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. 1975 Mar;245(3):617–638. doi: 10.1113/jphysiol.1975.sp010865

Secretion of calcium in pancreatic juice.

B Ceccarelli, F Clemente, J Meldolesi
PMCID: PMC1330809  PMID: 1142221

Abstract

1. The orgin of the calcium secreted by the pancreas has been investigated in vivo in the guinea-pig by a study carried out in parallel (a) in the juice secreted in response to the injection of either secretin or caerulein and (b) in the pancreatic tissue and in cell fractions isolated thereform. 2. In agreement with previous findings we observed that the concentration of calcium is low in the secretin-stimulated and high in the caerulein-stimulated juice. In the latter calcium and protein are proportional (cal0 n-mole:mg). 3. After I.V. injection of 45Ca the radioactivity decreases rapidly and quasi-exponentially in the blood plasma. A roughly parallel time course is found in the secretin-stimulated juice: the evolution of the juice: plasma radioactivity ratio resembles that observed with the extraceullar space marker [3H]D-sorbitol. In contrast, the time course of 45Ca in plasma and caerulein-stimulated juice are not proportional: the high levels characteristic of this juice are reached several minutes after the injection and maintained thereafter. This increase is followed ca. 50 min later by the appearance of the newly synthesized [3H]L-leucine-labelled proteins. 4. The pancreatic tissue is rich in calcium which is localized primarily in zymogen granules (Ca.36 n-mole:mg protein) and mitochondria; the soluble cytoplasm is low in calcium. 5. The injected 45Ca accumulates in zymogen granules faster than [3H]L-leucine-labelled proteins. The 45Ca:protein ratio of these organelles is considerably lower than that of the caerulein-stimulated juice. 6. It is concluded (a) that calcium is secreted in to the pancreatic juice in two fractions, one (possibly released by simple diffusion) associated with the electrolyte component, the other with protein of the juice, (b) that zymogen granules are the major, but not the only source of the latter fraction, and (c) that the zymogen granule-associated calcium joins the exportable proteins some time after their synthesis, possibly in the Golgi complex and/or in the condensing vacuoles.

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Selected References

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  1. Alonso G. L., Bazerque P. M., Arrigó D. M., Tumilasci O. R. Adenosine triphosphate--dependent calcium uptake by rat submaxillary gland microsomes. J Gen Physiol. 1971 Sep;58(3):340–350. doi: 10.1085/jgp.58.3.340. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Argent B. E., Case R. M., Scratcherd T. Amylase secretion by the perfused cat pancreas in relation to the secretion of calcium and other electrolytes and as influenced by the external ionic environment. J Physiol. 1973 May;230(3):575–593. doi: 10.1113/jphysiol.1973.sp010205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BAUER H., GOODFORD P. J., HUETER J. THE CALCIUM CONTENT AND 45-CALCIUM UPTAKE OF THE SMOOTH MUSCLE OF THE GUINEA-PIG TAENIA COLI. J Physiol. 1965 Jan;176:163–179. doi: 10.1113/jphysiol.1965.sp007542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Benzonana G. Sur le role des ions calcium durant l'hydrolyse des triglycérides insolubles par la lipase pancréatique en présence de sels biliaires. Biochim Biophys Acta. 1968 Jan 8;151(1):137–146. doi: 10.1016/0005-2744(68)90168-x. [DOI] [PubMed] [Google Scholar]
  5. Bertaccini G., De Caro G., Endean R., Erspamer V., Impicciatore M. The action of caerulein on pancreatic secretion of the dog and biliary secretion of the dog and the rat. Br J Pharmacol. 1969 Sep;37(1):185–197. doi: 10.1111/j.1476-5381.1969.tb09537.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. CARO L. G., PALADE G. E. PROTEIN SYNTHESIS, STORAGE, AND DISCHARGE IN THE PANCREATIC EXOCRINE CELL. AN AUTORADIOGRAPHIC STUDY. J Cell Biol. 1964 Mar;20:473–495. doi: 10.1083/jcb.20.3.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Case R. M. Calcium and gastrointestinal secretion. Digestion. 1973;8(3):269–288. doi: 10.1159/000197324. [DOI] [PubMed] [Google Scholar]
  8. Case R. M., Clausen T. The relationship between calcium exchange and enzyme secretion in the isolated rat pancreas. J Physiol. 1973 Nov;235(1):75–102. doi: 10.1113/jphysiol.1973.sp010379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Case R. M., Harper A. A., Scratcherd T. The secretion of electrolytes and enzymes by the pancreas of the anaesthetized cat. J Physiol. 1969 Apr;201(2):335–348. doi: 10.1113/jphysiol.1969.sp008759. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. DESNUELLE P., GABELOTEAU C. Sur le role du calcium pendant l'activation du trypsinogène par la trypsine. Arch Biochem Biophys. 1957 Jul;69:475–485. doi: 10.1016/0003-9861(57)90512-x. [DOI] [PubMed] [Google Scholar]
  11. Delaage M., Lazdunski M. The binding of Ca2+ to trypsinogen and its relation to the mechanism of activation. Biochem Biophys Res Commun. 1967 Aug 7;28(3):390–394. doi: 10.1016/0006-291x(67)90323-3. [DOI] [PubMed] [Google Scholar]
  12. Goebell H., Steffen C., Bode C. Stimulatory effect of pancreozymin-cholecystokinin on calcium secretion in pancreatic juice of dogs. Gut. 1972 Jun;13(6):477–482. doi: 10.1136/gut.13.6.477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Goodford P. J., Leach E. H. The extracellular space of the smooth muscle of the guinea-pig taenia coli. J Physiol. 1966 Sep;186(1):1–10. doi: 10.1113/jphysiol.1966.sp008016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol. 1967 Aug;34(2):577–596. doi: 10.1083/jcb.34.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. II. Transport to condensing vacuoles and zymogen granules. J Cell Biol. 1967 Aug;34(2):597–615. doi: 10.1083/jcb.34.2.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  17. Makhlouf G. M., Blum A. L. An assessment of models for pancreatic secretion. Gastroenterology. 1970 Dec;59(6):896–908. [PubMed] [Google Scholar]
  18. Matthews E. K., Petersen O. H., Williams J. A. Pancreatic acinar cells: acetylcholine-induced membrane depolarization, calcium efflux and amylase release. J Physiol. 1973 Nov;234(3):689–701. doi: 10.1113/jphysiol.1973.sp010367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Meldolesi J. Effect of caerulein on protein synthesis and secretion in the guinea-pig pancreas. Br J Pharmacol. 1970 Dec;40(4):721–731. doi: 10.1111/j.1476-5381.1970.tb10649.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Meldolesi J., Jamieson J. D., Palade G. E. Composition of cellular membranes in the pancreas of the guinea pig. I. Isolation of membrane fractions. J Cell Biol. 1971 Apr;49(1):109–129. doi: 10.1083/jcb.49.1.109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Moore E. W., Makhlouf G. M. Calcium in normal human gastric juice. A four-component model with speculation on the relation of calcium to pepsin secretion. Gastroenterology. 1968 Oct;55(4):465–480. [PubMed] [Google Scholar]
  22. Pieterson W. A., Volwerk J. J., de Haas G. H. Interaction of phospholipase A2 and its zymogen with divalent metal ions. Biochemistry. 1974 Mar 26;13(7):1439–1445. doi: 10.1021/bi00704a019. [DOI] [PubMed] [Google Scholar]
  23. Poisner A. M., Hava M. The role of adenosine triphosphate and adenosine triphosphatase in the release of catecholamines from the adrenal medulla. IV. Adenosine triphosphate-- activated uptake of calcium by microsomes and mitochondria. Mol Pharmacol. 1970 Jul;6(4):407–415. [PubMed] [Google Scholar]
  24. SARDA L., MARCHIS-MOUREN G., CONSTANTIN M. J., DESNUELLE P. Sur quelques essais de purification de la lipase pancréatique. Biochim Biophys Acta. 1957 Feb;23(2):264–274. doi: 10.1016/0006-3002(57)90328-1. [DOI] [PubMed] [Google Scholar]
  25. STEIN E. A., HSIU J., FISCHER E. H. ALPHA-AMYLASES AS CALCIUM-METALLOENZYMES. I. PREPARATION OF CALCIUM-FREE APOAMYLASES BY CHELATION AND ELECTRODIALYSIS. Biochemistry. 1964 Jan;3:56–61. doi: 10.1021/bi00889a010. [DOI] [PubMed] [Google Scholar]
  26. Selinger Z., Naim E., Lasser M. ATP-dependent calcium uptake by microsomal preparations from rat parotid and submaxillary glands. Biochim Biophys Acta. 1970 Apr 21;203(2):326–334. doi: 10.1016/0005-2736(70)90147-1. [DOI] [PubMed] [Google Scholar]
  27. Sipos T., Merkel J. R. An effect of calcium ions on the activity, heat stability, and structure of trypsin. Biochemistry. 1970 Jul 7;9(14):2766–2775. doi: 10.1021/bi00816a003. [DOI] [PubMed] [Google Scholar]
  28. Van Venrooij W. J., Poort C., Kramer M. F., Jansen M. T. Relationship between extracellular amino acids and protein synthesis in vitro in the rat pancreas. Eur J Biochem. 1972 Nov 7;30(3):427–433. doi: 10.1111/j.1432-1033.1972.tb02114.x. [DOI] [PubMed] [Google Scholar]
  29. Wallach D., Schramm M. Calcium and the exportable protein in rat parotid gland. Parallel subcellular distribution and concomitant secretion. Eur J Biochem. 1971 Aug 16;21(3):433–437. doi: 10.1111/j.1432-1033.1971.tb01489.x. [DOI] [PubMed] [Google Scholar]
  30. de Haas G. H., Bonsen P. P., Pieterson W. A., van Deenen L. L. Studies on phospholipase A and its zymogen from porcine pancreas. 3. Action of the enzyme on short-chain lecithins. Biochim Biophys Acta. 1971 Jul 13;239(2):252–266. doi: 10.1016/0005-2760(71)90171-8. [DOI] [PubMed] [Google Scholar]

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