Transmembrane serine protease 11E (TMPRSS11E)

Transmembrane serine protease 11E (TMPRSS11E) is a type II transmembrane serine protease with endopeptidase activity, showing a preference for cleaving substrates with an arginine residue at P1. It is expressed on epithelial surfaces of several tissues, including the lung, where it is upregulated during injury or inflammation. TMPRSS11E can cleave and activate proteinase-activated receptor 1 (PAR-1), leading to increased secretion of pro-inflammatory cytokines such as IL-1β, IL-6, and TNF-α, thereby potentiating lung inflammation. It has also been shown to sensitize tumor cells to apoptosis through the epidermal growth factor receptor (EGFR) pathway and has a role in facilitating viral entry into cells for certain respiratory viruses. TMPRSS11E is implicated in pathology including acute respiratory distress syndrome, pneumonia, and various cancers, most notably squamous cell carcinoma. Pharmacological inhibition (e.g., camostat) or genetic silencing of TMPRSS11E reduces inflammation and lung injury in preclinical models, supporting its potential as a therapeutic target[1][2][3][6][8][9][10].

Other names

DESC1TM11ETMPRSS11E2

Proteolytic cleavage of substrates including PAR-1, contributing to cytokine release and inflammation; Sensitization of tumor cells to apoptosis via EGFR cleavage; Facilitation of some viral entry pathways