炎症体
上睑下垂
半胱氨酸蛋白酶
胞浆
化学
程序性细胞死亡
半胱氨酸蛋白酶1
细胞生物学
体外
细胞凋亡
劈理(地质)
生物
生物化学
酶
古生物学
受体
断裂(地质)
作者
Yue Zhao,Jianjin Shi,Feng Shao
出处
期刊:Methods in molecular biology
日期:2017-11-25
卷期号:: 131-148
被引量:52
标识
DOI:10.1007/978-1-4939-7519-8_9
摘要
Gasdermin-D (also known as GSDMD), the newly identified executioner of pyroptotic cell death, is cleaved by activated caspase-1 downstream of canonical inflammasome activation or caspase-4, 5, and 11 upon their ligation and activation by cytosolic LPS. Upon a single cleavage between the two domains in Gasdermin-D, the N-terminal domain binds to membrane lipids and lyses cells by forming pores of an inner diameter of 10–14 nm within the membrane. The inter-domain cleavage of Gasdermin-D is a reliable marker for the activation of inflammatory caspases and cell pyroptosis. Here, we describe the methods for examining Gasdermin-D cleavage by activated inflammatory caspases in vitro and upon inflammasome activation in vivo.
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