Summary
Earlier studies have suggested that the rate of incorporation of labeled amino acids into duodenal juice proteins during pancreatic stimulation may be used to calculate pancreatic enzyme synthesis and function. In the present study, a pulse/4 h continuous intravenous infusion of14 C labeled leucine was used to compare synthesis rates in 6 patients with chronic calcific pancreatis(CP) to 4 controls. Analysis of duodenal juice protein demonstrated a delay of approximately 1 h in the appearance of labeled proteins, followed by a linear increase in specific activity, allowing calculation of synthesis that varied between 2.6–2.8 h in controls and 6–48 h in CP. The protein in controls was representative of enzyme protein, but that of CP was not, since it was heavily contaminated with albumin (up to 50%). The results indicate that enzyme secreted during the first hour of stimulation is derived from pancreatic stores and that the synthesis rate of enzymes secreted thereafter is approximately 2.7 h in normal humans. The method was, however, unable to determine rates in patients with CP owing to heavy contamination of enzymes with exudative proteins.
Similar content being viewed by others
References
Boyd EJS, Wood H, Clarke G, Neill GD, Hutchinson F, Wormsley KG. Pancreatic synthesis rates: A new test of pancreatic function. Scand. J. Gastroenterol. 1982; 17: 225- 231.
O’Keefe SJD, Ogden J, Dicker J, Boyd E, Marks IN. Evaluation of the method of constant I V infusion of labelled amino acids in the measurements of pancreatic enzyme synthesis rates. Dig. Dis. Sci. 1986; (10): 360S, (1428).
Waterlow JC, Garlick PJ, Millward DJ. Total protein turnover from measurements on plasma and on the whole body. In Protein turnover in mammalian tissues and in the whole body. Amsterdam Elsevier North-Holland, chapter 8: 1978, 301–326.
O’Keefe SJD, Moldawer LL, Young, VR, Bilmazes C, Blackburn GL. The influence of intravenous nutrition on protein dynamics following surgery. Metabolism 1981; 30: 12: 1150–1158.
Waterlow JC. Lysine turnover in man measured by intravenous infusion of L(U14C) lysine. Clin. Sci. 1967; 33: 507–515.
Matthews DE, Motil KJ, Rohrbaugh DK, Burke JF, Young VR, Bier DM. Measurement of leucine metabolism in man from a primed, continuous infusion of L(1-3C) leucine. Am. J. Physiol. 1980; 238: (5): E473–479.
Simon O, Zebrowska T, Bergner H, Miinchmeyer R. Investigations on the pancreatic and stomach secretion in pigs by means of continuous infusion ofl4C-amino acids. Arch. Tierenahr. 1983; 33: 1: 9–22.
Schwert GW and Takenaka Y. A spectrphotometric determination of trypsin and chymotrypsin. Biochimica Biophysica Acta 1955; 16: 570–575.
Pimstone NR. A study of the starch-iodine complex: a modified colorimetric micro determination of amylase in biologic fluids. Clin. Chem. 1964; 10: 891–906.
Weber H. Mikromethode zur bestimmung der pankreaslipase im serum. Deutsch Med. Wsch. 1965; 90: 1170–1174.
Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72: 248- 254.
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. Gastroenterol. 1977; 72: (3): 417–420.
Rothman SS, Isenman LD. Secretion of digestive enzyme derived from two parallel intracellular pools. Am. J. Physiol. 1974 226: 1082–1087.
O’Keefe SJ, Abraham R, El-Zayadi A, Marshall W, Davis M, Williams R. Increased plasma tyrosine concentrations in patients with cirrhosis and fulminant hepatic failure associated with increased plasma tyrosine flux and reduced hepatic oxidation capacity. Gastroenterol. 1981; 81: (6) 1017–1024.
Multigner L, Figarella C, Sarles H. Diagnosis of chronic pancreatitis by measurement of lactoferrin in duodenal juice. Gut 1981; 22: (5): 350–354.
Clemente F, Ribeiro T, Colomb E, Sarles H. Comparison des proteines de sucs panreatiques humains normaux et pathologiques. Dosage des proteines seriques et mise en evidence d’une proteine particuliere dans la pancreatite chronique calcifiante. Biochem. Biophys. Acta 1971; 251: 456–466.
Scheele G, Bartelt D, Bieger W. Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis. Gastroenterol. 1981 80: (3): 461–473.
Tasso F, Stemmelin N, Sarles H, et al. Comparative morphometric study of the human pancreas in its normal state and in primary chronic calcifying pancreatitis. Biomedecine 1973; 18: 134–144.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
O’Keefe, S.J.D., Ogden, J.M., Young, G.O. et al. Measurement of pancreatic enzyme synthesis in humans. Int J Pancreatol 4, 13–27 (1989). https://doi.org/10.1007/BF02924144
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02924144