotriene A₄ Hydrolase. Tennessee Academy of Science Meeting, Martin, TN, 2005.
7. Archer, E. D., Seipelt, R. L., and Thompson, M. W. A Conserved Tryptophan Residue With an Altered pKa Is Essential for the Peptidase Reaction of Saccharomyces cerevisiae Leukotriene A₄ Hydrolase. ASBMB/ Experimental Biology 2006 Conference, San Francisco, CA, 2006 (Submitted).
8. Thompson, M. W., Archer, E. D., Terry, A. N., and Seipelt, R. L. Halide ions alter substrate specificity of Saccharomyces cerevisiae leukotriene A₄ hydrolase but do not increase catalytic efficiency. ASBMB/ Experimental Biology 2006 Conference, San Francisco, CA, 2006 (Submitted).