Serine protease 1 (Trypsin-1) (PRSS1)

Human trypsin-1, also known as cationic trypsinogen and encoded by the PRSS1 gene, is the most abundant isoform of trypsinogen produced by the pancreatic acinar cells [1, 10]. It is secreted into the duodenum as an inactive zymogen and subsequently activated by enteropeptidase, where it plays a central role in digestion by cleaving proteins at lysine and arginine residues [2, 12]. Beyond its direct digestive function, trypsin-1 is responsible for the proteolytic activation of other pancreatic zymogens, including chymotrypsinogen and procarboxypeptidases [2, 11]. Mutations in the PRSS1 gene, particularly gain-of-function variants like R122H, are strongly associated with hereditary pancreatitis due to premature activation of the enzyme within the pancreas, leading to autodigestion and chronic inflammation [3, 12]. Consequently, trypsin-1 is a significant therapeutic target; serine protease inhibitors such as camostat and nafamostat are employed to mitigate its activity in inflammatory pancreatic conditions [5, 13]. Additionally, its involvement in activating protease-activated receptors (PARs) suggests a broader role in signaling pathways related to cancer progression and pain [15, 17]. The enzyme's activity is naturally regulated by inhibitors like SPINK1, and imbalances in this protease-antiprotease system are central to pancreatic pathology [4, 14]. Monitoring trypsin-1 levels or its activation peptides serves as a critical biomarker for diagnosing pancreatic disorders and assessing disease severity [17, 18].

Other names

Cationic trypsinogenTrypsinogen 1TRY1TRP1TRYP1Protease, serine 1Beta-trypsin

Serine protease inhibition