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M-calpain is a calcium-dependent cysteine protease involved in various cellular processes, including cytoskeleton remodeling, signal transduction, and apoptosis. It is a heterodimer composed of a large catalytic subunit (CAPN2) and a small regulatory subunit (CAPNS1). Activation of m-calpain requires calcium binding, which induces a conformational change that enables proteolytic activity. This enzyme plays a crucial role in both physiological and pathological conditions, making it a potential therapeutic target for diseases related to its dysregulation.
Drugs inhibit calpain by blocking the active site or altering calcium binding, which is essential for its activation.
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