Cationic trypsin-1 (PRSS1)

Cationic trypsin-1 is a major digestive serine protease produced as the inactive precursor, cationic trypsinogen, by pancreatic acinar cells. Upon secretion into the small intestine, it is cleaved and activated to trypsin, which hydrolyzes peptide bonds with specificity for lysine and arginine residues, thereby facilitating protein digestion and activating other digestive enzymes. Mutations in the PRSS1 gene may lead to hereditary pancreatitis due to inappropriate trypsin activation in the pancreas. Cationic trypsin-1 is tightly regulated: it requires calcium binding for stability and is subject to inhibition by endogenous inhibitors and controlled degradation by other proteases. In humans, cationic trypsinogen undergoes unique post-translational modification (tyrosine-sulfation), which improves its autoactivation efficiency. Cationic trypsin-1 is not a routine drug target, but its genetic and functional status are relevant in pancreatic disease and clinical diagnostics.

Other names

Cationic trypsinogenTrypsin-1Protease, serine 1TRY1TRYP1Beta-trypsinTrypsinogen ATrypsinogen 1Trypsin-1 preproprotein

Serine protease inhibitors prevent catalytic activity by binding to the active site or forming complexes (e.g., trypsin–inhibitor complex).