Our research is focused towards elucidating the physiological and pathophysiological role of Endo180.

We have undertaken an extensive characterization of the recycling endocytic glycoprotein, Endo180 (also known as CD280 and uPARAP). Interest in this receptor has stemmed from the demonstration that (a) it is a novel collagen binding/internalization receptor, (b) it forms a trimolecular complex on the cell surface with urokinase plasminogen activator (uPA) and the uPA receptor (uPAR) receptor and is required for uPA-mediated chemotaxis, and (c) it is pro-migratory in that downregulation of Endo180 impairs cell migration while ectopic expression results in enhanced cell migration.

Currently our research is focused towards elucidating the physiological and pathophysiological role of Endo180. In particular, to investigate its function in extracellular matrix remodeling both in vitro and in vivo, and to determining the molecular mechanisms underlying Endo180 mediated cell migration. These two aspects of the project are interrelated, given the importance of matrix remodeling and the acquisition of an enhanced migratory phenotype in the invasive spread of cancer.