Chestnut astringent skin extract, an α-amylase inhibitor, retards carbohydrate absorption in rats and humans

Journal of Nutritional Science and Vitaminology

Volumn 54, Issue 1, 2008, Pages 82-88

  Tsujita, Takahiro ^a   Takaku, Takeshi ^a   Suzuki, Tsuneo ^b  

^a EHIME UNIVERSITY   (Japan)

^b Genki Plaza Medical Center for Healthcare ^*  (Japan)

Author keywords

Amylase inhibitor; Blood glucose; Chestnut astringent skin; Oral carbohydrate tolerance test

Indexed keywords

AESCULUS HIPPOCASTANUM EXTRACT; AMYLASE INHIBITOR; ASTRINGENT AGENT; CARBOHYDRATE; GLUCOSE; INSULIN; STARCH;

ADULT; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CARBOHYDRATE ABSORPTION; CHESTNUT; CONTROLLED STUDY; DOSE RESPONSE; DRUG EFFECT; DRUG INHIBITION; FATTY ACID BLOOD LEVEL; FEMALE; GLUCOSE BLOOD LEVEL; HUMAN; HYPERGLYCEMIA; INSULIN BLOOD LEVEL; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; NORMAL HUMAN; RAT;

ADULT; ALPHA-AMYLASE; ANIMALS; BLOOD GLUCOSE; DIABETES MELLITUS, EXPERIMENTAL; DIABETES MELLITUS, TYPE 2; DIETARY CARBOHYDRATES; DISEASE MODELS, ANIMAL; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; FEMALE; HUMANS; HYPERGLYCEMIA; INTESTINAL ABSORPTION; MALE; MIDDLE AGED; NUTS; PHYTOTHERAPY; PLANT EXTRACTS; POSTPRANDIAL PERIOD; RATS; RATS, WISTAR; SWINE; TREES;

RATTUS; SUS; ZEA MAYS;

EID: 40949146199     PISSN: 03014800     EISSN: 18817742     Source Type: Journal    
DOI: 10.3177/jnsv.54.82     Document Type: Article

References (27)

1. Zimmer P, Alberti KG, Shaw J. 2001. Global and societal implications of the diabetes epidemic. Nature 414: 782-787.
2. King H, Aubert RE, Herman WH. 1998. Global burden of diabetes, 1995-2025; prevalence, numerical estimates, and projections. Diabetes Care 21: 1414-1431.
3. Felber JP, Golay A. 2002. Pathways from obesity to diabetes. Int J Obes Metab Disord 26: S39-S45.
4. Yoon KH, Lee JH, Kim JW, Cho JH, Choi YH, Ko SH, Zimmet P, Son HY. 2006. Epidemic obesity and type 2 diabetes in Asia. Lancet 368:1681- 1688.
5. Ali H, Houghton PJ, Soumyanath A. 2006. Alpha-amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amrus. J Ethnopharmacol 107: 449-455.
6. Tormo MA, Gil-Exojo I, Romero-de-Tejada A, Campillo JE. 2006. White bean amylase inhibitor administered orally reduces glycemia in type 2 diabetic rats. Br J Nutr 96: 539-544.
7. Layer P, Zinsmeister AR, DiMagno RP. 1986. Effect of decreasing intraluminal amylase activity on starch digestion and postprandial gastrointestinal function in human. Gastroenterology 91: 41-48.
8. Boivin M, Flourie B, Rizza RA, Go VL, DiMagno EP. 1988. Gastrointestinal and metabolic effects of amylase inhibition in diabetics. Gastroenterology 94: 387-394.
9. Lankisch M, Layer P, Rizza RA, DiMagno EP. 1998. Acute postprandial gastrointestinal and metabolic effects of wheat amylase inhibitor (WAI) in normal, obese and diabetic humans. Pancreas 17: 176-181.
10. Miller GL. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31: 426-428.
11. Folin O, Denis W. 1915. A colorimetric method for the determination of phenols (and phenol derivatives) in urine. J Biol Chem 22: 305-308.
12. Appel HD, Govenor HL, D'Ascenzo M, Siska E, Schultz JC. 2001. Limitations of Folin assays of foliar phenolics in ecological studies. J Chem Ecol 27: 761-778.
13. Svemsson B, Fukuda K, Nielsen PK, Bønsager BC. 2004. Proteinaceous α-amylase inhibitors. Biochim Biophys Acta 1696: 145-156.
14. Franco OL, Rigden DJ, Melo FR, Grossi-de-Sá MF. 2002. Plant α-amylase inhibitors and their interaction with insect α-amylase. Structure, function and potential for crop protection. Eur J Biochem 269: 397-412.
15. Kandra L, Fyémánt G, Zajácz Á, Batta G. 2004. Inhibitory effects of tannin on human salivary α-amylase. Biochem Biophys Res Commun 319: 1265-1271.
16. Okuda H, Morimoto C, Tsujita T. 1994. Role of endogenous lipid droplets in lipolysis in rat adipocytes. J Lipid Res 35: 36-44.
17. Wolfe RR. 1998. Metabolic interactions between glucose and fatty acids in humans. Am J Clin Nutr 67 (suppl): 519S-526S.
18. Randle RJ. 1998. Regulatory interactions between lipids and carbohydrates: the glucose fatty acid cycle after 35 years. Diabetes Metab Rev 14: 263-283.
19. Manganiello V, Vaughan M. 1973. An effect of insulin on cyclic adenosine 3′,5′-monophosphate phosphodiesterase activity in fat cells. J Biol Chem 248: 7164-7170.
20. Morimoto C, Tsujita T, Okuda H. 1998. Antilipolytic actions of insulin on basal and hormone-induced lipolysis in rat adipocytes. J Lipid Res 39: 957-962.
21. Meglasson MD, Matschinsky FM. 1986. Pancreatic islet glucose metabolism and regulation of insulin secretion. Diabetes Metab Rev 2: 163-214.
22. Yu YG, Chung CH, Fowler A, Suh SW. 1988. Amino acid sequence of a probable amylase/protease inhibitor from rice seeds. Arch Biochem Biophys 265: 466-475.
23. Gomez L, Sanchez-Monge R, Lopez-Otin C, Salcedo G. 1991. Wheat inhibitors of heterologous alpha-amylases: Characterization of major components from the monomeric class. Plant Physiol 96: 768-774.
24. Tormo MA, Gil-Exojo I, Romero de Tejada A, Campillo JE. 2006. White bean amylase inhibitor administered orally reduces glycaemia in type 2 diabetic rats. Br J Nutr 96: 539-544.
25. Koukiekolo R, Le Berre-Anton V, Desseaux V, Moreau Y, Rouge P, Marchis-Mouren G, Santimone M. 1999. Mechanism of porcine pancreatic alpha-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose. Eur J Biochem 265: 20-26.
26. Pekha MR, Padmaja G. 2002. Alpha-amylase inhibitor changes during processing of sweet potato and taro tubers. Plant Foods Hum Nutr 57: 285-294.
27. Prathiha S, Nmbian B, Leelamma S. 1995. Enzyme inhibitors in tuber crops and their thermal stability. Plant Foods Hum Nutr 48: 247-257.