The inactive form of this proteinase, denoted pro-ADAM10, was activated upon Ca2+ influx by reducing the Ca2+/CaM-pro-ADAM10 interaction, and the activated proteinase subsequently induced the cleavage of the adhesion molecules CD44 and L1CAM (cell adhesion molecule L1) [123], disrupting the cell–cell interaction, detaching cells from the extracellular matrix, and thus enhancing the invasiveness of the tumor cells. Here, ADAM10 is linked to neoplasm.