Gastrointestinal proteases

Gastrointestinal proteases are a diverse group of enzymes responsible for the hydrolysis of dietary proteins into absorbable peptides and amino acids within the digestive tract. This group includes gastric enzymes like pepsin and pancreatic enzymes such as trypsin, chymotrypsin, elastase, and carboxypeptidases, as well as brush-border peptidases. Beyond their primary digestive role, these proteases act as signaling molecules by activating protease-activated receptors (PARs), which regulate intestinal permeability, inflammation, and visceral sensitivity. Dysregulation of proteolytic activity is a hallmark of several gastrointestinal disorders, including exocrine pancreatic insufficiency, inflammatory bowel disease (IBD), and irritable bowel syndrome (IBS). Therapeutically, these enzymes are targeted through replacement therapies (e.g., pancrelipase for pancreatic insufficiency) or through the use of inhibitors (e.g., camostat) to mitigate inflammation and pain. Additionally, exogenous proteases are being developed to detoxify gluten in patients with celiac disease.

Other names

Digestive proteasesIntestinal proteasesPancreatic proteasesGastric proteasesPeptidases

Hydrolysis of peptide bonds to facilitate protein digestion; activation of protease-activated receptors (PARs) to modulate intestinal signaling; degradation of immunogenic gluten peptides to prevent autoimmune responses.