caspázy

Caspases are a family of cysteine proteases that play a critical role in programmed cell death, also known as apoptosis. These enzymes are activated by specific upstream signals and then execute the process by cleaving a wide range of cellular substrates. The name "caspase" is derived from the fact that they are cysteine-dependent aspartate-directed proteases, meaning they utilize a cysteine residue in their active site and cleave proteins after aspartate residues.

There are two main functional groups of caspases: initiator caspases and effector caspases. Initiator caspases, such as caspase-8 and caspase-9, are activated by death signals and in turn activate effector caspases. Effector caspases, including caspase-3 and caspase-7, are responsible for dismantling the cell by cleaving key cellular proteins involved in maintaining cell structure and function. This cleavage leads to the characteristic morphological changes of apoptosis, such as cell shrinkage, DNA fragmentation, and the formation of apoptotic bodies.

The precise regulation of caspase activity is crucial for normal development and tissue homeostasis. Dysregulation of caspases can contribute to various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Inhibitors of caspases are being investigated as potential therapeutic agents for conditions where excessive cell death is detrimental.