trypsinogen
Sign in to saveTrypsinogen () is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the intestinal mucosa. Once activated, the trypsin can cleave more trypsinogen into trypsin, a process called autoactivation. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.
Research
3,135 papers- Immunoassay for trypsinogen-4.Analytical biochemistry · 2022
- Trypsinogen (PRSS1 and PRSS2) gene dosage correlates with pancreatitis risk across genetic and transgenic studies: a systematic review and re-analysis.Human genetics · 2022
- Pathologically relevant trypsinogen activation in pancreatitis.American journal of physiology. Gastrointestinal and liver physiology · 2026
- Trypsinogen mutations in pancreatic disorders.Endocrinology and metabolism clinics of North America · 2006
- Trypsinogen isoforms in the ferret pancreas.Scientific reports · 2018
via PubMed
~4 min read
Article
8 sectionsContents
- Function
- Activation of trypsinogen
- Safeguards against trypsinogen activation
- Serum trypsinogen
- Trypsinogen isoforms
- Diseases
- References
- External links
Trypsinogen () is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the intestinal mucosa. Once activated, the trypsin can cleave more trypsinogen into trypsin, a process called autoactivation. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.
==Function==