Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1977 Jun 1;73(3):578–593. doi: 10.1083/jcb.73.3.578

Inhibitory effect of colchicines on amylase secretion by rat parotid glands: possible localization in the golgi area

C Patzelt, D Brown, B Jeanrenaud
PMCID: PMC2111413  PMID: 873990

Abstract

Colchicine inhibited amylase secretion by isolated rat parotid glands only 6 h after administration of the drug in vivo. This delayed effect was not the result of the inability of the drug to reach its reaction site. When parotid glands were emptied of their secretory granules by isoproterenol treatment, the subsequent replenishment of cells with granules was inhibited by colchicines. Colchicine concomitantly produced alterations of the Golgi complexes, the cisternae of which were reduced in size and surrounded by clusters of microvesicles. Incubation of parotid glands with colchicines for prolonged durations failed to alter stored amylase secretion as stimulated by isoproterenol, but it inhibited the release of de novo synthesized enzyme. Another colchicines-binding activity, firmly bound to the particular fraction of homogenates, was found, of which a part may represent membrane located microtubular protein. An assembly-disassembly cycle of microtubules appears to exist in the parotid gland, as in the liver. However, only 14 percent of tubulin was found to be polymerized as microtubules in parotid glands as opposed to 40 percent in the liver. The present data suggest that colchicine primarily inhibits the transfer of secretory material towards or away from the Golgi complexes but not the hormone-stimulated secretion of stored amylase.

Full Text

The Full Text of this article is available as a PDF (3.3 MB).

Selected References

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

  1. Aledort L. M., Weed R. I., Troup S. B. Ionic effects on firefly bioluminescence assay of red blood cell ATP. Anal Biochem. 1966 Nov;17(2):268–277. doi: 10.1016/0003-2697(66)90205-3. [DOI] [PubMed] [Google Scholar]
  2. Amsterdam A., Ohad I., Schramm M. Dynamic changes in the ultrastructure of the acinar cell of the rat parotid gland during the secretory cycle. J Cell Biol. 1969 Jun;41(3):753–773. doi: 10.1083/jcb.41.3.753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Arstila A. U., Nuuja I. J., Trump B. F. Studies on cellular autophagocytosis. Vinblastine-induced autophagy in the rat liver. Exp Cell Res. 1974 Aug;87(2):249–252. doi: 10.1016/0014-4827(74)90477-7. [DOI] [PubMed] [Google Scholar]
  4. Bhattacharyya B., Volff J. Membrane-bound tubulin in brain and thyroid tissue. J Biol Chem. 1975 Oct 10;250(19):7639–7646. [PubMed] [Google Scholar]
  5. Butcher F. R., Goldman R. H. Effect of cytochalasin B and colchicine on the stimulation of -amylase release from rat parotid tissue slices. Biochem Biophys Res Commun. 1972 Jul 11;48(1):23–29. doi: 10.1016/0006-291x(72)90338-5. [DOI] [PubMed] [Google Scholar]
  6. Castle J. D., Jamieson J. D., Palade G. E. Radioautographic analysis of the secretory process in the parotid acinar cell of the rabbit. J Cell Biol. 1972 May;53(2):290–311. doi: 10.1083/jcb.53.2.290. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cope G. H., Williams M. A. Exocrine secretion in the parotid gland: a stereological analysis at the electron microscopic level of the zymogen granule content before and after isoprenaline-induced degranulation. J Anat. 1973 Nov;116(Pt 2):269–284. [PMC free article] [PubMed] [Google Scholar]
  8. Danielsson A. Techniques for measuring amylase secretion from pieces of mouse pancreas. Anal Biochem. 1974 May;59(1):220–234. doi: 10.1016/0003-2697(74)90028-1. [DOI] [PubMed] [Google Scholar]
  9. Ehrlich H. P., Ross R., Bornstein P. Effects of antimicrotubular agents on the secretion of collagen. A biochemical and morphological study. J Cell Biol. 1974 Aug;62(2):390–405. doi: 10.1083/jcb.62.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Garland D., Teller D. C. A reexamination of the reaction between colchicine and tubulin. Ann N Y Acad Sci. 1975 Jun 30;253:232–238. doi: 10.1111/j.1749-6632.1975.tb19202.x. [DOI] [PubMed] [Google Scholar]
  11. HAM R. G. CLONAL GROWTH OF MAMMALIAN CELLS IN A CHEMICALLY DEFINED, SYNTHETIC MEDIUM. Proc Natl Acad Sci U S A. 1965 Feb;53:288–293. doi: 10.1073/pnas.53.2.288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jamieson J. D., Palade G. E. Synthesis, intracellular transport, and discharge of secretory proteins in stimulated pancreatic exocrine cells. J Cell Biol. 1971 Jul;50(1):135–158. doi: 10.1083/jcb.50.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lacy P. E., Malaisse W. J. Microtubules and beta cell secretion. Recent Prog Horm Res. 1973;29:199–228. doi: 10.1016/b978-0-12-571129-6.50009-9. [DOI] [PubMed] [Google Scholar]
  16. Le Marchand Y., Patzelt C., Assimacopoulos-Jeannet F., Loten E. G., Jeanrenaud B. Evidence for a role of the microtubular system in the secretion of newly synthesized albumin and other proteins by the liver. J Clin Invest. 1974 Jun;53(6):1512–1517. doi: 10.1172/JCI107701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Le Marchand Y., Singh A., Assimacopoulos-Jeannet F., Orci L., Rouiller C., Jeanrenaud B. A role for the microtubular system in the release of very low density lipoproteins by perfused mouse livers. J Biol Chem. 1973 Oct 10;248(19):6862–6870. [PubMed] [Google Scholar]
  18. Mollenhauer H. H. Distribution of microtubules in the golgi apparatus of Euglena gracilis. J Cell Sci. 1974 Jun;15(1):89–97. doi: 10.1242/jcs.15.1.89. [DOI] [PubMed] [Google Scholar]
  19. Moskalewski S., Thyberg J., Friberg U. In vitro influence of colchicine on the Golgi complex in A- and B-cells of guinea pig pancreatic islets. J Ultrastruct Res. 1976 Feb;54(2):304–317. doi: 10.1016/s0022-5320(76)80159-1. [DOI] [PubMed] [Google Scholar]
  20. Moskalewski S., Thyberg J., Lohmander S., Friberg U. Influence of colchicine and vinblastine on the golgi complex and matrix deposition in chondrocyte aggregates. An ultrastructural study. Exp Cell Res. 1975 Oct 15;95(2):440–454. doi: 10.1016/0014-4827(75)90569-8. [DOI] [PubMed] [Google Scholar]
  21. Müller P., Singh A., Orci L., Jeanrenaud B. Secretory processes, carbohydrate and lipid metabolism in isolated mouse hepatocytes. Aspects of regulation by glucagon and insulin. Biochim Biophys Acta. 1976 Apr 23;428(2):480–494. doi: 10.1016/0304-4165(76)90057-x. [DOI] [PubMed] [Google Scholar]
  22. Orci L., Le Marchand Y., Singh A., Assimacopoulos-Jeannet F., Rouiller C., Jeanrenaud B. Letter: Role of microtubules in lipoprotein secretion by the liver. Nature. 1973 Jul 6;244(5410):30–32. doi: 10.1038/244030a0. [DOI] [PubMed] [Google Scholar]
  23. Patzelt C., Singh A., Marchand Y. L., Orci L., Jeanrenaud B. Colchicine-binding protein of the liver. Its characterization and relation to microtubules. J Cell Biol. 1975 Sep;66(3):609–620. doi: 10.1083/jcb.66.3.609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Pipeleers D. G., Pipeleers-Marichal M. A., Kipnis D. M. Microtubule assembly and the intracellular transport of secretory granules in pancreatic islets. Science. 1976 Jan 9;191(4222):88–90. doi: 10.1126/science.1108194. [DOI] [PubMed] [Google Scholar]
  25. Redman C. M., Banerjee D., Howell K., Palade G. E. Colchicine inhibition of plasma protein release from rat hepatocytes. J Cell Biol. 1975 Jul;66(1):42–59. doi: 10.1083/jcb.66.1.42. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Seybold J., Bieger W., Kern H. F. Studies on intracellular transport of secretory proteins in the rat exocrine pancreas. II. Inhibition of antimicrotubular agents. Virchows Arch A Pathol Anat Histol. 1975 Nov 28;368(4):309–327. doi: 10.1007/BF00432309. [DOI] [PubMed] [Google Scholar]
  27. Shelanski M. L., Gaskin F., Cantor C. R. Microtubule assembly in the absence of added nucleotides. Proc Natl Acad Sci U S A. 1973 Mar;70(3):765–768. doi: 10.1073/pnas.70.3.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Singh A., Le Marchand Y., Orci L., Jeanrenaud B. Colchicine administration to mice: a metabolic and ultrastructural study. Eur J Clin Invest. 1975 Nov 21;5(6):495–505. doi: 10.1111/j.1365-2362.1975.tb00482.x. [DOI] [PubMed] [Google Scholar]
  29. Stein O., Stein Y. Colchicine-induced inhibition of very low density lipoprotein release by rat liver in vivo. Biochim Biophys Acta. 1973 Apr 13;306(1):142–147. doi: 10.1016/0005-2760(73)90219-1. [DOI] [PubMed] [Google Scholar]
  30. Temple R., Williams J. A., Wilber J. F., Wolff J. Colchicine and hormone secretion. Biochem Biophys Res Commun. 1972 Feb 16;46(3):1454–1461. doi: 10.1016/s0006-291x(72)80140-2. [DOI] [PubMed] [Google Scholar]
  31. Wolff J., Williams J. A. The role of microtubles and microfilaments in thyroid secretion. Recent Prog Horm Res. 1973;29:229–285. doi: 10.1016/b978-0-12-571129-6.50010-5. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES