Summary
The effect of starvation for 3, 5, or 7 d on body weight, fat stores, pancreatic weight, and enzyme composition was studied in 300 g rats and was compared with a. 3-d fast in 200 g rats. In the 300 g animals, fasting led to a gradual hypotrophy of the pancreas with a marked, continuous decrease in amylase content. Pancreatic lipase, trypsinogen, chymotrypsinogen, proelastase, and secretory trypsin inhibitor contents increased temporarily, but by d 7, they declined to about the initial values. This decline in enzyme levels coincided with the exhaustion of fat stores. The decrease in amylase content could be related to decreases in circulating insulin levels, whereas the temporary increase in lipase content may be owing to changes in plasma free fatty acid concentrations. In 200 g rats, starvation for 3 d led to exhaustion of fat stores that was accompanied by greater losses of pancreatic weight, protein, and amylase contents. In addition, the levels of trypsinogen and chymotrypsinogen decreased and lipase was unchanged. These findings indicate that during starvation, changes in pancreatic secretory enzymes are time-dependent and vary with the age, body weight, and/or adipose tissue mass of the rats.
Similar content being viewed by others
References
Webster PD, Singh M, Tucker PC, and Black O. Effect of fasting and feeding on the pancreas. Gastroenterology 1962; 62: 600–605.
Mainz DL, Parks NM, and Webster PD. Effect of fasting and refeeding on pancreatic DNA synthesis and content. Proc Soc Exp Biol Med 1977; 156: 340–344.
Morisset JA and Webster PD. Effects of fasting and feeding on protein synthesis by the rat pancreas. J Clin Invest 1972; 51: 1–8.
Fölsch UR, Dreessen UW, Talaulicar M, Willms B, and Creutzfeldt W. Effect of long-term fasting of obese patients on pancreatic exocrine function, gastrointestinal hormones and bicarbonate concentration. Z Gastroenterol 1984; 22: 357–364.
Deschodt-Lanckman M, Robberecht P, Camus J, and Christophe J. Short-term adaptation of pancreatic hydrolases to nutritional and physiological stimuli in adult rats. Biochimie 1971; 53: 789–796.
Lee PC, Brooks S, and Lebenthal E. Effect of fasting and refeeding on pancreatic enzymes and secretagogue responsiveness in rats. Am J Physiol 1982; 242: G215-G221.
Viera-Matos AN and Tenenhouse A. The effect of fasting on the in vitro synthesis of amylase in rat exocrine pancreas. Can J Physiol Pharmacol 1977; 55: 90–97.
Bazin R, Lavau M, and Herzog J. Pancreatic lipase and ketogenic conditions. Biomedicine 1978; 28: 160–165.
StöckmannF and Söling HD. Regulation of biosynthesis of trypsinogen and chymotrypsinogen by nutritional and hormonal factors in the rat. Eur J Clin Invest 1981; 11: 121–132.
Goodman MN and Ruderman NB. Starvation in the rat. I. Effect of age and obesity on organ weights, RNA, DNA, and protein. Am J Physiol 1980; 239: E269-E276.
Goodman MN, Reed Larsen P, Kaplan MM, Aoki TT, Young VR, and Ruderman NB. Starvation in the rat. II. Effect of age and obesity on protein sparing and fuel metabolism. Am J Physiol 1980; 239: E277-E286.
Solomon TE. Regulation of exocrine pancreatic cell proliferation and enzyme synthesis. Johnson LR, Ed. Physiology of the Gastrointestinal Tract, Raven, New York, 1981; 873–892.
Peckman SC, Entenman C, and Carroll HW. The influence of a hypercaloric diet on gross body and adipose tissue composition in the rat. J Nutr 1962; 77: 187–197.
Schneider WC. Determination of nucleic acids in tissues by pentose analysis. Methods Enzymol 1957; 3: 680–684.
Giles KW and Myers A. An improved diphenylamine method for the estimation of deoxyribonucleic acid. Nature (London) 1965; 206: 93.
Fritz H, Trautschold I, and Werle E. Protease inhibitors. Bergmeyer HU, Ed. Methods of Enzymatic Analysis, vol. 2, 2nd edition, Verlag Chemie, Weinheim, Academic, New York 1974; 1064–1080.
Ceska M, Brown B, and Birath K. A new rapid method for the clinical determination of alpha-amylase activities in human serum and urine. Optimal conditions. Clin Chim Acta 1969; 26: 437–444.
HoneggerJ and Hadorn B. The determination of lipase activity in human duodenal juice. Biol Gastroenterol 1973; 6: 217–223.
Solomon TE, Petersen H, Elashoff J, and Grossman MT. Interaction of caerulein and secretin on pancreatic size and composition in rat. Am J Physiol 1978; 235: E714-E719.
Dagorn JC. Nonparallel enzyme secretion from rat pancreas: in vivo studies. J Physiol (London) 1978; 280: 435–448.
Erlanger BF, Kokowsky W, and Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 1961; 95: 271–278.
Bundy HF. Chymotrypsin-catalyzed hydrolysis of N-acetyl- and N-benzoyl-L-tyrosine p-nitroanilides. Arch Biochem Biophys 1963; 102: 416–422.
Bieth J, Spiess B, and Wermuth CG. The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem Med 1974; 11: 350–357.
Goa J. Micro biuret method for protein determination; determination of total protein in cerebrospinal fluid. Scand J Clin Lab Invest 1953; 5: 218–222.
HyvärinenA and Nikkilä EA. Specific determination of blood glucose with o-toluidine. Clin Chim Acta 1962; 7: 140–144.
Novak M. Colorimetric ultramicro method for the determination of free fatty acids. J Lipid Res 1965; 6: 431–433.
Grimm H. Analysis of variance. Delaunois AL, Ed. Biostatistics in Pharmacology, vol. 2, Pergamon Press, Oxford, 1973; 675–716.
Palla JC, Ben Abdeljlil A, and Desnuelle P. Action de l’insuline sur la biosynthese de l’amylase et de quelques autres enzymes du pancreas de rat. Biochim Biophys Acta 1968; 158: 25–35.
Lavau M, Bazin R, and Herzog J. Comparative effects of oral and parenteral feeding on pancreatic enzymes in the rat. J Nutr 1974; 104: 1432–1437.
Korc M, Owerbach D, Quinto C, and Rutter WJ. Pancreatic islet-acinar cell interaction: amylase messenger RNA levels are determined by insulin. Science 1981; 213: 351–353.
Goldfine ID and Williams JA. Receptors for insulin and CCK in the acinar pancreas: relationship to hormone action. Int Rev Cytol 1983; 85: 1–38.
BazinR and Lavau M. Diet composition and insulin effect on amylase to lipase ratio in pancreas of diabetic rats. Digestion 1979; 19: 386–391.
Mlekusch W, Paletta B, Truppe W, Paschke E, and Grimus R. Plasma concentrations of glucose, corticosterone, glucagon and insulin and liver content of metabolic substrates and enzymes during starvation and additional hypoxia in the rat. Horm Metab Res 1981; 13: 612–614.
Danielsson A. Effects of nutritional state and administration of glucose, glibenclamide or diazoxide on the storage of amylase in mouse pancreas. Digestion 1974; 10: 150–161.
Saudek CD and Felig P. The metabolic events of starvation. Am J Med 1976; 60: 117- 126.
Parilla R. Flux of metabolic fuels during starvation in the rat. Pflügers Arch 1978; 374: 3–7.
Schick J, Kern H, and Scheele G. Hormonal stimulation in the exocrine pancreas results in coordinate and anticoordinate regulation of protein synthesis. J Cell Biol 1984; 99: 1569–1574.
Liddle RA, Goldfine ID, and Williams JA. Bioassay of plasma cholecystokinin in rats: effects of food, trypsin inhibitor, and alcohol. Gastroenterology 1984; 87: 542–549.
Schick J, Verspohl R, Kern H, and Scheele G. Two distinct adaptive responses in the synthesis of exocrine pancreatic enzymes to inverse changes in protein and carbohydrate in the diet. Am J Physiol 1984; 247: 6611–6616.
Marks WH and Ohlsson K. Isolation and partial characterization of the pancreatic secretory trypsin inhibitor in the rat. Biochim Biophys Acta 1982; 717: 91–97.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Nagy, I., Pap, Á. & Varró, V. Time-course of changes in pancreatic size and enzyme composition in rats during starvation. Int J Pancreatol 5, 35–45 (1989). https://doi.org/10.1007/BF02925696
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02925696