Serine protease 57 (PRSS57)

Serine protease 57 (PRSS57), also known as neutrophil serine protease 4 (NSP4), is an arginine-specific serine protease encoded on chromosome 19. It is a member of the peptidase S1 family and shares the overall trypsin-fold, but possesses unique substrate-recognition features allowing cleavage after both standard and posttranslationally modified arginine (including methylarginine and citrulline). PRSS57 is synthesized during early granulocyte differentiation and stored in azurophil granules, then rapidly released upon neutrophil activation to participate in host defense against pathogens. Its maturation critically depends on cathepsin C. To date, its role is primarily in the innate immune response, with further research ongoing to clarify specific disease associations and potential as a therapeutic target[1][2][3][4][6][7].

Other names

NSP4Neutrophil serine protease 4PRSSL1UNQ782/PRO1599UNQ782Serine protease 1-like protein 1protease, serine 57PRSS57

No drugs with defined mechanism of action directly targeting PRSS57 in current literature[1][2][6]. General protease inhibitors may affect its activity, but none are clinically validated or specific.