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.
CITATION STYLE
Zhao, Y., Shi, J., & Shao, F. (2018). Inflammatory caspases: Activation and cleavage of Gasdermin-D in vitro and during pyroptosis. In Methods in Molecular Biology (Vol. 1714, pp. 131–148). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7519-8_9
Mendeley helps you to discover research relevant for your work.