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. 1979 Oct;64(4):1097–1102. doi: 10.1172/JCI109548

Site of Substrate Stimulation of Jejunal Sucrase in the Rat

Martin H Ulshen 1,2, Richard J Grand 1,2
PMCID: PMC372221  PMID: 479372

Abstract

To identify the site of stimulation of sucrase by a sucrose diet, changes in sucrase-specific activity of jejunal mucosa were studied after introduction of sucrose diet to carbohydrate-deprived rats. Results were correlated with simultaneous changes in villus gradients of sucrase-specific activity. Simultaneous with the introduction of sucrose diet, [3H]thymidine (100 μCi) was administered intravenously, and rates of cell migration measured during adaptation to the new diet. After a 72-h fast, rats fed sucrose diet for 6, 12, or 18 h showed no change in sucrase-specific activity in either whole mucosa or villus gradients. However, within 18-24 h after starting a sucrose diet, there was a marked rise in whole mucosal sucrase-specific activity above fasting values (99 ± 14 vs. 38 ± 4 μM glucose/min per g protein, P < 0.001) in association with the development of a region of increased activity at the lower villus (154 ± 22 vs. 60 ± 9 μM glucose/min per g protein, P < 0.02, but with no change in villus tip activity (56 ± 5 vs. 46 ± 8 μM glucose/min per g protein). Similar changes were seen in animals fed 24 h of sucrose diet after a 72-h carbohydratefree diet. Fasted animals fed sucrose diet for 36 h had increased sucrase-specific activity at the villus tip (144 ± 11 μM glucose/min per g protein) as well as at the lower villus region, and this pattern persisted at 1 wk of sucrose diet. Maximal activity patterns for isomaltase and maltase paralleled those for sucrase, but the villus gradients for lactase were unaffected by sucrose diet. The region of maximal sucrase-specific activity always coincided with or followed the leading edge of radioactivity as determined by liquid scintillation counting. Therefore, sucrose-mediated changes in sucrase activity of the jejunal mucosa in the rat appear to be initiated at the level of the crypt epithelial cell and are expressed after a latent period of 18-24 h during which these cells mature and migrate toward the villus tip.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BLAIR D. G., YAKIMETS W., TUBA J. Rat intestinal sucrase. II. The effects of rat age and sex and of diet on sucrase activity. Can J Biochem Physiol. 1963 Apr;41:917–929. [PubMed] [Google Scholar]
  2. Deren J. J., Broitman S. A., Zamcheck N. Effect of diet upon intestinal disaccharidases and disaccharide absorption. J Clin Invest. 1967 Feb;46(2):186–195. doi: 10.1172/JCI105521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Doell R. G., Rosen G., Kretchmer N. Immunochemical studies of intestinal disaccharidases during normal and precocious development. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1268–1273. doi: 10.1073/pnas.54.4.1268. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dubs R., Gitzelmann R., Steinmann B., Lindenmann J. Catalytically inactive sucrase antigen of rabbit small intestine: the enzyme precursor. Helv Paediatr Acta. 1975 May;30(1):89–102. [PubMed] [Google Scholar]
  5. Grand R. J., Chong D. A., Isselbacher K. J. Intracellular processing of disaccharidases: the effect of actinomycin D. Biochim Biophys Acta. 1971 Feb 28;261(2):341–352. doi: 10.1016/0304-4165(72)90058-x. [DOI] [PubMed] [Google Scholar]
  6. Grand R. J., Jaksina S. Additional studies on the regulation of carbohydrate-dependent enzymes in the jejunum: changes in amino acid pools, protein synthesis, and the effect of actinomycin-D. Gastroenterology. 1973 Mar;64(3):429–437. [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Levine G. M., Deren J. J., Steiger E., Zinno R. Role of oral intake in maintenance of gut mass and disaccharide activity. Gastroenterology. 1974 Nov;67(5):975–982. [PubMed] [Google Scholar]
  9. McManus J. P., Isselbacher K. J. Effect of fasting versus feeding on the rat small intestine. Morphological, biochemical, and functional differences. Gastroenterology. 1970 Aug;59(2):214–221. [PubMed] [Google Scholar]
  10. Messer M., Dahlqvist A. A one-step ultramicro method for the assay of intestinal disaccharidases. Anal Biochem. 1966 Mar;14(3):376–392. doi: 10.1016/0003-2697(66)90280-6. [DOI] [PubMed] [Google Scholar]
  11. Nordström C., Dahlqvist A., Josefsson L. Quantitative determination of enzymes in different parts of the villi and crypts of rat small intestine. Comparison of alkaline phosphatase, disaccharidases and dipepeptidases. J Histochem Cytochem. 1967 Dec;15(12):713–721. doi: 10.1177/15.12.713. [DOI] [PubMed] [Google Scholar]
  12. Rosensweig N. S., Herman R. H. Control of jejunal sucrase and maltase activity by dietary sucrose or fructose in man. A model for the study of enzyme regulation in man. J Clin Invest. 1968 Oct;47(10):2253–2262. doi: 10.1172/JCI105910. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rosenweig N. S., Herman R. H. Dose response of jejunal sucrase and maltase activities to isocaloric high and low carbohydrate diets in man. Am J Clin Nutr. 1970 Nov;23(11):1373–1377. doi: 10.1093/ajcn/23.11.1373. [DOI] [PubMed] [Google Scholar]
  14. Rosenweig N. S., Herman R. H. Time response of jejunal sucrase and maltase activity to a high sucrose diet in normal man. Gastroenterology. 1969 Mar;56(3):500–505. [PubMed] [Google Scholar]
  15. Steiner M., Bourges H. R., Freedman L. S., Gray S. J. Effect of starvation on the tissue composition of the small intestine in the rat. Am J Physiol. 1968 Jul;215(1):75–77. doi: 10.1152/ajplegacy.1968.215.1.75. [DOI] [PubMed] [Google Scholar]

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