Measurement of Glucose Absorption

Living reference work entry

Abstract

Starch as the predominant ingredient of human food is rapidly degraded in the gastrointestinal tract by salivary and pancreatic α-amylase to maltose which is further hydrolyzed by maltase localized in the brush border of the small intestine to glucose. Glucose is immediately absorbed leading to hyperglycemia and consequently to hyperinsulinemia. Both phenomena are undesirable in diabetics and in obese patients. The inhibition of the digestion of starch leads to a decrease and a retardation of glucose absorption. In nature, α-amylase inhibitors are found in wheat and other grains (Shainkin and Birk 1970). Several inhibitors of amylase and α-glucosidase have been developed (Bischoff 1991). Animal experiments with high doses of absorbable α-glucosidase inhibitors indicate that lysosomal storage of glycogen may occur (Lembcke et al. 1991).

Keywords

Jejunal Loop Luminal Perfusate Intestinal Glucose Absorption Gold Thioglucose Intestinal Disaccharidase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References and Further Reading

Inhibition of Polysaccharide-Degrading Enzymes

  1. Bischoff H (1991) Wirkung von Acarbose auf diabetische Spätkomplikationen und Risikofaktoren – Neue tierexperimentelle Ergebnisse. Aktuelle Endokrinologie Stoffwechel 12:25–32Google Scholar
  2. Bischoff H (1994) Pharmacology of α-glucosidase inhibition. Eur J Clin Invest 24(Suppl 3):3–10PubMedGoogle Scholar
  3. Bischoff H, Puls W, Krause HP, Schutt H, Thomas G (1985) Pharmacological properties of the novel glucosidase inhibitors BAYM1099 (Miglitol) and BAY O 1248. Diabetes Res Clin Pract 8(Suppl 1):S53Google Scholar
  4. Lembcke B, Lamberts R, Creutzfeldt W (1991) Lysosomal storage of glycogen as a sequel of α-glucosidase inhibition by the absorbed deoxynojirimycin derivative emiglitate (BAYo1248). A drug-induced pattern of hepatic glycogen storage mimicking Pompe’s disease (glycogenosis type II). Res Exp Med 191:389–404CrossRefGoogle Scholar
  5. Shainkin R, Birk Y (1970) α-Amylase inhibitors from wheat. Isolation and characterization. Biochim Biophys Acta 221:502–513PubMedCrossRefGoogle Scholar

Assay for α-Amylase

  1. Rick W, Stegbauer HP (1970) α-Amylase. Messung der reduzierenden Gruppen. In: Bergmeyer H (ed) Methoden der enzymatischen Analyse, vol II, 2nd ed., Wiley VCH Verlag Chemie, Weinheim, Germany, pp 848–853Google Scholar

Assay for α-Glucosidase

  1. Dahlqvist A (1964) Method for assay of intestinal disaccharidases. Anal Biochem 7:18–25PubMedCrossRefGoogle Scholar
  2. Glick Z, Bray GA (1983) Effects of acarbose on food intake, body weight and fat depots in lean and obese rats. Pharmacol Biochem Behav 19:71–78PubMedCrossRefGoogle Scholar
  3. Ikeda H, Odaka H, Matsuo T (1991) Effect of a disaccharidase inhibitor, AO-128, on a high sucrose-diet-induced hyperglycemia in female Wistar fatty rats. Jpn Pharmacol Ther 19:155–150Google Scholar
  4. Matsuo T, Odaka H, Ikeda H (1992a) Effect of an intestinal disaccharidase inhibitor (AO-128) on obesity and diabetes. Am J Clin Nutr 55(Suppl 1):314S–317SPubMedGoogle Scholar

Everted Sac Technique for Assaying α-Glucosidase

  1. Madar Z (1983) Demonstration of amino acid and glucose transport in chicken small intestine everted sac as a student laboratory exercise. Biochem Educ 11:9–11CrossRefGoogle Scholar
  2. Madar Z, Omusky Z (1991a) Inhibition of intestinal α-glucosidase activity and postprandial hyperglycemia by α-glucosidase inhibitors in fa/fa rats. Nutr Res 11:1035–1046CrossRefGoogle Scholar
  3. Lembcke B, Fölsch UR, Creutzfeldt W (1985) Effect of 1-desoxynojirimycin derivatives on small intestinal disaccharidase activities and on active transport in vitro. Digestion 31:120–127PubMedCrossRefGoogle Scholar

Evaluation of Glucose Absorption In vivo

  1. Au A, Gupta A, Schembri P, Cheeseman CI (2002) Rapid insertion of GLUT2 into the rat jejunal brush-border membrane promoted by glucagon-like peptide 2. Biochem J 367:247–254PubMedCentralPubMedCrossRefGoogle Scholar
  2. Boyd CA, Parsons DS (1979) Movements of monosaccharides between blood and tissues of vascularly perfused small intestine. J Physiol 287:371–391PubMedCentralPubMedCrossRefGoogle Scholar
  3. Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72:248–254PubMedCrossRefGoogle Scholar
  4. Cheeseman CI (2002) Intestinal hexose absorption: transcellular or paracellular fluxes. J Physiol 544:336PubMedCentralPubMedCrossRefGoogle Scholar
  5. Corpe CP, Basaleh MM, Affleck J, Gould GW, Jess TJ, Kellett GL (1996) The regulation of GLUT5 and GLUT2 activity in the adaptation of intestinal brush-border fructose transport in diabetes. Pfluglers Arch Eur J Physiol 432:192–201CrossRefGoogle Scholar
  6. Czaky TZ, Fischer E (1981) Intestinal sugar transport in experimental diabetes. Diabetes 30:568–574CrossRefGoogle Scholar
  7. Debnam ES, Ebrahim HY, Swaine DJ (1990) Diabetes mellitus and sugar transport across the brush border and basolateral membranes of rat jejunal enterocytes. J Physiol 424:13–25PubMedCentralPubMedCrossRefGoogle Scholar
  8. Ferraris RP (2001) Dietary and developmental regulation of intestinal sugar transport. Biochem J 360:265–276PubMedCentralPubMedCrossRefGoogle Scholar
  9. Hediger MA, Coady MJ, Ikeda TS, Wright EM (1987) Expression cloning and sequencing of the Na+/glucose cotransporter. Nature 330:379–381PubMedCrossRefGoogle Scholar
  10. HelliweU PA, Richardson M, Affleck J, Kellett GL (2000) Stimulation of fructose transport across the intestinal brush-border membrane by PMA is mediated by GLUT2 and dynamically regulated by protein kinase C. Biochem J 350:149–154CrossRefGoogle Scholar
  11. Hirsh AJ, Cheeseman CI (1998) Cholecystokinin decreases intestinal hexose absorption by a parallel reduction in SGLT1 abundance in the brush-border membrane. J Biol Chem 273:14545–14549PubMedCrossRefGoogle Scholar
  12. Kellett GL, Brot-Laroche E (2005) Apical GLUT2, A major pathway of intestinal sugar absorption. Diabetes 54:3056–3062PubMedCrossRefGoogle Scholar
  13. Kellett GL, Helliwell PA (2000) The diffusive component of intestinal glucose absorption is mediated by the glucose-induced recruitment of GLUT2 to the brush border membrane. Biochem J 350:155–162PubMedCentralPubMedCrossRefGoogle Scholar
  14. Le Marchand-Brustel Y, Rochet N, Grémeaux T, Marot I, Van Obberghen E (1990) Effect of an a-glycosidase inhibitor on experimentally induced obesity in mice. Diabetologia 33:24–30PubMedCrossRefGoogle Scholar
  15. Madar Z, Omusky Z (1991b) Inhibition of intestinal α-glucosidase activity and postprandial hyperglycemia by α-glucosidase inhibitors in fa/fa rats. Nutr Res 11:1035–1046CrossRefGoogle Scholar
  16. Maenz DD, Cheeseman CI (1986) Effect of hyperglycemia on D-glucose transport across the brush-border and basolateral membrane of rat small intestine. Biochim Biophys Acta 860:277–285PubMedCrossRefGoogle Scholar
  17. Matsuo T, Odaka H, Ikeda H (1992b) Effect of an intestinal disaccharidase inhibitor (AO-128) on obesity and diabetes. Am J Clin Nutr 55(Suppl 1):314S–317SPubMedGoogle Scholar
  18. Okada H, Shino A, Ikeda H, Matsuo T (1992) Anti-obesity and antidiabetic actions of a new potent disaccharidase inhibitor in genetically obese-diabetic mice, KKAy. J Nutr Sci Vitaminol 38:27–37Google Scholar
  19. Puls W, Keup U (1973) Influence of an α-amylase inhibitor (BAY d 7791) on blood glucose, serum insulin and NEFA in starch loading tests in rats, dogs and man. Diabetologia 9:97–101PubMedCrossRefGoogle Scholar
  20. Puls W, Keup U, Krause HP, Thomas G, Hoffmeister F (1977) Glucosidase inhibition. A new approach to the treatment of diabetes, obesity, and hyperlipoproteinaemia. Naturwissenchaftliche 64:536–537CrossRefGoogle Scholar
  21. Sharp PA, Debnam ES (1994) The role of cyclic AMP in the control of sugar transport across the brush-border and basolateral membranes of rat jejunal enterocytes. Exp Physiol 70:203–214CrossRefGoogle Scholar
  22. Takami K, Okada H, Tsukuda R, Matsuo T (1991) Antidiabetic actions of a disaccharidase inhibitor, AO-128, in spontaneously diabetic (GK) rats. Jpn J Pharmacol Ther 19:161–171Google Scholar
  23. Thomson AB (1981) Uptake of glucose into the intestine of diabetic rats: effects of variations in the effective resistance of the unstirred water layer. Diabetes 30:247–255PubMedCrossRefGoogle Scholar
  24. Thorens B, Cheng ZQ, Brown D, Lodish HF (1990) Liver glucose transporter: a basolateral protein in hepatocytes and intestine and kidney cells. Am J Physiol 259:C279–C285PubMedGoogle Scholar
  25. Walker J, Jijon HB, Diaz H, Salehi P, Churchill T, Madsen KL (2005) 5-Aminoimidazole-4-carboxamide riboside (AICAR) enhances GLUT2-dependent jejunal glucose transport: a possible role for AMPK. Biochem J 385:485–491PubMedCentralPubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Helmholtz Center Munich, Institute for Diabetes and ObesityMunichGermany

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