Associate Member, Biochemistry and Molecular Biology
Professor, Oral and Biological Sciences
Canada Research Chair in Proteases and Diseases
Martin Luther University Halle-Wittenberg, GDR, 1980, MSc, Biochemistry
Martin Luther University Halle-Wittenberg, GDR, 1983, Biochemistry
Friedrich-Schiller-University Jena, Germany, 1997, D.Sc. Biochemistry
phone: 6048221787
Life Sciences Centre LSI 4.558
2350 Health Sciences Mall
Vancouver, BC V6T 1Z3

Many human diseases are characterized by an excessive proteolytic degradation of proteins of the extracellular matrix (e.g., bone and cartilage diseases, atherosclerosis, destructive lung diseases, cancer) or by an inappropriate proteolytic processing of proteins leading to auto-immune diseases and disorders caused by regulatory defects. Our laboratory is leading in the identification of novel therapeutic targets among intracellular lysosomal proteases and is focused on the role of these proteases in the pathogenesis of rheumatoid arthritis, atherosclerosis and certain forms of immune disorders. Our aim is to understand the role of lysosomal proteases in health and disease which may lead to new therapeutic approaches to treat these illnesses. To achieve our objective, we exploit an interdisciplinary approach which includes methods of molecular biology, enzymology, crystallography, histology, animal models and a wide range of collaborations with clinical and biotech institutions.

For full bibliography see:

Regulation of the collagenase activity of cathepsins by glycosaminoglycans.
Li, Z., Yasuda, Y., Li, W. Bogyo, M., Katz, N., Gorden, R. Fields, G.B., Brömme, D.
J. Biol.Chem. 279, 5470-5479, 2004.

Cysteine protease cathepsin F is present in atherosclerotic lesions and induces low density lipoprotein aggregation, fusion, and retention to human aortic proteoglycans in vitro.
Öörni, K., Sneck, M., Brömme, D., Pentikäinen, M.O., Mäyränpää, M., Aitio, H., Kovanen, P.T.
J.Biol. Chem. 259, 34776-84, 2004.

Cathepsin V: A novel and potent elastolytic activity expressed in activated macrophages.
Yasuda, Y., Li, Z., Greenbaum. D., Bogyo, M., Weber, E., Brömme, D.
J. Biol. Chem. 279, 36761-70, 2004.

Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L. Arch.
Puzer, L., Cotrin, S.S., Alves, M.F., Egborge, T., Araujo, M.S., Juliano, M.A., Juliano, L., Brömme, D., Carmona, A.K.
Biochem. Biophys. 430, 274-83, 2004.

Cathepsin V. Cathepsin V is involved in the Degradation of Invariant Chain in Human Thymus and is Overexpressed in Myasthenia Gravis.
Tolosa, E., Li, W., Yasuda, Y., Denzin, L.K., Stevanovic, S., Driessen, C., Kurek, R., Weber, E., Melms, A., Brömme, D.
J. Clin. Invest. 2003;112:517-526, 2003.

Selective Inhibition of the Collagenolytic Activity of Human Cathepsin K by Altering its S2 Subsite Specificity.
Lecaille, F., Choe, Y., Brandt, W., Li, Z., Charles, S., Craik, C.S., Brömme, D.
Biochemistry 41, 8447-8454, 2002.

Collagenase activity of cathepsin K requires chondroitin sulfate.
Li, Z., Hou, W.S., Escalante, C., Gelb, B.D., Brömme, D.
J. Biol. Chem. 277, 28669-28676, 2002.

Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium.
Hou WS, Li W, Keyszer, G., Weber, E., Levy, R., Klein, M.J., Gravallese, E.M, Goldring, S.R., Brömme, D.
Arthritis & Rheumatism 46, 663-674, 2002.

Human and Parasitic Papain-like Cysteine Proteases: Their Role in Physiology and Pathology. Lecaille, F., Kaleta, J., Brömme, D.
Chem Rev 102, 4459-4488, 2002.