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Complete tyrosine-O-sulphation of gastrin in neonatal rat pancreas

Nature volume 309, pages 456–458 (1984)Cite this article

Abstract

Modification of tyrosine residues of proteins has attracted great interest. Although phosphorylation has received most attention1–3, tyrosine-O-sulphation is also common4 and has been closely investigated in the hormones gastrin and cholecystokinin (CCK). CCK regulates pancreatic enzyme secretion. It is always sulphated5–9 and sulphation increases its pancreatic secretagogue activity 100-fold10–13. By contrast, only half of gastrin molecules are tyrosine- O-sulphated5–9 and sulphation does not influence the ability of gastrin to regulate gastric acid secretion6. We now report that in neonatal rat pancreas, which is the major source of gastrin in the newborn rat14, gastrin is completely sulphated. Moreover, the disappearance of gastrin from the pancreas during the first weeks after birth parallels the appearance of CCK in the intestine. Since sulphation is essential for pancreatic secretagogue activity of gastrin as well as of CCK10–13, pancreatic gastrin in the neonate may be the equivalent of intestinal CCK in the adult.

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References

  1. Erikson, R. L., Purchio, A. F., Erikson, E., Collett, M. S. & Brugge, J. S. J. Cell Biol. 87, 319–325 (1980).

    Article  CAS  Google Scholar 

  2. Huttner, T. Cell 22, 647–648 (1980).

    Article  Google Scholar 

  3. Ushiro, H. & Cohen, S. J. biol. Chem. 255, 8353–8365 (1980).

    Google Scholar 

  4. Huttner, W. B. Nature 299, 273–276 (1982).

    Article  ADS  CAS  Google Scholar 

  5. Mutt, V. & Jorpes, J. E. Eur. J. Biochem. 6, 156–162 (1969).

    Article  Google Scholar 

  6. Gregory, R. A. & Tracy, H. J. Gut 5, 103–117 (1964).

    Article  CAS  Google Scholar 

  7. Rehfeld, J. F., Stadil, F. & Vikelsøe, J. Gut 15, 102–111 (1974).

    Article  CAS  Google Scholar 

  8. Rehfeld, J. F. & Larsson, L.-I. J. biol. Chem. 256, 10425–10429 (1981).

    Google Scholar 

  9. Andersen, B. N., Magistris, L. de. & Rehfeld, J. F. Clinica chim. Acta 127, 29–39 (1983).

    Article  CAS  Google Scholar 

  10. Mutt, V. in Gastrointestinal Hormones (ed. Glass, W. B. J.) 169–221 (Raven, New York, 1983).

    Google Scholar 

  11. Jensen, R. T., Lemp, G. F. & Gardner, J. D. J. biol Chem. 257, 5554–5559 (1982).

    CAS  PubMed  Google Scholar 

  12. Dockray, G. J. Q. Jl exp. Physiol. 58, 163–169 (1973).

    CAS  Google Scholar 

  13. Jensen, S. L. et al. Am. J. Physiol. 238, E186–192 (1980).

    CAS  PubMed  Google Scholar 

  14. Larsson, L.-I., Rehfeld, J. F., Håkanson, R. & Sundler, F. Nature 262, 609–610 (1976).

    Article  ADS  CAS  Google Scholar 

  15. Rehfeld, J. F., Stadil, F. & Rubin, B. Scand. J. clin. Lab. Invest. 30, 221–232 (1972).

    Article  CAS  Google Scholar 

  16. Rehfeld, J. F., Magistris, L. de & Andersen, B. N. Regul. Peptides 2, 333–342 (1981).

    Article  CAS  Google Scholar 

  17. Rehfeld, J. F. J. biol. Chem. 253, 4016–4021 (1978).

    CAS  PubMed  Google Scholar 

  18. Reeve, J. R. et al. Peptides 2, 453–458 (1981).

    Article  CAS  Google Scholar 

  19. Korc, M., Owerbach, D., Quinto, C. & Rutter, W. J. Science 213, 351–353 (1981).

    Article  ADS  CAS  Google Scholar 

  20. Solomon, T., Petersen, H., Elashoff, J. & Grossman, M. I. Am. J. Physiol. 236, E714–719 (1978).

    Google Scholar 

  21. Pictet, R. & Rutter, W. J. in Handbook of Physiology Sect. 7, Vol. 1 (eds Freinkel, N. & Steiner, D. F.) 25–26 (American Physiological Society, 1972).

    Google Scholar 

  22. Andersen, B. N. & Stadil, F. Regul. Peptides 6, 231–239 (1983).

    Article  CAS  Google Scholar 

  23. Zollinger, R. M. & Coleman, D. W. The Influence of Pancreatic Tumours on the Stomach (Thomas, Springfield, 1974).

    Google Scholar 

  24. Baldwin, G. S. FEBS Lett. 137, 1–5 (1982).

    Article  CAS  Google Scholar 

  25. Bayon, A., Shoemaker, W. J., Bloom, F. E., Mauss, A. & Guilemin, R. Brain Res. 179, 93–101 (1979).

    Article  CAS  Google Scholar 

  26. Haynes, L. W., Smyth, D. G. & Zakarian, S. Brain Res. 232, 115–128 (1981).

    Article  Google Scholar 

  27. Gregory, H., Hardy, P. M., Jones, D. S., Kenner, G. W. & Sheppard, R. C. Nature 204, 931–935 (1964).

    Article  ADS  CAS  Google Scholar 

  28. Schaffmayer, A., Werner, M. & Becker, H. D. Digestion 24, 146–154 (1982).

    Article  Google Scholar 

  29. Baldwin, G. S., Knesel, J. & Monckton, J. M. Nature 301, 435–437 (1983).

    Article  ADS  CAS  Google Scholar 

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  1. S. J. Brand

    Present address: Endocrine Genetics Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, USA

Authors and Affiliations

  1. University Department of Clinical Chemistry, Rigshospitalet, DK-2100, Copenhagen, Denmark

    S. J. Brand, B. N. Andersen & J. F. Rehfeld

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  2. B. N. Andersen
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  3. J. F. Rehfeld
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Brand, S., Andersen, B. & Rehfeld, J. Complete tyrosine-O-sulphation of gastrin in neonatal rat pancreas. Nature 309, 456–458 (1984). https://doi.org/10.1038/309456a0

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