Stennicke H R, Salvesen G S
Program for Apoptosis and Cell Death, Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Biochim Biophys Acta. 1998 Sep 8;1387(1-2):17-31. doi: 10.1016/s0167-4838(98)00133-2.
Caspases comprise a structurally related group of cysteine proteases that share a dominant primary specificity for cleaving peptide bonds following Asp residues. Present in the cytosol of all animals, the caspases participate in proteolytic pathways required for executing programmed cell death, or apoptosis. In mammals the caspases have also evolved a function in activating proinflammatory cytokines. We review the current knowledge of the substrate specificity, structure, and activation mechanisms of human caspases and relate these findings to their fundamental biologic role.
半胱天冬酶是一组结构相关的半胱氨酸蛋白酶，它们对天冬氨酸残基之后的肽键具有主要的切割特异性。半胱天冬酶存在于所有动物的细胞质中，参与执行程序性细胞死亡或凋亡所需的蛋白水解途径。在哺乳动物中，半胱天冬酶还进化出了激活促炎细胞因子的功能。我们综述了目前关于人类半胱天冬酶的底物特异性、结构和激活机制的知识，并将这些发现与其基本生物学作用联系起来。
