Inactivation of pancreatic digestive proteases by deconjugated bilirubin from the liver: A critical mechanism for gut protection

Each day, a large amount of different kinds of digestive enzymes are produced by the pancreas and discharged into the gut to digest the food [1, 2]. Among these enzymes, those such as amylase are made in the pancreas as the active form. However, digestive enzymes such as trypsin and chymotrypsin are initially created in pancreas in the form of non-active zymogens as trypsinogen and chymotrypsinogen, which are only activated in the lumen of gut where the digestion of food occurred. This would have reflected the high potential of self-damage they may strike, as the protein of the body are just the same by nature as those from the meat or egg. However, up to date, the exact profound mechanism as how the gut is protected from the damage by these pancreatic digestive proteases remained poorly investigated and noticed. Here I address that inactivation of digestive proteases by the deconjugated bilirubin would have played a critical role.