Activation of proteases in cerulein-induced pancreatitis

Pancreas. 1989;4(5):565-71. doi: 10.1097/00006676-198910000-00007.

Abstract

The activation of zymogen proteases and lysosomal enzyme cathepsin B in the pancreas was investigated in cerulein-induced pancreatitis in rats. Acute pancreatitis was induced by two intraperitoneal injections of 40 micrograms/kg of body weight of cerulein at intervals of 1 h. After the first cerulein injection, the active trypsin and elastase contents in the pancreas tissues significantly increased, and reached the highest level at 3 h after the first injection, followed by peaks at 5 h in the serum amylase and lipase levels and the pancreas wet weight. Cathepsin B contents in pancreas tissues showed a parallel increase with active zymogen enzymes during the first 3 h of pancreatitis. These findings may suggest that the intracellular activation of trypsinogen is an important step in the development of cerulein-induced acute pancreatitis and that cathepsin B plays a role in the activation of trypsinogen in pancreatic acinar cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amylases / blood
  • Animals
  • Body Weight
  • Cathepsin B / analysis
  • Cathepsin B / metabolism
  • Cathepsin B / pharmacology
  • Ceruletide
  • Enzyme Precursors / metabolism
  • Lipase / metabolism
  • Lysosomes / enzymology
  • Male
  • Pancreas / analysis
  • Pancreas / drug effects
  • Pancreas / enzymology
  • Pancreatic Elastase / metabolism
  • Pancreatitis / chemically induced
  • Pancreatitis / enzymology*
  • Peptide Hydrolases / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Trypsin / metabolism
  • Trypsinogen / metabolism

Substances

  • Enzyme Precursors
  • Ceruletide
  • Trypsinogen
  • Lipase
  • Amylases
  • Peptide Hydrolases
  • Pancreatic Elastase
  • Trypsin
  • Cathepsin B