What is trypsinogen activation peptide?

Trypsinogen activation peptide (TAP) is the amino-terminus peptide released by the activation of trypsinogen. In experimental acute pancreatitis, the inappropriate activation of trypsinogen within the pancreas results in the release of TAP into the blood, urine, and peritoneum[10,11].

Is trypsinogen involved in peptide cleavage?

Since trypsin also cleaves the peptide bond after an arginine or a lysine, it can cleave other trypsinogen, and the activation process therefore becomes autocatalytic.

What stimulates trypsinogen release?

enzyme enteropeptidase
(f) Zymogens are activated physiologically only after they enter the duodenum, where the brush-border enzyme enteropeptidase activates trypsinogen, and trypsin then activates other pancreatic zymogens. As with gastric secretion, pancreatic secretion is stimulated during cephalic, gastric, and intestinal phases.

How is trypsinogen activated?

Trypsinogen is activated by enterokinase, which cleaves an amino-terminal activation peptide (TAP). Active trypsin then cleaves and activates all of the other pancreatic proteases, a phospholipase, and colipase, which is necessary for the physiological action of pancreatic triglyceride lipase.

Where does trypsinogen activation peptide ( TAP ) come from?

Trypsinogen activation peptide (TAP) is a cleavage product of trypsinogen which is released into systemic circulation with zymogen granule activation. Because of its low molecular weight, TAP is rapidly excreted in urine and is easily detected in both urine and serum.

How does trypsinogen play a role in pancreatitis?

However, activation of trypsinogen within the acinar cell plays a key role in the pathogenesis of acute pancreatitis, because conversion of trypsinogen triggers a pancreatic enzyme cascade that activates the remaining zymogens, resulting in autodigestion of the surrounding tissue (Rinderknecht, 1986).

How is trypsinogen measured in plasma and urine?

Intra-acinar activation of trypsinogen releases TAP into circulation, which is rapidly cleared by the kidneys for excretion in urine because of its small size. TAP can be quantitated by an enzyme-linked immunosorbent assay (ELISA) in the plasma and urine using a specific antibody to TAP ( Wu et al., 2008 ).

Which is the inactive preform of the enzyme trypsin?

Trypsinogen is the inactive preform (or zymogen) of trypsin, a proteolytic enzyme synthesized exclusively by pancreatic acinar cells and normally secreted into the duodenum where it is activated, with only minimal amounts reaching the circulation. Jian-Min Chen, Claude Férec, in Handbook of Proteolytic Enzymes (Third Edition), 2013