title: Influence of exogenous application of pancreatic extracts on endogenous pancreatic enzyme secretion.
abstract: The existence of negative feedback inhibition of human pancreatic enzyme secretion by proteases is controversially discussed. We have recently demonstrated that jejunal application of porcine pancreatic extracts, in a dose commonly used to treat digestive insufficiency, stimulated rather than inhibited, human pancreatic enzyme secretion. We have now studied the influence of duodenal application of high concentrations of either pure trypsin or porcine pancreatic extracts with trypsin-equivalent activity, on human pancreatic enzyme secretion. Twenty-three male volunteers were intubated with a gastric tube and a two-lumen jejunal tube to collect secretions separately via the first and third tubes and to perfuse either pure trypsin or porcine pancreatic extracts distal to the pylorus via the second tube. PEG-4.000 was continuously perfused via the second tube to correct for losses of volume. Volunteers received PEG alone during the first hour, phenylalanine during the second, PEG alone again during the third, and either phenylalanine together with trypsin or porcine pancreatic extracts during the fourth h. Activities of lipase, amylase, and chymotrypsin were measured in 15-min fractions. In addition, human lipase secretion was measured with an enzyme immunoassay, which does not crossreact with porcine lipase. Plasma cholecystokinin (CCK) was measured using a sensitive bioassay, which utilizes amylase release by isolated rat pancreatic acini. Perfusion of the duodenum with phenylalanine caused a statistically significant stimulation of enzyme secretion. This stimulation could be inhibited by high concentrations of pure trypsin. In contrast, application of porcine pancreatic extracts, which contained the equivalent activity of trypsin, caused further increases of lipase secretion when compared to phenylalanine alone.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Medizinische Poliklinik, University of Würzburg, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Mössner
authors.forename: J H
authors.initials: JH
authors.lastname: Stange
authors.forename: M
authors.initials: M
authors.lastname: Ewald
authors.forename: W
authors.initials: W
authors.lastname: Kestel
authors.forename: W
authors.initials: W
authors.lastname: Fischbach
mesh_terms: D000328:Adult; D000681:Amylases / Q000378:metabolism; D002766:Cholecystokinin / Q000097:blood; D002918:Chymotrypsin / Q000378:metabolism; D004386:Duodenum; D005246:Feedback; D006801:Humans; D008049:Lipase / Q000378:metabolism; D008297:Male; D010179:Pancreas / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D010184:Pancreatic Extracts / Q000008:administration & dosage / Q000494:pharmacology*; D010649:Phenylalanine / Q000008:administration & dosage / Q000494:pharmacology; D014357:Trypsin / Q000008:administration & dosage / Q000494:pharmacology
chemical_list: D010184:Pancreatic Extracts; D010649:Phenylalanine; D002766:Cholecystokinin; D008049:Lipase; D000681:Amylases; D002918:Chymotrypsin; D014357:Trypsin