Skip to main content
Log in

The effect of feeding on the secretion of pepsin, trypsin and chymotrypsin in the Atlantic salmon,Salmo salar L

  • Published:
Fish Physiology and Biochemistry Aims and scope Submit manuscript

Abstract

Pepsin stored in the stomach mucosa of the Atlantic salmon (Salmo salar L.) increases within two days of the onset of starvation. Trypsin and chymotrypsin in the pyloric caeca/pancreas behave similarly, indicating that when no food is present in the gut, digestive enzymes accumulate in the secretory tissues. As a corollary, trypsin and chymotrypsin activities in the gut contents fell during starvation, indicating that secretion is greatly reduced when food is not present. At the onset of feeding, pepsin is rapidly synthesised in the mucosal tissues and then secreted. Twenty four hours after feeding, the pepsin levels of the mucosa are still low, suggesting that synthesis may be a rapid response to the presence of food in the stomach. Secretion of trypsin and chymotrypsin appears to take place as soon as digesta enters the intestine, between 4 and 14h after feeding, and resynthesis of enzyme precursors appears to be complete again within a further 11h. It is suggested that both synthesis and release may be under the control of cholecystokinin.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References cited

  • Alcon, E. and Bdolah, A. 1975. Increase of proteolytic activity and synthetic capacity of the pancreas in snakes after feeding. Comp. Biochem. Physiol. 50A: 627–631.

    Google Scholar 

  • Brock, F.M., Forsberg, C.W. and Buchanan-Smith, J.G. 1982. Proteolytic activity of rumen microorganisms and effects of proteinase inhibitors. Appl. Env. Microbiol. 44: 561–569.

    Google Scholar 

  • Buddington, R.K. and Doroshov, S.I. 1986. Digestive enzyme complement of white sturgeon (Acipenser transmontanus). Comp. Biochem. Physiol. 83A: 561–567.

    Google Scholar 

  • Case, R.M. 1978. Synthesis, intracellular transport and discharge of exportable proteins in the pancreatic acinar cell and other cells. Biol. Rev. 53: 211–354.

    Google Scholar 

  • Charney, J. and Tomarelli, R.M. 1947. A colorimetric method for the determination of the proteolytic activity of the duodenal juice. J. Biol. Chem. 171: 501–505.

    Google Scholar 

  • Crawley, J.N. and Corwin, R.L. 1994. Biological actions of chelecystokinin. Peptides 15: 731–755.

    Google Scholar 

  • Del Mar, E.G., Largman, C., Brodrick, J.W. and Geokas, M.C. 1979. A sensitive new substrate for chymotrypsin. Anal. Biolchem. 99: 316–320.

    Google Scholar 

  • Dockray, G.J. 1989. The integrative functions of CCK in the upper gastrointestinal tract.In The Neuropeptide Cholecystokinin (CCK): Anatomy and Biochemistry, Receptors, Pharmacology, and Physiology. pp 232–239. Edited by J. Hughes, G. Dockray, G. Woodruff. Ellis Horwood Ltd. Chichester.

    Google Scholar 

  • Einarsson, S. 1994. Proteases in the Atlantic salmon,Salmo salar L. Physiological and biological aspects. Ph.D. Thesis, University of Glasgow, Scotland.

    Google Scholar 

  • Einarsson, S. and Davies, P.S. 1996. On the localisation and ultrastructure of pepsinogen, trypsinogen and chymotrypsinogen secreting cells in the Atlantic salmon,Salmo salar L. Comp. Biochem. Physiol. (In Press).

  • Erlanger, B.F., Kokowsky, N. and Cohen, W. 1961. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95: 271–278.

    Google Scholar 

  • Girard-Globa, A., Bourdel, G. and Lardeux, B. 1980. Regulation of protein synthesis and enzyme accumulation in the rat pancreas by amount and timing of dietary protein. J. Nutr. 110: 1380–1390.

    Google Scholar 

  • Holmgren, S., Grove, D.J. and Nilsson, S. 1985. Substance P acts by releasing 5-hydroxytryptamine from enteric neurons in the stomach of the rainbow trout,Salmo gairdneri. Neuroscience 14: 683–693.

    Google Scholar 

  • Holstein, B. and Cederberg, C. 1984. Effect of 5-HT on basal and stimulated secretions of acid and pepsin and on gastric volume outflow in thein vivo gastrically and intestinally perfused cod,Gadus morhua. Agents and Actions 15: 290–305.

    Google Scholar 

  • Holstein, B. and Cederberg, C. 1986. Effects of tachykinins on gastric acid and pepsin secretion and on gastric outflow in the Atlantic cod,Gadus morhua. Am. J. Physiol. 250: G309-G315.

    Google Scholar 

  • Johnson, W.C. and Lindsay, A.J. 1939. An improved universal buffer. Analyst, Lond. 64: 490–492.

    Google Scholar 

  • Onishi, T., Murayama, S. and Takeuchi, M. 1973. Sequence of digestive enzyme levels in carp after feeding-II. Bull. Tokai Reg. Fish. Res. Lab. 75: 33–38.

    Google Scholar 

  • Overnell, J. 1973. Digestive enzymes of the pyloric caeca and their associated mesenteries in the cod (Gadus morhua). Comp. Biochem. Physiol. 46B: 519–531.

    Google Scholar 

  • Pilz, J. and Plantikow, H. 1992. Sterile isolation and long-term culture of exocrine cells from the pancreas of pike (Esox lucius L.): Influence of culture media and hormone CCK/PZ.In Fish in Exotoxicology and Ecophysiology, pp. 1–19. Edited by Th. Braunbeck, W. Hanke and H. Segner. VCH Verlag Chemie, Weineim.

    Google Scholar 

  • Poort, C. and Geuze, J.J. 1969. The effect of temperature elevation and feeding on the pancreas ofRana esculenta in late winter. A biochemical and ultrastructural study. Z. Zellfors. Mikros. Anat. 98: 1–8.

    Google Scholar 

  • Pringle, G.M., Houlihan, D.F., Callanan, K.R., Mitchell, A.I., Raynard, R.S. and Houghton, G.H. 1992. Digestive enzyme levels and histopathology of pancreas disease in farmed Atlantic salmon (Salmo salar). Comp. Biochem. Physiol. 102A: 759–768.

    Google Scholar 

  • Reggio, H., Cailla-Deckmyn, H. and Marchis-Moureen, G. 1971. Effect of pancreozymin on rat pancreatic enzyme biosynthesis. J. Cell Biol. 50: 333–343.

    Google Scholar 

  • Smit, H. 1967. Influence of temperature on the rate of gastric juice secretion in the brown bullhead,Ictalurus nebulosus. Comp. Biochem. Physiol. 21: 125–132.

    Google Scholar 

  • Tomarelli, R.M., Charney, J. and Harding, M.L. 1949. The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity. J. Lab. Clin. Med. 34: 428–433.

    Google Scholar 

  • Van Venrooij, W.J. and Poort, C. 1971. Rate of protein synthesis and polyribosome formation in the frog pancreas after fasting and feeding. Biochim. Biophys. Acta 247: 46470.

    Google Scholar 

  • Yoshinaka, R., Sato, M. and Ikeda, S. 1981a. Distribution of trypsin and chymotrypsin and their zymogens in digestive system of catfish. Bull. Jap. Soc. Sci. Fish. 47: 1615–1618.

    Google Scholar 

  • Yoshinaka, R., Sato, M. and Ikeda, S. 1981b.In vitro activation of trypsinogen and chymotrypsinogen in the pancreas of catfish. Bull. Jap. Soc. Sci. Fish. 47: 1473–1478.

    Google Scholar 

  • Yoshinaka, R., Sato, M., Sato, T. and Ikeda, S. 1984. Distribution of trypsin and chymotrypsin, and their zymogens in digestive organs of eel (Anguilla japonica). Comp. Biochem. Physiol. 78B: 569–573.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Einarsson, S., Davies, P.S. & Talbot, C. The effect of feeding on the secretion of pepsin, trypsin and chymotrypsin in the Atlantic salmon,Salmo salar L. Fish Physiol Biochem 15, 439–446 (1996). https://doi.org/10.1007/BF01875587

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01875587

Keywords

Navigation