Summary
Mitochondria play a major role in many apoptotic responses. They coordinate caspase activation through the release of cytochrome c and DIABLO/ Smac as a result of the outer mitochondrial membrane becoming permeable. The release of these proteins is controlled by Bd-2 family members. The mechanisms whereby Bd-2 family members control the permeability of the outer mitochondrial membrane are still unclear.
Apoptosis is an essential process required for the development and maintenance of tissue homeostasis. Increased apoptosis could contribute to neurodegenerative diseases. Central components of the death machinery include the Bd-2, apoptotic protease-activating factor-1 (Apaf-1) and caspase family members. The caspases are cysteine proteases that cleave key intracellular substrates, resulting in the morphological and biochemical changes associated with apoptosis. Recently, it was found that, in many apoptotic responses, caspase activation is coordinated by mitochondria.
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Terradillos, O., Roucou, X., Da Cruz, S., Sanchez, B., Martinou, JC. (2001). Bcl-2 Family Members and Permeabilization of the Outer Mitochondrial Membrane. In: Henderson, C.E., Green, D.R., Mariani, J., Christen, Y. (eds) Neuronal Death by Accident or by Design. Research and Perspectives in Neurosciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-04333-2_3
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DOI: https://doi.org/10.1007/978-3-662-04333-2_3
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