Abstract
The pancreatic lipase and trypsin activities in streptozotocin-induced diabetic rats were determined as well as the relative levels of mRNA coding for these proteins. It was found that after development of diabetes, the activities of pancreatic lipase and trypsin were significantly increased by 105% and 52%, respectively, accompanied by an increase in the levels of lipase and trypsinogen mRNA by 98% and 49%, respectively, while amylase activity and its mRNA were significantly decreased. The alteration of lipase, trypsin, and amylase activities and their mRNA in diabetic rats were all normalized by replacement of insulin. It is concluded that in the diabetic situation, the pretranslational control for pancreatic lipase and trypsinogen is stimulated, resulting in high levels of these enzymes in the diabetic rat.
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References
Williams JA, Goldfine ID: The insulin-pancreatic acinar axis. Diabetes 34:980–986, 1985
Chey WY, Shay H, Shuman CR: External pancreatic secretion in diabetes mellitus. Ann Intern Med 59:812–821, 1963
Söling HD, Unger KO: The role of insulin in the regulation of α-amylase synthesis in the rat pancreas. Eur J Clin Invest 2:199–212, 1972
Domschke W, Tympner F, Domschke S, Demling L: Exocrine pancreatic function in juvenile diabetics. Am J Dig Dis 20:309–312, 1975
Korc M, Owerbach D, Quinto C, Rutter WJ: Pancreatic islet-acinar cell interaction: Amylase messenger RNA levels are determined by insulin. Science 213:351–353, 1981
Bazin R, Lavau M: Diet composition and insulin effect on amylase to lipase ratio in pancreas of diabetic rats. Digestion 19:386–391, 1979
Bendayan M, Grégoire S: Immunohisto- and cytochemical studies of pancreatic enzymes in peri-insular and tele-insular acinar cells of streptozotocin-induced diabetic rats. Pancreas 2:272–282, 1987
Stöckmann F, Söling HD: Regulation of biosynthesis of trypsinogen and chymotrypsinogen by nutritional and hormonal factors in the rats. Eur J Clin Invest 11:121–132, 1981
Snook JT: Effect of diet, adrenalectomy, diabetes and actinomycin D on exocrine pancreas. Am J Physiol 215:1329–1333, 1968
Yokoyama J, Mori Y, Ikeda Y, Nishimura M, Mullen Y: Influence of B-cell impairment on pancreatic acini in NOD mice and streptozotocin-induced diabetic rats. Endocrinol Jpn 35:549–556, 1988
Kerfelec B, LaForge KS, Puigserver A, Scheele G: Primary structures of canine pancreatic lipase and phospholipase A2 messenger RNA. Pancreas 1:430–437, 1986
MacDonald RJ, Stary SJ, Swift GH: Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs. J Biol Chem 257:9724–9732, 1982
Erlanson C, Fernlund P, Borgström B: Purification and characterization of two proteins with colipase activity from porcine pancreas. Biochim Biophys Acta 310:437–445, 1973
Chirgwin JM, Przybyla AE, MacDonald RJ, Rutter WJ: Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294–5299, 1979
Schibler U, Tosi M, Pittet A-C, Fabiani L, Wellaner PK: Tissue-specific expression of mouse α-amylase genes. J Mol Biol 142:93–116, 1980
Rigby PWJ, Dieckmann M, Rhodes C, Berg P: Labeling deoxyribonucleic acid to high specific activityin vitro by nick translation with DNA polymerase I. J Mol Biol 113:237–251, 1977
Ceska M, Birath K: A new rapid method for the clinical determination of alpha-amylase activities in human serum and urine. Optimal conditions. Clin Chim Acta 26:437–444, 1969
Erlanson-Albertsson C, Larsson A, Duan R-D: Secretion of pancreatic lipase and colipase from rat pancreas. Pancreas 2:531–535, 1987
Folkesson HG, Weström BR, Lundin S, Karlsson BW: Decreased passage of the nonapeptide dNAVP over the intestinal epithelium during development in the young rat. Acta Physiol Scand 133:283–288, 1988
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ: Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275, 1951
Wicker C, Puigserver A, Rausch U, Scheele G, Kern H: Multiple-caerulein control of the gene expression of secretory protein in the rat pancreas. Eur J Biochem 151:461–466, 1985
Steinhilber W, Poensben J, Rausch U, Kern HF, Scheele GA: Translational control of anionic trypsinogen and amylase synthesis in rat pancreas in response to caerulein Stimulation. Proc Natl Acad Sci USA 85:6597–6601, 1988
Lahaie RG: Translational control of protein synthesis in isolated pancreatic acini: Role of CCK8, carbachol and insulin. Pancreas 1:403–410, 1986
Renaud W, Giorgi D, Iovanna J, Dagorn J-C: Regulation of concentration of mRNA for amylase, trypsinogen I and chymotrypsinogen B in rat pancreas by secretagogues. Biochem J 235:305–308, 1986
Solomon TE, Peterson H, Elashoff J, Grossman MI: Interaction of caerulein and secretin on pancreatic size and composition in rat. Am J Physiol 235:E714-E719, 1978
Rausch U, Vasiloudes P, Rüdiger K, Kern HF:In-vivo stimulation of rat pancreatic acinar cells by infusion of secretin. II Changes in individual rates of enzyme and isoenzyme biosynthesis. Cell Tissue Res 242:641–644, 1985
Rausch U, Rüdiger K, Vasiloudes P, Kern H, Scheele G: Lipase synthesis in the rat pancreas is regulated by secretin. Pancreas 1:522–528, 1986
Wicker C, Puigserver A: Effects of inverse changes in dietary lipid and carbohydrate on the synthesis of some pancreatic secretory proteins. Eur J Biochem 162:25–30, 1987
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Duan, RD., Poensgen, J., Wicker, C. et al. Increase in pancreatic lipase and trypsin activity and their mRNA levels in streptozotocin-induced diabetic rats. Digest Dis Sci 34, 1243–1248 (1989). https://doi.org/10.1007/BF01537273
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DOI: https://doi.org/10.1007/BF01537273