Thomas Bugge, Ph.D.
NIH/NIDCR
Building 30, Room 211
30 Convent Dr. MSC 4340
Bethesda, MD 20892-4340
United States
Vertebrate genomes encode hundreds of proteolytic enzymes that act on the surface of cells to regulate a range of biological processes. When missing or inappropriately regulated, these proteolytic enzymes also play a critical role in the development and progression of many important human diseases. The goal of Dr. Bugge’s research is to understand the biochemistry, biology, and pathology of cell-surface proteolytic enzymes. His team is particularly interested in determining their contribution to the development, regeneration, and malignant transformation of oral tissues. He and his colleagues also work on exploiting the detailed knowledge of protease expression in human cancer—generated from basic research studies—to develop novel tumor protease-activated pro-drugs for cancer therapy.
Biographical Sketch
Dr. Thomas Bugge performed his Ph.D. research on nuclear receptors at the European Molecular Biology Laboratory, Heidelberg, Germany. His postdoctoral studies at Childrens' Hospital Research Foundation, Cincinnati, OH, focused on understanding the biology of fibrinolytic proteins. Dr. Bugge was a research leader at the Finsen Laboratory, Copenhagen, Denmark and associate professor of pediatrics at the University of Cincinnati where he worked on fibrinolytic proteins, before being recruited to his current position at NIDCR in 1999. Dr. Bugge has received several NIH and international awards for his research, mentoring, and service to the scientific community, including the 2012 International Society for Fibrinolysis and Proteolysis Prize for "Outstanding Contributions to the Field of Fibrinolysis, Thrombolysis and Proteolysis," and the 2016 NIH Director’s Ruth L. Kirschstein Mentoring Award “For exemplary performance while demonstrating significant leadership, skill and ability in serving as a mentor. “
- Liu S, Liu J, Ma Q, Cao L, Fattah RJ, Yu Z, Bugge TH, Finkel T, Leppla SH. Solid tumor therapy by selectively targeting stromal endothelial cells. Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):E4079-87.
- Motley MP, Madsen DH, Jürgensen HJ, Spencer DE, Szabo R, Holmbeck K, Flick MJ, Lawrence DA, Castellino FJ, Weigert R, Bugge TH. A CCR2 macrophage endocytic pathway mediates extravascular fibrin clearance in vivo. Blood. 2016 Mar 3;127(9):1085-96.
- Szabo R, Lantsman T, Peters DE, Bugge TH. Delineation of proteolytic and non-proteolytic functions of the membrane-anchored serine protease prostasin. Development. 2016 Aug 1;143(15):2818-28.
- Friis S, Madsen DH, Bugge TH. Distinct Developmental Functions of Prostasin (CAP1/PRSS8) Zymogen and Activated Prostasin. J Biol Chem. 2016 Feb 5;291(6):2577-82.
- Madsen DH, Leonard D, Masedunskas A, Moyer A, Jürgensen HJ, Peters DE, Amornphimoltham P, Selvaraj A, Yamada SS, Brenner DA, Burgdorf S, Engelholm LH, Behrendt N, Holmbeck K, Weigert R, Bugge TH. M2-like macrophages are responsible for collagen degradation through a mannose receptor-mediated pathway. J Cell Biol. 2013 Sep 16;202(6):951-66.
- Szabo R, Bugge TH. Membrane-anchored serine proteases in vertebrate cell and developmental biology. Annu Rev Cell Dev Biol. 2011;27:213-35.
- Sales KU, Masedunskas A, Bey AL, Rasmussen AL, Weigert R, List K, Szabo R, Overbeek PA, Bugge TH. Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome. Nat Genet. 2010 Aug;42(8):676-83.
- Connolly BM, Choi EY, Gårdsvoll H, Bey AL, Currie BM, Chavakis T, Liu S, Molinolo A, Ploug M, Leppla SH, Bugge TH. Selective abrogation of the uPA-uPAR interaction in vivo reveals a novel role in suppression of fibrin-associated inflammation. Blood. 2010 Sep 2;116(9):1593-603.
- List K, Kosa P, Szabo R, Bey AL, Wang CB, Molinolo A, Bugge TH. Epithelial integrity is maintained by a matriptase-dependent proteolytic pathway. Am J Pathol. 2009 Oct;175(4):1453-63.
- Szabo R, Hobson JP, Christoph K, Kosa P, List K, Bugge TH. Regulation of cell surface protease matriptase by HAI2 is essential for placental development, neural tube closure and embryonic survival in mice. Development. 2009 Aug;136(15):2653-63.