Trypsin (Pancreatic serine protease) (PRSS)

Luminal trypsin and related trypsin-like serine proteases are a group of enzymes, primarily PRSS1 and PRSS2, synthesized in the pancreas and secreted into the intestinal lumen to catalyze the hydrolysis of dietary proteins [1][2]. In addition to their digestive functions, these proteases serve as potent signaling molecules by cleaving the N-terminal extracellular domain of Protease-Activated Receptor 2 (PAR2), triggering intracellular signaling pathways involved in inflammation and pain [3][5]. Dysregulation or excessive activity of these luminal proteases is strongly associated with the pathogenesis of irritable bowel syndrome (IBS) and inflammatory bowel disease (IBD), where they contribute to increased intestinal permeability and visceral hypersensitivity [3][5]. Therapeutic strategies targeting these enzymes utilize serine protease inhibitors, such as camostat mesylate and nafamostat, to block their catalytic activity and mitigate PAR2-driven symptoms [4][6]. Furthermore, premature activation of these proteases within the pancreatic parenchyma is a hallmark of acute pancreatitis, leading to autodigestion and tissue damage [7]. Monitoring fecal serine protease activity has emerged as a potential biomarker for assessing disease severity in gastrointestinal disorders [3].

Other names

Luminal trypsinTrypsin-like serine proteasesCationic trypsinogenAnionic trypsinogenMesotrypsinPRSS1PRSS2PRSS3Digestive serine proteases

Inhibition of the catalytic serine residue within the active site of the protease, preventing the cleavage of substrate proteins and the activation of protease-activated receptors.