Effects of fibronectin cleaved by neuropsin on cell adhesion and migration

Neuropsin is a serine protease cloned from the mouse hippocampus. Since neuropsin is a secreted protein which effectively cleaves fibronectin, it may affect cell adhesion or cell migration by modulating the content and/or chemical characteriscs of fibronectin in extracellular matrix (ECM). In adhesion assays, alpha5B2 cells expressing integrin alpha5beta1 bound less effectively to fibronectin teated with neuropsin than intact fibronectin. In Boyden chamber chemotaxis assays, the fibronectin-induced migration of alpha5B2 cells was not affected by neuropsin treatment. These findings suggest that neuropsin regulates the local microenvironment by modulating the interaction between cells and fibronectin in ECM.