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. 1993 Sep;34(9):1261–1266. doi: 10.1136/gut.34.9.1261

Duodenal juice total protein and pancreatic enzyme synthesis, turnover, and secretion in patients after acute pancreatitis.

J M Ogden 1, S J O'Keefe 1, J A Louw 1, G Adams 1, I N Marks 1
PMCID: PMC1375466  PMID: 7691692

Abstract

It is controversial whether acute pancreatitis has longterm effects on pancreatic function. Pancreatic enzyme synthesis, turnover, and secretion were measured in 10 patients in clinical remission who had had one or more (one to six) attacks of acute alcoholic pancreatitis. The studies were done between two and 29 months after the most recent attack. A control group included five patients with no evidence of pancreatic disease. A four hour primed/continuous intravenous infusion of [14C]L-leucine tracer was given with secretin (2 U/kg/h) and cholecystokinin (0.5 U/kg/h) and secreted duodenal juice aspirated. Amylase and trypsin were extracted from duodenal juice by affinity chromatography, permitting measurement of the rate of isotope incorporation into total protein, amylase, and trypsin. The results showed non-parallel changes in enzyme synthesis and turnover with decreases in total enzyme protein and amylase synthesis and turnover but preservation of trypsin synthesis and turnover. The low turnover rates may be ascribed to continuing pancreatic cell malfunction after recovery from acute alcoholic pancreatitis and suggest that the decreased amylase secretion rates are partly a consequence of impaired amylase synthesis and not simply because of loss of pancreatic tissue.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ammann R. W., Buehler H., Bruehlmann W., Kehl O., Muench R., Stamm B. Acute (nonprogressive) alcoholic pancreatitis: prospective longitudinal study of 144 patients with recurrent alcoholic pancreatitis. Pancreas. 1986;1(3):195–203. [PubMed] [Google Scholar]
  2. Ammann R. W., Tagwecher E., Kashiwagi H., Rosenmund H. Diagnostic value of fecal chymotrypsin and trypsin assessment for detection of pancreatic disease. A comparative study. Am J Dig Dis. 1968 Feb;13(2):123–146. doi: 10.1007/BF02232955. [DOI] [PubMed] [Google Scholar]
  3. BURTON P., EVANS D. G., HARPER A. A., HOWATH T., OLEESKY S., SCOTT J. E., VARLEY H. A test of pancreatic function in man based on the analysis of duodenal contents after administration of secretin and pancreozymin. Gut. 1960 Jun;1:111–124. doi: 10.1136/gut.1.2.111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boyd E. J., Wood H., Clarke G., Neill G. D., Hutchison F., Wormsley K. G. Pancreatic synthetic rates: a new test of pancreatic function. Scand J Gastroenterol. 1982 Mar;17(2):225–231. doi: 10.3109/00365528209182044. [DOI] [PubMed] [Google Scholar]
  5. Calvo E. L., Vaccaro M. I., Tumilasci O. R., Iovanna J. L. Synthesis and contents of pancreatic exportable enzymes. Effect of oleic acid intraduodenal administration. Acta Physiol Pharmacol Latinoam. 1988;38(2):145–150. [PubMed] [Google Scholar]
  6. Choi H. J., Goldstein F., Wirts C. W., Menduke H. Normal duodenal trypsin values in response to secretin-pancreozymin stimulation with preliminary data in patients with pancreatic disease. Gastroenterology. 1967 Sep;53(3):397–402. [PubMed] [Google Scholar]
  7. Dagorn J. C., Mongeau R. Different action of hormonal stimulation on the biosynthesis of three pancreatic enzymes. Biochim Biophys Acta. 1977 Jun 23;498(1):76–82. doi: 10.1016/0304-4165(77)90088-5. [DOI] [PubMed] [Google Scholar]
  8. Długosz J., Fölsch U. R., Czajkowski A., Gabryelewicz A. Feedback regulation of stimulated pancreatic enzyme secretion during intraduodenal perfusion of trypsin in man. Eur J Clin Invest. 1988 Jun;18(3):267–272. doi: 10.1111/j.1365-2362.1988.tb01257.x. [DOI] [PubMed] [Google Scholar]
  9. Goldberg D. M., Wormsley K. G. The interrelationships of pancreatic enzymes in human duodenal aspirate. Gut. 1970 Oct;11(10):859–866. doi: 10.1136/gut.11.10.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Green G. M., Lyman R. L. Feedback regulation of pancreatic enzyme secretion as a mechanism for trypsin inhibitor-induced hypersecretion in rats. Proc Soc Exp Biol Med. 1972 May;140(1):6–12. doi: 10.3181/00379727-140-36384. [DOI] [PubMed] [Google Scholar]
  11. Louie D. S., May D., Miller P., Owyang C. Cholecystokinin mediates feedback regulation of pancreatic enzyme secretion in rats. Am J Physiol. 1986 Feb;250(2 Pt 1):G252–G259. doi: 10.1152/ajpgi.1986.250.2.G252. [DOI] [PubMed] [Google Scholar]
  12. Lu L., Louie D., Owyang C. A cholecystokinin releasing peptide mediates feedback regulation of pancreatic secretion. Am J Physiol. 1989 Feb;256(2 Pt 1):G430–G435. doi: 10.1152/ajpgi.1989.256.2.G430. [DOI] [PubMed] [Google Scholar]
  13. MARKS I. N., TOMPSETT S. L. The diagnosis of pancreatic disease. Q J Med. 1958 Jul;27(107):431–461. [PubMed] [Google Scholar]
  14. Miyasaka K., Guan D. F., Liddle R. A., Green G. M. Feedback regulation by trypsin: evidence for intraluminal CCK-releasing peptide. Am J Physiol. 1989 Aug;257(2 Pt 1):G175–G181. doi: 10.1152/ajpgi.1989.257.2.G175. [DOI] [PubMed] [Google Scholar]
  15. O'Keefe S. J., Ogden J. M., Young G. O., Dicker J., Girdwood A. H., Marks I. N. Measurement of pancreatic enzyme synthesis in humans. Problems in patients with calcific pancreatitis. Int J Pancreatol. 1989 Feb;4(1):13–27. doi: 10.1007/BF02924144. [DOI] [PubMed] [Google Scholar]
  16. Ogden J. M., O'Keefe S. J., Ehlers M. R., Kirsch R. E., Marks I. N. Single step affinity chromatographic purification of human alpha-amylase from aspirated duodenal juice and its application in the measurement of pancreatic alpha-amylase synthesis rates in man. Clin Chim Acta. 1989 Feb 28;180(2):129–139. doi: 10.1016/0009-8981(89)90344-6. [DOI] [PubMed] [Google Scholar]
  17. Ogden J. M., O'Keefe S. J., Marks I. N. Development of a method for the purification of human trypsin by single step affinity chromatography suitable for human isotope incorporation studies. Clin Chim Acta. 1992 Nov 30;212(3):141–147. doi: 10.1016/0009-8981(92)90181-o. [DOI] [PubMed] [Google Scholar]
  18. Owyang C., Louie D. S., Tatum D. Feedback regulation of pancreatic enzyme secretion. Suppression of cholecystokinin release by trypsin. J Clin Invest. 1986 Jun;77(6):2042–2047. doi: 10.1172/JCI112534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Owyang C., May D., Louie D. S. Trypsin suppression of pancreatic enzyme secretion. Differential effect on cholecystokinin release and the enteropancreatic reflex. Gastroenterology. 1986 Sep;91(3):637–643. doi: 10.1016/0016-5085(86)90633-5. [DOI] [PubMed] [Google Scholar]
  20. Regan P. T., Go V. L., DiMagno E. P. Comparison of the effects of cholecystokinin and cholecystokinin octapeptide on pancreatic secretion, gallbladder contraction, and plasma pancreatic polypeptide in man. J Lab Clin Med. 1980 Oct;96(4):743–748. [PubMed] [Google Scholar]
  21. Rick W. Zur Pathologie der Enzymsekretion des Pankreas. Acta Gastroenterol Belg. 1965 May-Jun;28(5):389–400. [PubMed] [Google Scholar]
  22. Robberecht P., Cremer M., Christophe J. Discharge of newly synthesized proteins in pure juice collected from the human pancreas. Indication of more than one pool of intracellular digestive enzymes. Gastroenterology. 1977 Mar;72(3):417–420. [PubMed] [Google Scholar]
  23. Simon O., Zebrowska T., Bergner H., Münchmeyer R. Investigations on the pancreatic and stomach secretion in pigs by means of continuous infusion of 14C-amino acids. Arch Tierernahr. 1983 Jan;33(1):9–22. doi: 10.1080/17450398309425668. [DOI] [PubMed] [Google Scholar]
  24. Steinhilber W., Poensgen J., Rausch U., Kern H. F., Scheele G. A. Translational control of anionic trypsinogen and amylase synthesis in rat pancreas in response to caerulein stimulation. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6597–6601. doi: 10.1073/pnas.85.18.6597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Zieve L., Silvis S. E., Mulford B., Blackwood W. D. Secretion of pancreatic enzymes. I. Response to secretin and pancreozymin. Am J Dig Dis. 1966 Sep;11(9):671–684. doi: 10.1007/BF02239420. [DOI] [PubMed] [Google Scholar]
  26. el Newihi H., Dooley C. P., Saad C., Staples J., Zeidler A., Valenzuela J. E. Impaired exocrine pancreatic function in diabetics with diarrhea and peripheral neuropathy. Dig Dis Sci. 1988 Jun;33(6):705–710. doi: 10.1007/BF01540434. [DOI] [PubMed] [Google Scholar]

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