James B. McCarthy, Ph.D.

Professor
(612) 625-7454
mccar001@umn.edu   

Educational Background

Board Certification

Research Interests

Dr. McCarthy’s research focus is on elucidating active domains within extracellular matrix (ECM) components that can promote cellular adhesion and motility. The approach has included isolating larger proteolytic fragments of specific ECM components and evaluating these fragments for cell adhesion/motility promoting activity and for other biological properties. Active fragments are then used as a basis for generating synthetic peptides, with the major goal being to identify active structures within ECM components that have cell adhesion/motility-promoting activities. One purpose for generating these synthetic peptides is to use them as tools for the identification of cell-surface receptors important in the recognition of the extracellular matrix. Receptors currently identified using this approach include two main types: cell-surface proteoglycans and integrins. A central and basic question currently being addressed by Dr. McCarthy's group concerns how these two classes of cellular recognition receptors, as well as others, may work in concert to modulate the adhesive phenotype of both normal and transformed cell types. Coincident with this line of research are efforts to elucidate potential signal transduction mechanisms that are involved in cellular recognition, adhesion, and motility.

These synthetic peptides potentially have several additional uses, including therapeutic applications in controlling tumor invasion and metastasis, control of inflammatory or immune responses, nerve regeneration, or conditioning of various biomaterials to improve their performance. Ongoing collaborations with investigators in the Biomedical Engineering Center and elsewhere are designed to explore these and other potential applications of synthetic peptide technology.

Recent Publications

• Reiland, J., L.T. Furcht and J.B. McCarthy. 1999. CXC-chemokines stimulate invasion and chemotaxis in prostate carcinoma cells through the CXCR2 receptor.  The Prostate. 41:78-88.

• Eisenmann, K.M., J.B. McCarthy, M.A. Simpson, P.J. Keely, J-L. Guan, K. Tachibana, L. Furcht and J. Iida. 1999. Melanoma chondroitin sulfate proteoglycan signaling through cdc42, Ack-1 and p130cas regulates integrin-mediated cell spreading.  Nature Cell Biology. 1:507-513.

• Iida, J.,Pei, D.,Kang, T.,Simpson, M. A.,Herlyn, M., Furcht, L. T., McCarthy, J. B.. 2001. Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen.  J Biol Chem. 276:18786-94.

• Simpson, M. A., Reiland, J., Burger, S. R., Furcht, L. T., Spicer, A. P., Oegema, T. R., Jr., McCarthy, J. B. 2001. Hyaluronan synthase elevation in metastatic prostate carcinoma cells correlates with hyaluronan surface retention, a prerequisite for rapid adhesion to bone marrow endothelial cells.  J Biol Chem. 276:17949-57.