Pancreatic lysosomal thiol proteinases and inhibitors in acute pancreatitis induced in rats.
When examining the level of esterolysis and that of cathepsin B or H, a significant positive correlation was found in the rat pancreas with inflammation induced by a closed duodenal loop, whereas there was a significant negative correlation between the activity of cathepsin B or H and that of its endogenous inhibitors. The levels of endogenous inhibitors of cathepsins B and H in rats with a pancreatitis were lower than in the sham-treated group. The endogenous inhibitors of cathepsins B and H were destroyed by incubation with the supernatant fraction obtained from the inflamed pancreas. These observations indicate that the activities of pancreatic cathepsins B and H are closely related to the severity of acute pancreatitis and that lesser levels of thiol proteinase inhibitors in the pancreatitis group than in the sham-treated group are due to destruction of the inhibitors by the enhanced protease activity.
Shikimi
T
T
Department of Pharmacology, Shimane Medical University, Japan.
Yamamoto
D
D
Handa
M
M
D000208:Acute Disease; D000818:Animals; D002401:Cathepsin B / Q000037:antagonists & inhibitors / Q000378:metabolism*; D056655:Cathepsin H; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D010179:Pancreas / Q000201:enzymology*; D010195:Pancreatitis / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D002403:Cathepsins; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056655:Cathepsin H; C534128:Ctsh protein, rat