Sara Courtneidge, Ph.D.
Professor and Program Director, Tumor Microenvironment
The spread of cancer cells from the original tumor site to other organs, known as metastasis, is the leading cause of cancer death. To metastasize, cells must acquire a number of properties, including the ability to move, survive in the bloodstream, cross tissue boundaries and grow in a foreign organ. These last two properties require the activity of proteases, which are enzymes that break up other proteins.
The Courtneidge laboratory studies how the activity of these proteases is controlled by cell surface structures called invadopodia. These finger-like projections from the cell membrane are found in metastatic cancer cells but not in non-invasive cells. Dr. Courtneidge’s laboratory discovered a protein, called Tks5, which controls the formation of these invadopodia in cancer cells. Reducing the expression of Tks5 in cancer cells also inhibited metastatic tumor growth in animal models. These promising results suggest that inhibiting invadopodia formation might be a good approach to controlling metastatic disease.
Cells with invadopodia
In collaboration with Dr. Jeff Price and scientists in the Conrad Prebys Center for Chemical Genomics, Dr. Courtneidge has initiated efforts to identify inhibitors of invadopodia formation. To date, several promising chemicals have been identified. In addition, some novel kinases have been discovered to control invadopodia formation. This is important because these enzymes can be successfully inhibited by small molecules. Indeed, several kinase inhibitors, such as sunitinib and lapatinib, have been approved as cancer therapeutics in recent years. The goal of this research is to identify chemicals that will form the starting point for further pharmaceutical development and ultimately clinical testing.