Gasdermin A (GSDMA)

Gasdermin A (GSDMA) is a member of the gasdermin family, a group of structurally related pore-forming proteins involved in regulated cell death known as pyroptosis[1]. GSDMA consists of a repressive C-terminal domain and a cytotoxic N-terminal domain; when the linker between these domains is cleaved by specific proteases (such as inflammatory caspases or granzymes), the N-terminal is released, oligomerizes, and forms large pores in cell membranes[1]. This results in membrane permeabilization and cell death by pyroptosis, an inflammatory form of programmed cell death[1]. Gasdermin A is expressed in epithelial tissues and is involved in physiological and pathological processes including cell differentiation, inflammation, coagulation, and cancer, with emerging evidence suggesting a role as a tumor suppressor[1]. While GSDMD is the best studied gasdermin, GSDMA shares similar structural and mechanistic features within the family, and current research is exploring its utility as a therapeutic target in inflammatory diseases and cancer[1]. No clinically approved drugs directly target GSDMA at present.

Other names

Gasdermin-AGSDMAGasdermin-1GSDMGSDM1FKSG9GSDMA-NTGSDMA-CTFLJ39120

Not established for marketed drugs; experimentally, drugs or molecules that modify gasdermin cleavage or activation could modulate pore formation and pyroptosis