Caspases are a family of proteolytic enzymes that play a crucial role in cellular processes such as apoptosis, also known as programmed cell death. They are divided into two main groups based on their structure and function: initiator caspases (such as caspase-8) which activate the executioner caspases (like caspase-3), and executioner caspases themselves, which carry out the actual process of cellular dismantling. Caspases are synthesized as inactive precursors called procaspases, which are activated through proteolytic cleavage by other enzymes or under certain conditions within the cell. The activation and subsequent action of caspases ultimately lead to the characteristic morphological and biochemical changes associated with apoptosis, including DNA fragmentation, membrane blebbing, and plasma membrane rupture.