Gasdermin D (N-terminal fragment) (GSDMD-N)

The N-terminal fragment of Gasdermin D (GSDMD-N) is generated after GSDMD is cleaved by inflammatory caspases (e.g., caspase-1, -4, -5, -11). GSDMD-N moves to the plasma membrane, where it oligomerizes to form large, non-selective transmembrane pores. This process leads to cell swelling, membrane rupture (pyroptosis), and the release of inflammatory cytokines such as IL-1β and IL-18[1][2][4][5][7]. GSDMD-N is central to both canonical and non-canonical pyroptosis pathways, linking microbial or danger detection to the execution of a highly inflammatory form of cell death. This mechanism is crucial in innate immune defense but contributes to pathologies such as septic shock, chronic inflammation, and tissue damage when dysregulated.

Other names

GSDMD-NGSDMD N-terminal fragmentGasdermin D N-terminal domain

Direct inhibition of pore formation (by blocking GSDMD-N membrane binding/polymerization); Prevention of GSDMD cleavage (by inhibiting upstream caspases)