kaspázy9

Kaspázy 9, also known as CASP9, is a protein-coding gene that plays a crucial role in programmed cell death, or apoptosis. It belongs to the cysteine-aspartic protease (caspase) family, a group of enzymes essential for executing the apoptotic cascade. Kaspázy 9 is classified as an initiator caspase, meaning it is activated early in the apoptotic pathway and subsequently activates downstream effector caspases. Its activation is primarily triggered by the release of cytochrome c from the mitochondria into the cytoplasm, a process that occurs during intrinsic apoptosis. Upon release, cytochrome c binds to Apaf-1, forming a large protein complex called the apoptosome. Kaspázy 9 is recruited to the apoptosome, where it undergoes auto-catalytic cleavage and activation. Once activated, kaspázy 9 cleaves and activates effector caspases, such as kaspázy 3 and kaspázy 7, which then dismantle cellular components, leading to cell death. Mutations or dysregulation of kaspázy 9 have been implicated in various diseases, including cancer and neurodegenerative disorders, highlighting its critical importance in maintaining cellular homeostasis.