Hormonal and cholinergic effects on amylase and lysosomal enzyme activities in pancreatic tissue and ascites of rats with acute experimental pancreatitis.
The effects of hormonal or cholinergic stimulation on survival and on activities of lysosomal enzymes and amylase in pancreatic tissue and ascites were studied in rats with induced pancreatitis. Pancreatitis per se caused an increase of the activities of cathepsin D, N-acetyl-beta-D-glucosaminidase and amylase, and a decrease of acid phosphatase in pancreatic tissue. Pancreatic protein concentration was not influenced. In pancreatitic rats administration of cerulein or carbachol markedly decreased survival rate. Cerulein increased the activities of cathepsin D and amylase in ascites and cathepsin D and acid phosphatase in pancreatic tissue. Carbachol increased the activities of cathepsin D and amylase in ascites and acid phosphatase in pancreatic tissue. Both cerulein and carbachol decreased the activity of amylase in pancreatic tissue. Administration of secretin or the anticholinergic drug Pro-Banthine did not influence survival rate or the activities of lysosomal enzymes and amylase in ascites. In pancreatic tissue the activity of acid phosphatase was slightly increased by secretin or Pro-Banthine. In conclusion, the results show a nonparallel alteration of lysosomal enzyme activities in pancreatic tissue in rats with pancreatitis. Cerulein and cholinergic stimulation decreased survival rate and brought about a marked increase of cathepsin D activity in ascites and, in the case of cerulein, also in pancreatic tissue. The implication of lysosomes and especially the catheptic proteases in the pathogenesis and outcome of acute pancreatitis deserves further attention.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000135:Acid Phosphatase / Q000378:metabolism*; D000208:Acute Disease; D000681:Amylases / Q000378:metabolism*; D000818:Animals; D001202:Ascitic Fluid / Q000201:enzymology; D002217:Carbachol / Q000494:pharmacology; D002402:Cathepsin D; D002403:Cathepsins / Q000378:metabolism*; D002108:Ceruletide / Q000494:pharmacology; D006596:Hexosaminidases / Q000378:metabolism*; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology; D008297:Male; D010179:Pancreas / Q000201:enzymology; D010195:Pancreatitis / Q000201:enzymology* / Q000209:etiology; D011413:Propantheline / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D012633:Secretin / Q000494:pharmacology
D011413:Propantheline; D012633:Secretin; D002108:Ceruletide; D002217:Carbachol; D000135:Acid Phosphatase; D000681:Amylases; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D002403:Cathepsins; D002402:Cathepsin D