半胱天冬酶-1 激活的复杂生物物理难题。
The intricate biophysical puzzle of caspase-1 activation.
机构信息
Department of Chemistry & Biochemistry, University of Missouri-St. Louis, St. Louis, MO, USA.
Department of Chemistry & Biochemistry, University of Missouri-St. Louis, St. Louis, MO, USA.
出版信息
Arch Biochem Biophys. 2021 Mar 15;699:108753. doi: 10.1016/j.abb.2021.108753. Epub 2021 Jan 13.
This review takes a closer look at the structural components of the molecules involved in the processes leading to caspase-1 activation. Interleukins 1β and 18 (IL-1β, IL-18) are well-known proinflammatory cytokines that are produced following cleavage of their respective precursor proteins by the cysteine protease caspase-1. Active caspase-1 is the final step of the NLRP3 inflammasome, a three-protein intracellular complex involved in inflammation and induction of pyroptosis (a proinflammatory cell-death process). NLRP3 activators facilitate assembly of the inflammasome complex and subsequent activation of caspase-1 by autoproteolysis. However, the definitive structural components of active caspase-1 are still unclear and new data add to the complexity of this process. This review outlines the historical and recent findings that provide supporting evidence for the structural aspects of caspase-1 autoproteolysis and activation.
这篇综述深入探讨了参与 caspase-1 激活过程的分子的结构组成。白细胞介素 1β 和 18（IL-1β、IL-18）是众所周知的前炎性细胞因子，在它们各自的前体蛋白被半胱氨酸蛋白酶 caspase-1 切割后产生。活性 caspase-1 是 NLRP3 炎性小体的最后一步，NLRP3 炎性小体是一种涉及炎症和诱导细胞焦亡（一种促炎细胞死亡过程）的三蛋白细胞内复合物。NLRP3 激活剂促进炎性小体复合物的组装，并随后通过自切割激活 caspase-1。然而，活性 caspase-1 的明确结构组成仍不清楚，新的数据增加了这一过程的复杂性。本综述概述了提供 caspase-1 自切割和激活的结构方面的支持证据的历史和最新发现。
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