Transmembrane serine protease 9 (TMPRSS9)

Transmembrane serine protease 9 (TMPRSS9) is a membrane-bound type II serine polyprotease encoded by the TMPRSS9 gene. It is notable for its unique structure featuring multiple tandem serine protease domains, with two catalytically active and one catalytically inactive protease released upon cleavage. TMPRSS9 participates in proteolytic processes, including plasminogen activation and conversion of pro-urokinase-type plasminogen activator (uPA) to active uPA, thereby modulating fibrinolytic pathways. Expression is highest in tissues such as liver, pancreas, intestine, and testis, and in immune cell subsets. Functionally, TMPRSS9 has been implicated in cancer progression through enhancement of tumor cell invasiveness, particularly in pancreatic cancer, but its broader roles in normal physiology and disease remain only partially understood[2][4][7][8][9].

Other names

Transmembrane protease serine 9Serase-1Serase-2Serase-3Polyserase-1Polyserase-IPolyserine protease 1

Inhibition of serine protease activity (demonstrated for inhibitors such as aprotinin, α2-antiplasmin, plasminogen activator inhibitor 1 on splice variants such as Serase-1B)[4]