The pancreas is the organ that secretes trypsin.
Trypsin is a crucial enzyme for protein digestion, but it isn't secreted in its active form. Instead, the pancreas releases an inactive precursor called trypsinogen. This prevents the enzyme from digesting the proteins within the pancreas itself.
Here's a breakdown of the process:
- Production: The pancreatic acinar cells synthesize and package trypsinogen into zymogen granules.
- Secretion: Upon stimulation (e.g., by hormones like cholecystokinin), the pancreas secretes trypsinogen into the pancreatic duct, which empties into the duodenum (the first part of the small intestine).
- Activation: In the duodenum, an enzyme called enteropeptidase (or enterokinase), which is produced by the duodenal mucosa, cleaves trypsinogen to form active trypsin.
- Function: Active trypsin then catalyzes the hydrolysis of peptide bonds, breaking down larger proteins into smaller peptides and amino acids, facilitating their absorption. Trypsin also activates other pancreatic proenzymes like chymotrypsinogen and procarboxypeptidase, further contributing to protein digestion.
Because trypsin is specifically produced by the pancreas, it serves as an important marker for pancreatic function. Measuring trypsin levels can help diagnose pancreatic disorders such as pancreatitis or cystic fibrosis.
