By Andréa C. LeBlanc
McGill Univ., Montreal, Canada. deals state-of-the-art protocols to enquire apoptosis in neurons, ways to discover key proteins fascinated by neuronal apoptosis, innovations to review synaptosis and realize proapoptotic proteins in situ, and notes at the pitfalls and merits of every strategy.
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Extra info for Apoptosis Techniques and Protocols
Exhaustive lists of caspase substrates have been presented elsewhere (19); Table 2 describes a functional classification of substrate cleavage. The involvement of caspases in apoptosis is a three-step process. Caspases first cleave substrates that further amplify the apoptotic signal. Caspases then dismantle proteins that ensure cell function and survival. Finally, they activate the effectors of the apoptotic phenotype, that is, enzymes that will package the dead cell for phagocytosis (Table 2 and references therein).
USA 94, 3668–3672. 19. -T. and Youle, R. Y. (1998) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 273, 10,777–10,783. 20. , Wei, M. , and Korsmeyer, S. J. (1998) Enforced dimerization of Bax results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17, 3878–3885. 21. Wolter, K. , Smith, C. , and Youle, R. J. (1997) Movement of Bax from the cytosol to mitochondria during apoptosis. J. Cell Biol. 139, 1281–1292.
Caspases Caspases are a unique family of cysteinyl aspartate proteases that display an absolute requirement for aspartate for proteolytic activity (3). To date, 14 mammalian caspases have been identified, 11 of which are found in humans (Table 1). Recently, caspase homologs lacking caspase protease activity have been identified in humans, Caenorhabditis elegans and Dictyostelium discoideum (the paracaspases), and in Arabidopsis thaliana (the metacaspases) (4). Caspases share homology at the amino acid and at the structural level.