Chymotrypsin C (CTRC)

Chymotrypsin C (CTRC) is a critical pancreatic serine protease enzyme in the peptidase S1 family that serves as a central regulator of trypsinogen activation and degradation[1][3]. It acts to protect the pancreas from autodigestion and pancreatitis by selectively cleaving key regulatory bonds in trypsinogen and degrading prematurely activated trypsin, thus curtailing excessive protease activity[1][2]. CTRC’s activity is modulated by local calcium concentrations, and variants or mutations that reduce its secretion or function are significant genetic risk factors for chronic pancreatitis, affecting enzymatic activation, stability, or secretion[1][2]. The gene encoding CTRC also produces a serum calcium-decreasing factor, and some loss-of-function mutations can also elicit endoplasmic reticulum stress responses in pancreatic cells[2]. No approved small-molecule drugs directly target CTRC, and no standard biomarkers are in clinical use except for genetic testing of CTRC variants as a risk factor for pancreatitis[2][1].

Other names

Chymotrypsinogen CCaldecrinCLCRELA4Elastase 4Elastase IVSerum calcium-decreasing factorChymotrypsin-CChymotrypsin C (caldecrin)