Summary
Pure pancreatic juice was collected from 8 control subjects, 12 patients with chronic pancreatitis and 4 patients with cancer of the pancreas by endoscopic retrograde cannulation of the papilla. Samples were collected at 1 minute intervals for 20 minutes after rapid intravenous injection of secretin (Eisai, 1 U/kg) and for 10 minutes after rapid intravenous injection of CCK-PZ (Boots, 1 U/kg).
Determinations of volume, bicarbonate concentration and three hydrolases (amylase, chymotrypsinogen and lipase) were made. Our tentative conclusions are (1) pancreatic enzymes are likely to be affected one after another, not in parallel fashion, in chronic pancreatitis and in cancer of the pancreas, (2) bicarbonate concentration and chymotrypsinogen or lipase are most susceptible in chronic pancreatitis and lipase secretion seems to be more susceptible than other parameters in cancer of the pancreas. Amylase is the least affected enzyme in both pancreatic diseases, and (3) determinations of chymotrypsinogen and/or lipase should be preferably performed among hydrolytic enzymes in the evaluation of exocrine pancreatic function in chronic pancreatitis and cancer of the pancreas.
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References
Dreiling DA and Janowitz HD: The measurement of pancreatic secretory function. In Ciba Foundation Symposium: The Exocrine Pancreas: Normal and Abnormal Functions. Edited by AVS De Reuck, MP Cameron. Boston, Little, Brown & Company, 1961, pp 225–252
Burton P, Evans DG, Harper AA, Howat HT, Oleesky S, Scott JE and Varley H: A test of pancreatic function in man based on the analysis of duodenal contents after administration of secretin and pancreozymin. Gut 1: 111–124, 1960
Lagerlof HO: The secretin test of pancreatic function. Quart J Med 8: 115–126, 1939
Diamond JS and Siegel SA: The clinical application of secretin in the study of pancreatic function. NY State J Med 41: 869–874, 1941
Barbezat GO and HansenJDL: The exocrine pancreas and protein-calorie malnutrition. Pediatrics 42: 77–92, 1968
Filippini L und Ammann R: Klinisch-funktionelle diagnostik des Pancreas-karzinoms mit spezieller Berucksichtigung von Pancreozymin-Sekretin-Test und proteo-lytischer Stuhlenzymaktivitat. Schweiz Med Wschr 97: 803–810, 1967
Ammann RW, Tagwercher E, Kashiwagi H and Rosenmund H: Diagnostic value of fecal chymotrypsin and trypsin assessment for detection of pancreatic disease. Amer J Dig Dis n s 13: 123–146, 1968
Hadorn B, Zoppi G, Shmerling DH, Prader A, Mclntyre and Anderson CM: Quantitative assessment of exocrine pancreatic function in infants and children. J Pediat 73: 39–50, 1968
Choi HJ, Goldstein F, Wirts CW and Menduke HO: Normal duodenal trypsin values in response to secretinpancreozymin stimulation with preliminary data in patients with pancreatic disease. Gastroenterology 53: 397–402, 1967
Mott C, Sarles H, Tiscornia O and Gullo L: Inhibitory action of alcohol on man exocrine pancreatic secretion. Amer J Dig Dis 17: 902–910, 1972
Wormsley KG and Goldberg DM: The interrelationships of the pancreatic enzymes. Gut 13: 398–412, 1972
Harada H, Tanaka J, Shundo T, Hayashi T, Sasaki T, Yamamoto N, Sato T, Mishima K and Kimura I: A diagnostic approach to inflammatory disease of the pancreas by means of endoscopic retrograde cholangiopancreatography. Gastroent japonica 12: 387–394, 1977
Lowry OH, Rosegrough NJ, Farr AL, et al: Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275, 1951
Toda Y, Hayakawa T, Noda A, et al: Amylase and macroamylase. Jap J Clin Med 31: 558–569, 1973
Kurooka S, Hashimoto M, Tomita M, et al: Relationship between the structures of S-acyl thiol compounds and their rates of hydrolysis by pancreatic lipase and hepatic carboxylic esterase. J Biochem 79: 533–541, 1976
Kurooka S, Okamoto S and Hashimoto M: A novel and simple colorimetric assay for human serum lipase. J Biochem 81: 361–369, 1977
Kinugasa K: A new test of exocrine pancreatic function using N-benzoyl-L-tyrosyl-p-aminobenzoic acid. Part II. The correlation of PFD and chymotrypsin output during PS-test. Jap J Gastroent 74: 1337–1346, 1977
Goldberg DM, Sale JK, Fawcett N and Wormsley KG: Trypsin and chymotrypsin as aids in the diagnosis of pancreatic disease. Amer J Dig Dis 17: 780–792, 1972
Diamond JS, Siegel SA, Gall MB and Karlen S: The use of secretin as a clinical test of pancreatic function. Amer J Dig Dis 6: 366–372, 1939
Rick W: Zur Pathologie der Enzymsekretion des Pankreas. Actagastro-ent belg 28: 389–400, 1965
Ribet A, Pascal JP, Vaysse N, Augier D et Thouvenot JP: Relations entre le taux des proteines totales et l’activite des enzymes dans le sue pancreatique humain normal et pathologique. 7th congr Clin Chem, Geneva/Evian 1969, vol. 2, pp. 155–162 (Karger, Basel 1970)
Capitaine Y, Cros RC, Gullo L, Barros-Mott C de, Pastor J, Pauli AM and Sarles H: Etude multivariee des donnees de l’exploration pancreatique par tubage. Biol Gastroenterol 60: 302–308, 1971
Gullo L, Sarles H and Mott CB: Functional investigation of exocrine pancreas following acute pancreatitis. Re Gastroenterol 4: 18–21, 1972
Minaire Y, Descos L, Daly JP, Bererd MB and Lambert R: The interrelationships of pancreatic enzymes in health and diseases under cholecystokinin stimulation. Digestion 9: 8–20, 1973
Zieve L, Silvis SE, Mulford B and Blackwood WD: Secretion of pancreatic enzymes. I. Response to secretin and pancreozymin. Amer J Dig Dis ns 11: 671–684, 1966
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Harada, H., Hayashi, T., Ono, A. et al. Analysis of human pure pancreatic juice in chronic pancreatitis and cancer of the pancreas. Gastroenterol Jpn 13, 461–467 (1978). https://doi.org/10.1007/BF02774912
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DOI: https://doi.org/10.1007/BF02774912