Efektorikaspaseet

Efektorikaspaseet, also known as effector caspases, are a crucial family of proteases involved in programmed cell death, or apoptosis. These enzymes play a central role in executing the cellular dismantling process once a cell receives an apoptotic signal. Unlike initiator caspases, which are activated by upstream signaling pathways, effector caspases are directly responsible for cleaving a wide range of cellular substrates. This cleavage leads to the characteristic morphological and biochemical changes associated with apoptosis, such as DNA fragmentation, membrane blebbing, and the formation of apoptotic bodies.

The primary effector caspases in mammals are caspase-3, caspase-6, and caspase-7. These proteases are synthesized as inactive proenzymes and are activated through proteolytic cleavage, typically by initiator caspases like caspase-8 or caspase-9. Once activated, effector caspases cleave numerous cellular proteins, including structural components like lamins and cytoskeletal proteins, as well as DNA repair enzymes and regulatory proteins. This widespread proteolytic activity ensures the rapid and efficient elimination of the damaged or unwanted cell. The precise substrates and functions of each effector caspase can vary, contributing to the finely tuned regulation of apoptosis.