Inflammatory Caspases: Activation and Cleavage of Gasdermin-D In Vitro and During Pyroptosis
- PMID: 29177860
- DOI: 10.1007/978-1-4939-7519-8_9
Inflammatory Caspases: Activation and Cleavage of Gasdermin-D In Vitro and During Pyroptosis
Abstract
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.
Keywords: GSDMD; Gasdermin-D; Inflammasome; Inflammatory caspases; LPS; Pyroptosis; Recombinant proteins.
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