School of Medicine

Wayne State University School of Medicine


Rafael A. Fridman, Ph.D.
Leader of Proteases and Cancer Program of the Barbara Ann Karmanos Cancer Institute
Department of Pathology
540 E. Canfield Ave, Room 8200
Detroit, MI 48201
Matrix metalloproteinases, proteases, protease inhibitors, prostate cancer, and bone metastasis
Administrative Contact
Brenda Batts
Research Interests

The research program in Dr. Fridmanís laboratory is focused on understanding the role of pericellular proteolysis in pathological conditions.  Specifically, the focus is on the regulation and function of matrix metalloproteinases (MMPs), a family of zinc-dependent endopeptidases known to be major mediators of pericellular proteolysis.  Specifically, Dr. Fridman and colleagues investigate the function and regulation of membrane-anchored MMPs (MT-MMPs) including the transmembrane MMPs such as MT1-MMP and MT3-MMP and the GPI-anchored MMPs, MT6- and MT4-MMP.  Studies are aimed at defining the expression and role of MT-MMPs in cancer progression with emphasis in prostate and breast cancer and the development of bone metastasis.  Approaches include studies on protease expression, trafficking, activation, and inhibition in cellular systems and in mouse models of cancer.  Dr. Fridmanís group is also conducting studies to identify new and selective mechanism-based inhibitors for MT-MMPs for inhibition of tumor growth and metastasis.  


Ph.D. (1986): Hebrew University, Jerusalem, Israel

Postdoctoral Fellowship
1987-1990: National Institutes of Health, Bethesda, MD, USA, in the field of Tumor Biology


1. Toth M, Hernandez-Barrantes S, Osenkowski P, Bernardo MM, Gervasi DC, Shimura Y, Meroueh O, Kotra LP, Galvez BG, Arroyo AG, Mobashery S, and Fridman R, 2002, Complex pattern of membrane type 1-matrix metalloproteinase shedding regulation by autocatalytic cell surface inactivation of active enzyme, J Biol Chem, 277: 26340-50.
2. Kruger A, Arlt M, Gerg M, Bernardo MM, Kopitz C, Chang M, Mobashery S and Fridman R, 2005, Antimetastatic activity of a novel mechanism-based gelatinase inhibitor,  Cancer Res, 65: 3523-6.
3. Sun Q, Weber CR, Sohail A, Bernardo MM, Toth M, Zhao H, Turner JR, and Fridman R, 2007, MT6-MMP is highly expressed in human colon cancer, promotes tumor growth and exhibits unique biochemical properties, J Biol Chem, 282: 21998-2010.
4. Cho J-A, Osenkowski P, Zhao H, Kim S, Toth M, Cole K, Aboukameel A,  Saliganan A, Schuger L, Bonfil  RD,  and Fridman R, 2008, The inactive 44-kDa processed form of MT1-MMP enhances proteolytic activity via regulation of endocytosis of active MT1-MMP,  J Biol Chem, 283: 17391-405.
5. Sohail A, Sun Q, Zhao H, Bernardo MM, Cho J-A and Fridman R, 2008, MT4-(MMP17) and MT6-MMP (MMP25), a unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer,  Cancer Met Rev, 27: 289-302.