Calcium Activated Neutral Protease (CANP), also known as calpain, is a class of cellular enzymes that are involved in various physiological processes. It is a calcium-dependent protease, meaning that its activity is regulated by the presence of calcium ions. CANPs play a critical role in the breakdown and remodeling of cellular components, such as cytoskeletal proteins, during processes like cell migration, differentiation, and apoptosis.
CANPs belong to the family of cysteine proteases and are characterized by a neutral pH optimum for their enzymatic activity. They are found in nearly all mammalian tissues, with different isoforms and subunits expressed in specific cell types and organelles. The activation of CANPs occurs through the binding of calcium ions, which induces conformational changes, making the enzyme active and capable of cleaving specific target proteins.
The functions of CANPs are diverse and include regulating various cellular processes, such as synaptic plasticity, blood clotting, muscle contraction, and inflammation. They are also involved in the degradation of damaged or misfolded proteins, contributing to protein quality control mechanisms within cells.
Abnormal regulation of CANPs has been implicated in several human diseases, including neurodegenerative disorders, cardiovascular diseases, and cancer. Excessive activation of CANPs can lead to uncontrolled proteolysis, resulting in cellular damage and tissue dysfunction.
Overall, Calcium Activated Neutral Proteases are a group of enzymes that play crucial roles in cellular processes by regulating protein degradation and remodeling. Their activity is dependent on the presence of calcium ions, and dysregulation of CANPs has significant implications for human health.
