Calpain-2 (None)

Calpain-2, also known as m-calpain or calcium-activated neutral protease II, is a large catalytic subunit of the calpain family—calcium-dependent, non-lysosomal cysteine proteases found in most mammalian tissues[1][6]. It typically exists as a heterodimer with the common small regulatory subunit (CAPNS1/CAPN4). Calpain-2 requires higher calcium concentrations for activation than its close paralog calpain-1 and is involved in the limited proteolysis of key structural and regulatory proteins. Its critical functions include modulation of the cytoskeleton for cell migration, cell signal transduction, apoptosis, and cell cycle events[1][3][6]. Dysregulated calpain-2 activity is implicated in various pathologies, including cancer, neurodegenerative, cardiovascular, and inflammatory diseases. While calpain inhibitors have shown preclinical efficacy as therapeutic agents, drug development is complicated by the enzyme family's ubiquitous expression, structural similarity among isoforms, and essential roles in normal physiology[4][6].

Other names

m-calpaincalpain IIcalcium-activated neutral protease IICANP2

Inhibition of protease activity (for inhibitors: block the catalytic cysteine in the active site) Reduction of substrate cleavage and downstream cellular effects