Effects of inverse changes in dietary lipid and carbohydrate on the synthesis of some pancreatic secretory proteins
- 1 January 1987
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 162 (1) , 25-30
- https://doi.org/10.1111/j.1432-1033.1987.tb10536.x
Abstract
The effect of ingesting isocaloric and isonitrogenous diets with increasing amounts of lipid (9-30%) and consequently decreasing amounts of carbohydrates (68.7-1.25%) on the exocrine pancreas was studied in adult male Wistar rats. Pancreatic contents of chymotrypsin, lipase and colipase activity, as well as syntehsis of amylase, lipase, procarboxypeptidases and individual serine proteases were examined. Lipid-free diets and diets containing 1% lipid were found to have little effect on pancreatic proteins as compared with lipid-rich diets were two distinct patterns of response were observed. Ingestion of diets containing 3-20% lipid resulted in a progressive increase in the activity of lipase, colipase and chymotrypsin up to 2-fold in the first case and 1.6-fold in the two other cases when animals were fed the 20% fat diet. Under the latter conditions, the relative synthesis of secretory proteins, as exprssed as percentage of the radioactivity incorporated into individual proteins compared to that incorporated into the total mixture of exocrine proteins, was unchanged for procarboxypeptidases, whereas it was stimulated for lipase (2-fold) and serine proteases (1.6-fold). Amylase relative synthesis progressively decreased as the lipid content of diets increased. Consumption of hyperlipidic diets containing 25% and 30% fat resulted in a further enhancement in the activity of lipase and colipase in the gland in contrast with chymotrypsin activity which was unchanged as compared to the control diet (3% lipid). As far as biosynthesis was concerned, a plateau in the relative synthesis of lipase and serine protease was reached. Amylase relative synthesis further decreased down to 2.2-fold when rats were fed the 30% fat-rich diet whereas that of procarboxypeptidases was markedly increased (about 1.7-fold). Absolute rates of synthesis of total pancreatic secretory proteins, as expressed with regard to the DNA content of the tissue, indicated that biosynthesis of all secretory pancreatic proteins was stimulated by hyperlipidic diets (at least 2-fold with the 30% lipid diet). Consequently, when such an increase was taken into consideration, the absolute synthesis of amylase was found to be unchanged throughout the dietary manipulations, whereas that of lipase, procarboxypeptidases and serine proteases were stimulated by 4.0-fold, 3.4-fold and 3.2-fold, respectively.This publication has 22 references indexed in Scilit:
- Dietary Effects on Pancreatic Exocrine FunctionAnnals of Nutrition and Metabolism, 1981
- Mechanism of compartmentation of secretory proteins: transport of exocrine pancreatic proteins across the microsomal membraneThe Journal of cell biology, 1980
- Adaptation of the lipase-colipase system to dietary lipid content in pig pancreatic tissueAnnales de Biologie Animale Biochimie Biophysique, 1979
- An improved large scale procedure for the purification of porcine pancreatic lipaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Nutritional and circadian variations in lipase activity and colipase saturation in rat pancreasAnnales de Biologie Animale Biochimie Biophysique, 1977
- Determination of protein: A modification of the lowry method that gives a linear photometric responseAnalytical Biochemistry, 1972
- Short-term adaptation of pancreatic hydrolases to nutritional and physiological stimuli in adult ratsBiochimie, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- On chymotrypsinogen and trypsinogen biosynthesis by pancreas of rats fed on a starch-rich or a casein-rich dietBiochemical and Biophysical Research Communications, 1964
- Adaptation of the exocrine secretion of rat pancreas to the composition of the dietBiochemical and Biophysical Research Communications, 1963