Protease, serine, 2 (trypsin 2) (PRSS2)

Protease, serine, 2 (trypsin 2), abbreviated as PRSS2, encodes **anionic trypsinogen**, an enzyme of the trypsin family of serine proteases[1][3][4]. It is secreted by the pancreas and activated in the small intestine, where it hydrolyzes peptide bonds following lysine or arginine residues, facilitating protein digestion[1][4]. PRSS2 displays self-limiting properties by undergoing autocatalytic degradation upon activation, which protects the pancreas from excessive autodigestive damage and mitigates pancreatitis risk[1]. The enzyme also activates other proteases, including pro-urokinase in ovarian tumors and matrix metalloproteinases, contributing to extracellular matrix degradation, tumor invasion, and metastasis[2][3]. In addition, PRSS2 plays a role in defensin precursor processing in the ileum[3]. Increased PRSS2 expression is a hallmark of certain cancers such as gastric, pancreatic, and colorectal carcinoma, where it is linked to cell proliferation, invasion, and poor prognosis, suggesting utility as a cancer biomarker[2].

Other names

PRSS2Trypsin-2TRY2TRYP2TRY8anionic trypsinogenserine protease 2trypsin IItrypsinogen 2protease serine 2 preproprotein

Protease inhibition (potential general strategy, but no clinical drugs specifically targeting PRSS2 are cited). Downregulation (gene silencing shown to suppress cancer cell growth and invasion[2]).