Caspase-3/Sandbox: Difference between revisions
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Caspases are cysteine aspartic acid proteases that are crucial for the initiation (e.g. caspase-8, -9, -10) and execution (e.g. caspase-3, -6, -7) of apoptosis (Degterev, Boyce et al. 2003) through cleavage of death substrates, such as the BH3 domain-only protein BID by caspase-8 (Li, Zhu et al. 1998) and inhibitor of caspase-activated deoxyribonuclease (ICAD) by caspase-3 (Enari, Sakahira et al. 1998; Sakahira, Enari et al. 1998). It has become appreciated more recently that caspase activity, specifically caspase-8, is also required for T cell growth (Alam, Cohen et al. 1999; Kennedy, Kataoka et al. 1999; Misra, Jelley-Gibbs et al. 2005), and that the location and level of active caspases within cells may be a key determinant of survival or death (Misra, Russell et al. 2007; Koenig, Russell et al. 2008). We have previously observed that murine αβ T cells bearing high levels of caspase activity manifest increased rates of both cell growth and cell death (Dohrman, Russell et al. 2005). | |||
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==Structure & Function== | ==Structure & Function== | ||
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==References & Notes== | ==References & Notes== | ||
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Dohrman, A., J. Q. Russell, et al. (2005). "Cellular FLIP long form augments caspase activity and death of T cells through heterodimerization with and activation of caspase-8." J Immunol 175(1): 311-8. | |||
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