caspaseproteaasien

Caspase proteases, often shortened to caspases, are a family of cysteine-aspartic proteases that play a crucial role in programmed cell death, also known as apoptosis. These enzymes are synthesized as inactive pro-caspases and are activated through proteolytic cleavage. Once activated, caspases function as a cascade, with initiator caspases triggering the activation of effector caspases. Effector caspases then dismantle cellular components by cleaving specific protein substrates within the cell, leading to the characteristic morphological changes of apoptosis. There are both initiator and effector caspases, with distinct roles in initiating and executing the apoptotic process. Caspases are essential for normal development, tissue homeostasis, and eliminating damaged or infected cells. Dysregulation of caspase activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Inhibitors of caspases are being explored as potential therapeutic agents for conditions where excessive cell death is detrimental. Conversely, activators of caspases are being investigated for their potential in treating cancer by promoting tumor cell elimination.