9 Caspase 9 is one of a family of over a dozen caspases. Internal damage in the cell causes Bax to release the heterodimer of Apaf-1 and caspase 9. These aggregate in the cytosol. Caspase 9 cleaves and, in so doing, activates other caspases. The sequential activation of one caspase by another creates an expanding cascade of proteolytic activity, which leads to digestion of structural proteins in the cytoplasm degradation of chromosomal DNA and Death of the cell occurs.
Cytochrome c is found in the organelles of normal cells.
The cytochrome c interacts and binds to the protein Apaf-1 creating a complex that is now able to activate caspase. An activated capase leads to the fragmentation of DNA, and later the death of the cell. It shows apoptotic-stained cells that can be detected by light microscopy. Garland Publishing, 1999.