Activation of proteases in cerulein-induced pancreatitis.
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.
Yamaguchi
H
H
Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Kimura
T
T
Mimura
K
K
Nawata
H
H
D000681:Amylases / Q000097:blood; D000818:Animals; D001835:Body Weight; D002401:Cathepsin B / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology; D002108:Ceruletide; D004792:Enzyme Precursors / Q000378:metabolism; D008049:Lipase / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology; D008297:Male; D010179:Pancreas / Q000032:analysis / Q000187:drug effects / Q000201:enzymology; D010196:Pancreatic Elastase / Q000378:metabolism; D010195:Pancreatitis / Q000139:chemically induced / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin / Q000378:metabolism; D014362:Trypsinogen / Q000378:metabolism
D004792:Enzyme Precursors; D002108:Ceruletide; D014362:Trypsinogen; D008049:Lipase; D000681:Amylases; D010447:Peptide Hydrolases; D010196:Pancreatic Elastase; D014357:Trypsin; D002401:Cathepsin B