Inhibitor-Stimulated Non-Parallel Pancreatic Secretion in Man: Hormonal and Neural Regulation?

References

• DiMagno E P, Layer P. Human exocrine pancreatic enzyme secretion. The pancreas. Biology, pathobiology and disease2nd ed., V LW Go, et al. Raven Press Ltd, New York 1993; 275–300
   Google Scholar
• Miyasaka K, Green G M. Effect of partial exclusion of pancreatic juice on rat basal pancreatic secretion. Gastroenterology 1984; 86: 114–9
   PubMed Web of Science ®Google Scholar
• Louie D S, May D, Miller P, Owyang C. Cholecystokinin mediates feedback regulation of pancreatic enzyme secretion in rats. Am J Physiol 1986; 250: 252–9
   PubMedGoogle Scholar
• Adler G, Müllenhoff A, Koop I, Bozkurt T, Göke B, Beglinger C, et al. Stimulation of pancreatic secretion in man by a protease inhibitor (Camostate). Eur J Clin Invest 1988; 18: 98–104
   PubMed Web of Science ®Google Scholar
• Layer P, Jansen J BMJ, Cherian L, Lamers C BHW, Goebell H. Feedback regulation of human pancreatic secretion: effects of protease inhibition on duodenal delivery and small intestinal transit of pancreatic enzymes. Gastroenterology 1990; 98: 1311–9
   PubMedGoogle Scholar
• Fölsch U R. Feedback regulation of pancreatic exocrine secretion in animal and man. Eur J Clin Invest 1990; 20(Suppl 1)40–44
   Google Scholar
• Louie D S, May D, Miller P, Owyang C. Cholecystokinin mediates feedback regulation of pancreatic enzyme secretion in rats. Am J Physiol 1986; 250: 252–9
   PubMedGoogle Scholar
• Fushiki T, Kajiura H, Fukuoka S-I, Kido K, Semba T, Iwai K. Evidence for an intraluminal mediator in rat pancreatic enzyme secretion: reconstitution of the pancreatic response with dietary protein, trypsin and the monitor peptide. J Nutr 1989; 119: 622–7
   PubMedGoogle Scholar
• Harada H, Ishibashi T, Ochi K, Matsumoto S, Tanaka J, Seno T, et al. Effect of chronic administration of a protease inhibitor camostat on secretion of pure human pancreatic juice. Biomed Res 1989; 10: 63–9
   Google Scholar
• Holm H, Hanssen L E, Krogdahl Å, Florholmen J. High and low inhibitor soybean meals affect human duodenal proteinase activity differently: in vivo comparison with bovine serum albumin. J Nutr 1988; 118: 515–20
   PubMed Web of Science ®Google Scholar
• Holm H, Reseland J E, Thorsen L I, Flatmark A, Hanssen L E. Raw soybeans stimulate human pancreatic proteinase secretion. J Nutr 1992; 122: 1407–16
   PubMedGoogle Scholar
• Rausch U, Adler G, Weidenbach F, Rudolff D, Koop I, Kern H F. Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor: dose-response study on enzyme content and secretion, cholecystokinin release and pancreatic fine structure. Cell Tissue Res 1987; 247: 187–93
   PubMed Web of Science ®Google Scholar
• Sommer H, Kasper H. The action of synthetic secretion, cholecystokinin-octapeptide and combinations of these hormones on the secretion of the isolated perfused rat pancreas. Hepatogastroenterology 1981; 28: 311–4
   PubMedGoogle Scholar
• Green G M, Levan V H. Inhibition of rat pancreatic secretion by elastase. IRSC Med Sci 1985; 13: 153–4
   Google Scholar
• Chey W Y. Hormonal control of pancreatic exocrine secretion. The pancreas. Biology, pathobiology and disease2nd ed., V LW Go, et al. Raven Press Ltd, New York 1993; 403–24
   Google Scholar
• Liener I E, Goodale R L, Deshmukh A, Satterberg T L, Ward G, Dipietro C M, et al. Effect of a trypsin inhibitor from soybeans (Bowman-Birk) on the secretory activity of the human pancreas. Gastroenterology 1988; 94: 419–27
   PubMed Web of Science ®Google Scholar
• Magee D F. Does the sympathetic nervous system regulate the exocrine pancreas?. Int J Pancreatol 1989; 5: 109–16
   PubMedGoogle Scholar
• Hanssen L E. The effect of atropine on secretin release and aspired bicarbonate secretion after duodenal acidification in man. Scand J Gastroenterol 1980; 15: 465–9
   PubMed Web of Science ®Google Scholar
• Krogdahl Å, Holm H. Inhibition of human and rat pancreatic proteinases by crude and purified soybean proteinase inhibitors. J Nutr 1979; 109: 551–8
   PubMed Web of Science ®Google Scholar
• Thorsen L I, Holm H, Reseland J E, Bjørnsen S, Hanssen L E, Brosstad F. Characterization of a human trypsin resistant to Kunitz soybean trypsin inhibitor. Studies of duodenal juices after tube-instillation of raw soybean extract. Scand J Gastroenterol 1991; 26: 589–98
   PubMed Web of Science ®Google Scholar
• Bieth J, Spiess B, Wermuth C G. The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem Med 1974; 11: 350–7
   PubMed Web of Science ®Google Scholar
• Del Mar E G, Largman C, Brodrick J W, Fasset M, Geokas M C. Substrate specificity of human pancreatic elastase 2. Biochemistry 1980; 19: 468–72
   PubMed Web of Science ®Google Scholar
• Laurell C-B. Composition and variation of the gel electrophoretic fractions of plasma, cerebrospinal fluid and urine. Scand J Clin Lab Invest 1972; 29(Suppl 124)71–8
   Web of Science ®Google Scholar
• Weeke B. Rocket Immunoelectrophoresis. Scand J Immunol 1973; 2: 37–46
   PubMed Web of Science ®Google Scholar
• Stenman U-H, Koivunen E, Itkonen O. Biology and function of tumor-associated trypsin inhibitor, TATI. Scand J Clin Lab Invest 1991; 51: 5–9
   Web of Science ®Google Scholar
• Burhol P G, Jenssen T G, Lygren I, Schulz T B, Jorde R, Waldum H L. Iodination with Iodogen and radioimmunoassay of cholecystokinin (CCK) in acidified plasma, CCK release, and molecular CCK components in man. Digestion 1982; 23: 156–68
   PubMed Web of Science ®Google Scholar
• Bradley J V. Distribution-free statistical tests. Prentice-Hall Inc., Englewood Cliffs, NJ 1968
   Google Scholar
• Lindberg T, Noren O, Sjøstrøm H. Peptidases in the intestinal mucosa. Peptide transport in nutrition, D M Matthews, J W Payne. American Elsevier Publishing Company, New York 1975; 204–34
   Google Scholar
• Calam J, Bojarski J C, Springer C J. Raw soya-bean flour increases cholecystokinin release in man. Br J Nutr 1987; 58: 175–9
   PubMed Web of Science ®Google Scholar
• Adler G, Müllenhoff A, Bozkurt T, Göke B, Koop J, Arnold R. Comparison of the effect of single and repeated administrations of a protease inhibitor (camostate) on pancreatic secretion in man. Scand J Gastroenterol 1988; 23: 158–62
   PubMed Web of Science ®Google Scholar
• Adler G, Reinshagen M, Koop I, Göke B, Schafmayer A, Rovati L C, Arnold R. Differential effects of atropine and a cholecystokinin receptor antagonist on pancreatic secretion. Gastroenterology 1989; 96: 1158–64
   PubMedGoogle Scholar
• Layer P, Go V LW, DiMagno E P. Fate of pancreatic enzymes during small intestinal aboral transit in humans. Am J Physiol 1986; 251: 475–80
   PubMed Web of Science ®Google Scholar
• Muller D PR, Ghale G K. Stability of pancreatic enzyme activities in duodenal juice after pancreatic stimulation by a test meal or exogenous hormones. Ann Clin Biochem 1982; 19: 89–93
   PubMed Web of Science ®Google Scholar
• Sommer H, Schrezenmeir J, Kasper H. Output-dependent non-parallel enzyme secretion of the human pancreas. Hepatogastroenterology 1985; 32: 246–9
   PubMedGoogle Scholar
• Campbell D R, Potter M L, Curington C W, Toskes P P. Evidence that elastase may be important in feedback control of pancreatic exocrine secretion. Dig Dis Sci 1986; 31: 1127
   Google Scholar
• Adler G, Berglinger C, Braun U, Reinshagen M, Koop I, Schafmayer A, et al. Interaction of the cholinergic system and cholecystokinin in the regulation of endogenous and exogenous stimulation of pancreatic secretion in humans. Gastroenterology 1991; 100: 537–43
   PubMed Web of Science ®Google Scholar
• Stiefel D J, Keller P J. Preparation and some properties of human pancreatic amylase including a comparison with human parotid amylase. Biochim Biophys Acta 1973; 302: 345–61
   PubMedGoogle Scholar
• Malacinski G M, Rutter W J. Multiple molecular forms of α-amylase from the rabbit. Biochemistry 1969; 8: 4382–90
   PubMed Web of Science ®Google Scholar
• Karn R C, Rosenblum B B, Ward J C, Merritt A D, Shulkin J D. Immunological relationships and post-translational modification of human salivary amylase (amy1) and pancreatic amylase (amy2) isozymes. Biochem Genet 1974; 12: 485–99
   PubMedGoogle Scholar
• Merritt A D, Karn R C. The human α-amylases. Adv Hum Genet 1977; 8: 135–234
   PubMedGoogle Scholar
• Karn R C, Rosenblum B B, Merritt A D. A biochemical explanation for the complex isozyme patterns of salivary amylase (amy1) and pancreatic amylase (amy2). Am J Hum Genet 1973; 25: 39A
   Google Scholar
• Karn R C, Rosenblum B B, Ward J C, Merritt A D. Genetics and post-translational mechanisms determining human amylase isoenzyme heterogeneity. Isozymes. Genetics and evolution, C Markert. Academic Press, New York 1975; Vol. 4: 745–61
   Google Scholar
• Bozkurt T, Adler G, Koop I, Arnold R. Effect of atropine on intestinal phase of pancreatic secretion in man. Digestion 1988; 41: 108–15
   PubMed Web of Science ®Google Scholar
• Freeman T C, Davies R, Calam J. Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors. Clin Chim Acta 1990; 195: 27–40
   PubMedGoogle Scholar
• Balldin G, Borgstrøm A, Marks W H, Ohlsson K. On the role of the pancreatic secretory trypsin inhibitor as an activator of trypsin-α2-macroglobulin complexes in acute pancreatitis. Hoppe Seylers Z Physiol Chem 1984; 365: 751–6
   PubMedGoogle Scholar
• DiMagno E P, Go V LW, Summerskill W HJ. Relations between pancreatic enzyme outputs and malabsorption in severe pancreatic insufficiency. N Engl J Med 1973; 288: 813–5
   PubMed Web of Science ®Google Scholar
• Bahna S L, McCann M L. Tolerance to multiple food allergens by pancreatic enzyme supplement. J Allergy Clin Immunol 1993; 91: 151
   Google Scholar