caspáz

Caspases are a family of cysteine-dependent aspartate-specific proteases, which play a crucial role in programmed cell death, also known as apoptosis. They are classified into two main categories: initiator caspases and executioner caspases. Initiator caspases, such as caspase-8, caspase-9, and caspase-10, are activated in response to various death signals and initiate the apoptotic cascade. Executioner caspases, like caspase-3, caspase-6, and caspase-7, are activated downstream of initiator caspases and directly execute cell death by cleaving various cellular substrates.

Caspases are typically inactive in the cytoplasm as zymogens, which are precursor proteins that require processing to become active. Activation of caspases occurs through a process called autocatalysis, where the active form of the caspase cleaves and activates the zymogen form. This activation cascade is tightly regulated to ensure that apoptosis occurs only when necessary.

Caspases are involved in various physiological and pathological processes, including immune response, tissue remodeling, and disease progression. Dysregulation of caspase activity has been linked to several diseases, such as cancer, neurodegenerative disorders, and inflammatory conditions. Therefore, understanding the mechanisms of caspase activation and regulation is of great importance in the field of biology and medicine.