title: Effect of 3-hour pancreatic duct obstruction on pancreatic lysosomal and digestive enzymes in rabbits.
abstract: We studied the effect of short-term (3 hours) pancreatic duct obstruction (PDO) on the exocrine pancreas and on the secretion of lysosomal enzymes into the pancreatic juice of rabbits during stimulation by pancreatic secretagogues. The following evaluations were made: serum amylase levels, pancreatic water content, pancreatic amylase, trypsinogen and cathepsin B content, and output of pancreatic enzymes and lysosomal hydrolases when stimulated by secretin and caerulein as well as the distribution of cathepsin B in subcellular fraction. PDO for 3 hours plus secretin infusion caused a significant rise in serum amylase levels, pancreatic water content, and pancreatic amylase and trypsinogen content due to congestion of digestive enzymes during PDO. There was also a redistribution of cathepsin B from the lysosomal fraction to the zymogen fraction. In normal rabbits and in those with only secretin infusion, caerulein stimulated the secretion of cathepsin B, into pancreatic juice. Just after PDO, the secretion of cathepsin B, amylase and trypsinogen significantly decreased. By 24 hours after PDO, the output of cathepsin B stimulated by caerulein and secretin had increased significantly. Amylase and trypsinogen output were also significantly increased at this stage, in both the secretin and caerulein fractions. These results indicate that the secretion of lysosomal enzymes into pancreatic juice is stimulated by gut hormones, such as caerulein, in the normal physiological state and in pathological states, such as PDO. These results also show augmented secretion of both lysosomal enzymes and pancreatic digestive enzymes in the recovery stage after PDO and their important roles at this stage.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: First Department of Surgery, Faculty of Medicine, Kyoto University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Hirano
authors.forename: T
authors.initials: T
authors.lastname: Manabe
authors.forename: K
authors.initials: K
authors.lastname: Imanishi
authors.forename: K
authors.initials: K
authors.lastname: Ando
authors.forename: T
authors.initials: T
authors.lastname: Kyogoku
authors.forename: F
authors.initials: F
authors.lastname: Yotsumoto
authors.forename: T
authors.initials: T
authors.lastname: Imamura
authors.forename: G
authors.initials: G
authors.lastname: Ohshio
mesh_terms: D000681:Amylases / Q000378:metabolism; D000818:Animals; D002401:Cathepsin B / Q000378:metabolism; D003250:Constriction; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D010179:Pancreas / Q000201:enzymology* / Q000378:metabolism; D010182:Pancreatic Diseases / Q000503:physiopathology; D010183:Pancreatic Ducts; D010189:Pancreatic Juice / Q000201:enzymology; D011817:Rabbits; D014362:Trypsinogen / Q000378:metabolism
chemical_list: D014362:Trypsinogen; D000681:Amylases; D002401:Cathepsin B