Digestive proteases are synthesised and secreted by the pancreas as inactive zymogens whose activation occur in the duodenum. Activation of trypsin (PRSS1) within the pancreas before secretion is thought to be a major initiating factor in chronic pancreatitis. Chymotrypsin-C (CTRC) is a pancreatic serine protease that regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. CTRC regulates trypsinogen activation and stability by two opposing cleavage sites: it can cleave cationic trypsinogen either at Phe18-Asp19 in the activation peptide, leading to enhanced autoactivation or at Leu81-Glu82 within the Ca2+-binding loop, resulting in degradation (the latter not shown here) (Batra et al. 2013).