We now know that ced 3 is the prototype of a family

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Unformatted text preview: w know that Ced-3 is the prototype of a family of more than a dozen proteases, known as caspases because they have cysteine (C) residues at their active sites and cleave after aspartic acid (Asp) residues in their substrate proteins. The caspases are the ultimate effectors or executioners of programmed cell death, bringing about the events of apoptosis by cleaving more than 100 different cell target proteins (Figure 17.4). One key target of the caspases is an inhibitor of a DNase, which when activated is responsible for fragmentation of nuclear DNA. In addition, caspases cleave nuclear lamins, leading to fragmentation of the nucleus; cytoskeletal proteins, leading to disruption of the cytoskeleton, membrane blebbing, and cell fragmentation; and Golgi matrix proteins, leading to fragmentation of the Golgi apparatus. The translocation of phosphatidylserine to the cell surface is also dependent on caspases, although the caspase target(s) responsible for this plasma membrane alteration have not yet been identified. Apopt...
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This note was uploaded on 08/25/2009 for the course BIO 315 taught by Professor Steiner during the Spring '08 term at Kentucky.

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