Final answer:
Cytochrome C leakage from the mitochondria into the cytoplasm can initiate apoptosis by forming a complex with adaptor proteins that activates procaspase into caspase, leading to the cell's auto-digestion.
Step-by-step explanation:
Damage to the mitochondrion and leakage of cytochrome C into the cytoplasm may cause apoptosis. When mitochondria are subjected to high stress levels or damage, the mitochondrial permeability transition pore can open. This allows substances that are normally contained within the mitochondria, such as cytochrome C, to be released into the cytoplasm. Once in the cytosol, cytochrome C can bind to adaptor proteins, which facilitates the formation of a complex that has a high affinity for procaspase. These complexes induce a conformational change in procaspase, activating it to caspase, an enzyme that initiates cell auto-digestion. This molecular cascade is an integral part of the process of apoptosis, ensuring that cells that are damaged, no longer needed, or pose a potential threat to the organism, are safely dismantled and removed.