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H2N-ANERADLIAYLKQATK-OH

The Cytochrome c is a small heme protein found loosely associated with the inner membrane of the mitochondrion. Cytochromes c from certain eukaryotes, including plants and fungi but not higher animals, contains methylated lysine residues at specific positions1.

Cytochrome c is a required cofactor for Apaf-1 function2. Overexpression of bcl-2, or its close family member bcl-Xl, blocks the release of cytochrome c from mitochondria, which otherwise occurs when cells are signaled to undergo apoptosis3.

Cytochrome c is absolutely required in in vitro system for the activation of caspase-3 and caspase-9. When cytochrome c was depleted from HeLa cell S-100 extracts by a monoclonal antibody, the ability to activate caspases was abolished4. t. When cytochrome c was depleted, caspase-9 failed to bind Apaf-1 even in the presence of dATP. The binding was restored when purified cytochrome c was added. These suggest that cytochrome c initiates apoptosis by inducing the formation of the Apaf-1/caspase-9 complex4.

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