Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Effect of a low-molecular weight serine proteinase inhibitor (camostate) on amylase release from isolated pancreatic acini

  • 19 Accesses

  • 3 Citations

Summary

Oral administration of the proteinase inhibitor camostate to rats results in a characteristic regulation of pancreatic enzyme synthesis and release. These effects are thought to be mediated by an endogenous cholecystokinin release in answer to camostate feeding. An additional direct effect of the compound could be exerted directly on the acinar cell. We evaluated in the present study whether the acute or chronic influence of camostate alters the basal or cerulein-stimulated enzyme release from isolated rat acini.

Neither basal nor cerulein-induced (10−12 to 10−8 M) amylase release from acini of non-pretreated donor rats were influenced in the presence of 5, 50, or 500 µM camostate. After oral feeding of camostate (200 mg/kg b.wt. daily) over 5 days pancreatic growth occurred. In experiments with acini obtained from the camostate-pretreated rats highly significant reductions of the cerulein-induced amylase release were found as compared to controls. Our findings exclude a direct effect of camostate on the secretory process of pancreatic acinar cells. However, after repeated oral pretreatment of donor rats a “desensitization” of acini against cerulein stimulation occurs. This latter effect is ascribed to elevated endogenous cholecystokinin which was released in response to camostate feeding.

This is a preview of subscription content, log in to check access.

References

  1. 1.

    Adler G, Rausch U, Weidenbach F, Arnold R, Kern HF (1984) General and selective inhibition of pancreatic enzyme discharge using a proteinase inhibitor (FOY 305) Klin Wochenschr 62:406–411

  2. 2.

    Beckh K, Göke B, Müller R, Arnold R (1987) Elimination of the low-molecular weight proteinase inhibitor camostate (FOY 305) and its degradation products by the rat liver. Res Exp Med 187:401–406

  3. 3.

    Göke B, Fenchel K, Knobloch S, Arnold R, Adler G (1988) Increased CCK-response to proteinase inhibitor feeding after induction of pancreatic hypertrophy in rats. Pancreas 3:576–579

  4. 4.

    Göke B, Printz H, Koop I, Rausch U, Richter G, Arnold R, Adler G (1986) Endogenous CCK-release and pancreatic growth in rats after feeding a proteinase inhibitor (camostate) Pancreas 1:509–515

  5. 5.

    Keim V, Göke B (1986) Pancreatic secretion in the rat influenced by the low-molecular weight serine proteinase inhibitor gabexate mesilate. Eur J Clin Invest 16:519–525

  6. 6.

    Keim V, Göke B, Adler G (1988) Changes in pattern of enzyme secretion by rat pancreas during repeated trypsin inhibitor treatment. Am J Physiol 255:G236-G241

  7. 7.

    Leung YK, Lee PC, Lebenthal E (1986) Maturation of cholecystokinin receptors in pancreatic acini of rat. Am J Physiol 250:G 594–597

  8. 8.

    Otsuki M, Ohki A, Okabayashi Y, Suehiro I, Baba S (1987) Effect of synthetic protease inhibitor camostate on pancreatic exocrine function in rats. Pancreas 2:164–169

  9. 9.

    Otsuki M, Okabayashi Y, Ohki A, Hootman SR, Baba S, Williams JA (1984) Amylase secretion by isolated pancreatic acini after acute cholecystokinin treatment in vivo. Am J Physiol 246:G 419–425

  10. 10.

    Otsuki M, Williams JA (1983) Amylase secretion by isolated pancreatic acini after chronic cholecystokinin treatment in vivo. Am J Physiol 244:G 683–688

  11. 11.

    Stöckmann F, Göke B, Otto J, Lankisch PG, Creutzfeldt W (1984) Der Einfluß von FOY 305 auf Aktivität und Sekretion von Pankreasenzymen in vitro. Z Gastroenterol 22:311–317

  12. 12.

    Williams JA (1987) Role of receptors in mediating trophic stimuli in the pancreas. Gut 28:45–49 (S1)

  13. 13.

    Williams JA, Korc M, Dormer RC (1978) Action of secretagogues on a new preparation of functionally intact, isolated pancreatic acini. Am J Physiol 235:E 517–524

Download references

Author information

Correspondence to B. Göke.

Additional information

Supported in part by a grant from the Deutsche Forschungsgemeinschaft (Go 417/2-1) which is gratefully acknowledged. The results are part of the doctoral thesis of J. Leferink

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Göke, B., Leferink, J., Göke, R. et al. Effect of a low-molecular weight serine proteinase inhibitor (camostate) on amylase release from isolated pancreatic acini. Res. Exp. Med. 189, 33–38 (1989). https://doi.org/10.1007/BF01856026

Download citation

Key words

  • Camostate
  • Pancreatic acini
  • Amylase secretion