The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol.
Ca2+-Activated neutral protease (CANP), that consists of 80K and 30K subunits, is converted to a low-Ca2+-requiring form by autolysis in the presence of Ca2+. Phosphatidylinositol greatly reduces the Ca2+-requirement for the autolysis of native CANP. However, this effect was not observed for CANP with a trimmed 30K subunit lacking the NH2-terminal hydrophobic and glycine-rich region. This suggests that the NH2-terminal hydrophobic region of the 30K subunit is important for the interaction of CANP with the cell membrane and that the calcium sensitivity of CANP is increased at the cell membrane through the effect of phosphatidylinositol.
D000596:Amino Acids / Q000502:physiology; D000818:Animals; D001329:Autolysis; D002154:Calpain / Q000032:analysis*; D004789:Enzyme Activation / Q000187:drug effects*; D009132:Muscles / Q000201:enzymology; D010716:Phosphatidylinositols / Q000494:pharmacology*; D011817:Rabbits; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010716:Phosphatidylinositols; D002154:Calpain