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.
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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.
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.
Buddington, R.K. and Doroshov, S.I. 1986. Digestive enzyme complement of white sturgeon (Acipenser transmontanus). Comp. Biochem. Physiol. 83A: 561–567.
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.
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.
Crawley, J.N. and Corwin, R.L. 1994. Biological actions of chelecystokinin. Peptides 15: 731–755.
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.
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.
Einarsson, S. 1994. Proteases in the Atlantic salmon,Salmo salar L. Physiological and biological aspects. Ph.D. Thesis, University of Glasgow, Scotland.
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.
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.
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.
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.
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.
Johnson, W.C. and Lindsay, A.J. 1939. An improved universal buffer. Analyst, Lond. 64: 490–492.
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.
Overnell, J. 1973. Digestive enzymes of the pyloric caeca and their associated mesenteries in the cod (Gadus morhua). Comp. Biochem. Physiol. 46B: 519–531.
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.
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.
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.
Reggio, H., Cailla-Deckmyn, H. and Marchis-Moureen, G. 1971. Effect of pancreozymin on rat pancreatic enzyme biosynthesis. J. Cell Biol. 50: 333–343.
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.
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.
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.
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.
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.
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.
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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
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DOI: https://doi.org/10.1007/BF01875587