Calcium-Activated Neutral Protease (CANP) and its Biological and Medical Implications

Calcium activated neutral protease (CANP) apparently participates in a variety of cellular functions mediated by Ca2 +. The primary, structure of CANP reveals a novel domain structure comprising domains highly homologous to papain-like cysteine proteinases and calmodulin-like Ca2+ binding proteins, and a glycine-rich hydrophobic domain that interacts with the cell membrane and phospholipid. This finding provides new insight into the protease action, activity-regulation, biological and pathological function and molecular evolution of CANP. The primary structure and gene structure of CANP are described together with discussions on CANP from the above viewpoints.