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Volumn 52, Issue 3, 2006, Pages 283-291

Anti-diabetic activity of fruits of Terminalia chebula on streptozotocin induced diabetic rats

Author keywords

Carbohydrate metabolism; Diabetes; Electron microscope; Ethanolic extract; Terminalia chebula

Indexed keywords

ANTIDIABETIC AGENT; GLIBENCLAMIDE; GLUCOSE; GLYCOSYLATED HEMOGLOBIN; INSULIN; TERMINALIA CHEBULA EXTRACT;

EID: 33744737240     PISSN: 13449702     EISSN: 13475207     Source Type: Journal    
DOI: 10.1248/jhs.52.283     Document Type: Article
Times cited : (176)

References (48)
  • 1
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025-prevalence, numerical estimates and projections
    • King, H., Aubert, R. E. and Herman, W. H. (1998) Global burden of diabetes, 1995-2025-prevalence, numerical estimates and projections. Diabetes Care, 21, 1414-1431.
    • (1998) Diabetes Care , vol.21 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 2
    • 0010685770 scopus 로고    scopus 로고
    • Diabetes mellitus
    • (Stein, J. H. Ed.), Mosby, St. Louis
    • Garber, A. (1998) Diabetes mellitus. In International Medicine (Stein, J. H. Ed.), Mosby, St. Louis, pp. 1850-1854.
    • (1998) International Medicine , pp. 1850-1854
    • Garber, A.1
  • 5
    • 0033661509 scopus 로고    scopus 로고
    • Modulatory influence of Adhatoda veisca (Justica adhatoda) leaf extract on the enzyme of xenobiotic metabolism, antioxidant status and lipid peroxidation in mice
    • Singh, R. P., Padmavathi, B. and Rao, A. R. (2000) Modulatory influence of Adhatoda veisca (Justica adhatoda) leaf extract on the enzyme of xenobiotic metabolism, antioxidant status and lipid peroxidation in mice. Mol. Cell. Biochem., 213, 99-109.
    • (2000) Mol. Cell. Biochem. , vol.213 , pp. 99-109
    • Singh, R.P.1    Padmavathi, B.2    Rao, A.R.3
  • 7
    • 0005675997 scopus 로고
    • 2α-hydroxymicrometric acid, a pentacyclic triterpene form Terminalia chebula
    • Singh, C. (1990) 2α-hydroxymicrometric acid, a pentacyclic triterpene form Terminalia chebula. Phytochemistry, 29, 2348-2350.
    • (1990) Phytochemistry , vol.29 , pp. 2348-2350
    • Singh, C.1
  • 8
    • 0026073704 scopus 로고
    • Nutritative value of the Chebulinic myrobalan (Terminalia chebula Retz) and its potential as a food source
    • Barthakur, N. N. and Arnold, N. P. (1991) Nutritative value of the Chebulinic myrobalan (Terminalia chebula Retz) and its potential as a food source. Food Chemistry, 40, 213-219.
    • (1991) Food Chemistry , vol.40 , pp. 213-219
    • Barthakur, N.N.1    Arnold, N.P.2
  • 9
    • 0036284599 scopus 로고    scopus 로고
    • Anti-diabetic activity of medicinal plants and its relationship with their antioxidant property
    • Sabu, M. C. and Kuttan, R. (2002) Anti-diabetic activity of medicinal plants and its relationship with their antioxidant property. J. Ethanopharmacol., 81, 155-160.
    • (2002) J. Ethanopharmacol. , vol.81 , pp. 155-160
    • Sabu, M.C.1    Kuttan, R.2
  • 10
    • 0035996866 scopus 로고    scopus 로고
    • Inhibition of cancer cell growth by crude extract and the phenolics of Terminalia chebula Retz. fruit
    • Saleem, A., Husheem, M., Harkonen, P. and Pihalaja, K. (2002) Inhibition of cancer cell growth by crude extract and the phenolics of Terminalia chebula Retz. fruit. J. Ethanopharmacol., 81, 327-336.
    • (2002) J. Ethanopharmacol. , vol.81 , pp. 327-336
    • Saleem, A.1    Husheem, M.2    Harkonen, P.3    Pihalaja, K.4
  • 11
    • 0036125572 scopus 로고    scopus 로고
    • The in vitro antimutagenic activity of Triphala - An Indian herbal drug
    • Kaur, S., Arora, S., Kaur, K. and Kumar, S. (2002) The in vitro antimutagenic activity of Triphala - an Indian herbal drug. Food Chem. Toxicol., 40, 527-534.
    • (2002) Food Chem. Toxicol. , vol.40 , pp. 527-534
    • Kaur, S.1    Arora, S.2    Kaur, K.3    Kumar, S.4
  • 12
    • 0032501161 scopus 로고    scopus 로고
    • Antimutagenicity of hydrolyzable tannins from Terminalia chebula in Salmonella typhimurium
    • Karur, S., Grover, I. S., Singh, M. and Karur, S. (1998) Antimutagenicity of hydrolyzable tannins from Terminalia chebula in Salmonella typhimurium. Mutat. Res., 419, 169-179.
    • (1998) Mutat. Res. , vol.419 , pp. 169-179
    • Karur, S.1    Grover, I.S.2    Singh, M.3    Karur, S.4
  • 13
    • 0036270557 scopus 로고    scopus 로고
    • Inhibition of HIV-I integrase by galloyl glucose from Terminalia chebula and flavonol glycoside gallates from Euphorbia pekinensis
    • Ahn, M. J., Kim, C. Y., Lee, J. S., Kim, T. G., Kim, S. H., Lee, C. K., Lee, B. B., Shin, C. G., Huh, H. and Kim, J. (2002) Inhibition of HIV-I integrase by galloyl glucose from Terminalia chebula and flavonol glycoside gallates from Euphorbia pekinensis. Planta Med., 68, 457-459.
    • (2002) Planta Med. , vol.68 , pp. 457-459
    • Ahn, M.J.1    Kim, C.Y.2    Lee, J.S.3    Kim, T.G.4    Kim, S.H.5    Lee, C.K.6    Lee, B.B.7    Shin, C.G.8    Huh, H.9    Kim, J.10
  • 15
    • 0034069828 scopus 로고    scopus 로고
    • Antihyperglycemic activity of Musa sapientum flowers: Effect on lipid peroxidation in alloxan diabetic rats
    • Pari, L. and Umamaheswari, J. (2000) Antihyperglycemic activity of Musa sapientum flowers: effect on lipid peroxidation in alloxan diabetic rats. Phytother. Res., 14, 136-138.
    • (2000) Phytother. Res. , vol.14 , pp. 136-138
    • Pari, L.1    Umamaheswari, J.2
  • 16
    • 0032861574 scopus 로고    scopus 로고
    • Anti-diabetic activity of Picrorrhiza kurroa extract
    • Joy, K. L. and Kuttan, R. (1999) Anti-diabetic activity of Picrorrhiza kurroa extract. J. Ethanopharmacol., 67, 143-148.
    • (1999) J. Ethanopharmacol. , vol.67 , pp. 143-148
    • Joy, K.L.1    Kuttan, R.2
  • 17
    • 84996365648 scopus 로고
    • Effect of acetic acid concentration on the colour reaction in the O-toludine boric acid method for blood glucose estimation
    • Sasaki, T., Matsy, S. and Sonae, A. (1972) Effect of acetic acid concentration on the colour reaction in the O-toludine boric acid method for blood glucose estimation. Rinsh Kagaku, 1, 346-353.
    • (1972) Rinsh Kagaku , vol.1 , pp. 346-353
    • Sasaki, T.1    Matsy, S.2    Sonae, A.3
  • 18
    • 0000470054 scopus 로고
    • Spectrophotometric constants for common haemoglobin derivatives in human, dog and rabbit blood
    • Drabkin, D. C. and Austin, J. M. (1932) Spectrophotometric constants for common haemoglobin derivatives in human, dog and rabbit blood. J. Biol. Chem., 98, 719-733.
    • (1932) J. Biol. Chem. , vol.98 , pp. 719-733
    • Drabkin, D.C.1    Austin, J.M.2
  • 19
    • 0019471442 scopus 로고
    • A new colorimetric method for the estimation of glycosylated hemoglobin
    • Nayak, S. S. and Pattabiraman, T. N. (1981) A new colorimetric method for the estimation of glycosylated hemoglobin. Clin. Chim. Acta, 109, 267-274.
    • (1981) Clin. Chim. Acta , vol.109 , pp. 267-274
    • Nayak, S.S.1    Pattabiraman, T.N.2
  • 20
    • 7144228388 scopus 로고
    • Determination of hexokinase in tissue
    • Brandstrup, N., Kirk, J. E. and Bruni, C. (1957) Determination of hexokinase in tissue. J. Gerontol., 12, 166-171.
    • (1957) J. Gerontol. , vol.12 , pp. 166-171
    • Brandstrup, N.1    Kirk, J.E.2    Bruni, C.3
  • 21
    • 49749203103 scopus 로고
    • Pathological occurrence of glucose-6-phosphatase in serum in liver disease
    • Koide, H. and Oda, T. (1959) Pathological occurrence of glucose-6-phosphatase in serum in liver disease. Clin. Chim. Acta, 4, 554-561.
    • (1959) Clin. Chim. Acta , vol.4 , pp. 554-561
    • Koide, H.1    Oda, T.2
  • 22
    • 0014977781 scopus 로고
    • Fructose-1,6-bis phosphatase, phospho fructo kinase and glucose-6-phosphate dehydrogenase from fermenting and non fermenting yeasts
    • Gancedo, J. M. and Gancedo, C. (1971) Fructose-1,6-bis phosphatase, phospho fructo kinase and glucose-6-phosphate dehydrogenase from fermenting and non fermenting yeasts. Arch. Microbiol., 76, 132-138.
    • (1971) Arch. Microbiol. , vol.76 , pp. 132-138
    • Gancedo, J.M.1    Gancedo, C.2
  • 23
    • 70449290511 scopus 로고
    • Colorimetric determination of serum lactate dehydrogenase
    • King, J. (1959) Colorimetric determination of serum lactate dehydrogenase. J. Med. Lab. Technol., 16, 265-269.
    • (1959) J. Med. Lab. Technol. , vol.16 , pp. 265-269
    • King, J.1
  • 24
    • 77956988337 scopus 로고
    • Glycogen synthase from rat liver
    • (Colowick, S. P. and Kaplan, O. N., Eds.), Academic Press, New York
    • Leloir, L. F. and Goldenberg, S. H. (1962) Glycogen synthase from rat liver. In Methods of enzymology (Colowick, S. P. and Kaplan, O. N., Eds.), Academic Press, New York, pp. 145-148.
    • (1962) Methods of Enzymology , pp. 145-148
    • Leloir, L.F.1    Goldenberg, S.H.2
  • 25
    • 0000339905 scopus 로고
    • Regulation of glycogenlysis in muscle. Effects of glucagon and anoxia on lactate production, glycogen content and phosphorylase activity in the perfused isolated rat heart
    • Cornblath, M., Randle, P. J., Parmeggiani, A. and Morgan, H. E. (1963) Regulation of glycogenlysis in muscle. Effects of glucagon and anoxia on lactate production, glycogen content and phosphorylase activity in the perfused isolated rat heart. J. Biol. Chem., 238, 1592-1597.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1592-1597
    • Cornblath, M.1    Randle, P.J.2    Parmeggiani, A.3    Morgan, H.E.4
  • 26
    • 0002859674 scopus 로고
    • Mutations affecting accumulation of Neurospora glycogen
    • Morales, M. A., Jobbagy, A. J. and Terenizi, H. F. (1973) Mutations affecting accumulation of Neurospora glycogen. News Letter, 20, 24-25.
    • (1973) News Letter , vol.20 , pp. 24-25
    • Morales, M.A.1    Jobbagy, A.J.2    Terenizi, H.F.3
  • 28
    • 0034003084 scopus 로고    scopus 로고
    • Multiple low-dose and single high dose treatments with streptozotocin do not generate nitric oxide
    • Papaccio, G., Pisanthi, F. A., Latronico, M. Y., Ammendola, E. and Galdieri, M. (2000) Multiple low-dose and single high dose treatments with streptozotocin do not generate nitric oxide. J. Cell. Biochem., 77, 82-91.
    • (2000) J. Cell. Biochem. , vol.77 , pp. 82-91
    • Papaccio, G.1    Pisanthi, F.A.2    Latronico, M.Y.3    Ammendola, E.4    Galdieri, M.5
  • 30
    • 0036929262 scopus 로고    scopus 로고
    • Effect of Cassia auriculata flowers on blood sugar levels, serum and tissue lipids in streptozotocin diabetic rats
    • Pari, L. and Latha, M. (2002) Effect of Cassia auriculata flowers on blood sugar levels, serum and tissue lipids in streptozotocin diabetic rats. Singapore Med. J., 43, 617-621.
    • (2002) Singapore Med. J. , vol.43 , pp. 617-621
    • Pari, L.1    Latha, M.2
  • 31
    • 0032888354 scopus 로고    scopus 로고
    • Possible mechanism of antihyperglycemic effect of Azardirachta indica leaf extract. Part V
    • Chattopadhyay, R. R. (1999) Possible mechanism of antihyperglycemic effect of Azardirachta indica leaf extract. Part V. J. Ethanopharmacol., 67, 373-376.
    • (1999) J. Ethanopharmacol. , vol.67 , pp. 373-376
    • Chattopadhyay, R.R.1
  • 32
    • 0001022946 scopus 로고
    • A minor haemoglobin fraction and the level of fasting blood glucose
    • Alyassin, D. and Ibrahim, K. (1981) A minor haemoglobin fraction and the level of fasting blood glucose. J. Fac. Med. Unive. Baghdad, 23, 373-380.
    • (1981) J. Fac. Med. Unive. Baghdad , vol.23 , pp. 373-380
    • Alyassin, D.1    Ibrahim, K.2
  • 33
    • 0026773906 scopus 로고
    • Antidiabetic effects of S-allyl cystine sulphoxide isolated from garlic Allium sativum Linn
    • Sheela, G. C. and Augusti, K. T. (1992) Antidiabetic effects of S-allyl cystine sulphoxide isolated from garlic Allium sativum Linn. Indian J. Exp. Biol., 30, 523-526.
    • (1992) Indian J. Exp. Biol. , vol.30 , pp. 523-526
    • Sheela, G.C.1    Augusti, K.T.2
  • 34
    • 0017835519 scopus 로고
    • The glycosylation of hemoglobin: Relevance to diabetes mellitus
    • Bunn, H. G., Gabby, K. H. and Gallop, P. M. (1978) The glycosylation of hemoglobin: relevance to diabetes mellitus. Science, 200, 21-27.
    • (1978) Science , vol.200 , pp. 21-27
    • Bunn, H.G.1    Gabby, K.H.2    Gallop, P.M.3
  • 35
    • 0031174748 scopus 로고    scopus 로고
    • Effect of experimental diabetes on the activities of hexokinase, glucose-6-phosphate dehydrogenase and catecholamines in rat erythrocytes of different ages
    • Gupta, B. L., Nehal, M. and Baquer, N. Z. (1997) Effect of experimental diabetes on the activities of hexokinase, glucose-6-phosphate dehydrogenase and catecholamines in rat erythrocytes of different ages. Indian J. Exp. Biol., 35, 792-795.
    • (1997) Indian J. Exp. Biol. , vol.35 , pp. 792-795
    • Gupta, B.L.1    Nehal, M.2    Baquer, N.Z.3
  • 36
    • 0024314792 scopus 로고
    • Effects of diabetes and insulin-induced hypoglycemia on hexokinase and glucose-6-phosphate dehydrogenase in red blood cells
    • Nehal, M. and Baquer, N. Z. (1989) Effects of diabetes and insulin-induced hypoglycemia on hexokinase and glucose-6-phosphate dehydrogenase in red blood cells. Biochem. Int., 19, 185-191.
    • (1989) Biochem. Int. , vol.19 , pp. 185-191
    • Nehal, M.1    Baquer, N.Z.2
  • 37
    • 0021099839 scopus 로고
    • Levels of translatable mRNA coding for rat liver glucokinase
    • Spence, T. J. (1983) Levels of translatable mRNA coding for rat liver glucokinase. J. Biol. Chem., 258, 9143-9146.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9143-9146
    • Spence, T.J.1
  • 39
    • 0021368559 scopus 로고
    • Renal enzymes during experimental diabetes mellitus in the rat. Role of insulin, carbohydrate metabolism and ketoacidosis
    • Lemieux, G., Aranda, M. R., Fournel, P. and Lemieux, C. (1984) Renal enzymes during experimental diabetes mellitus in the rat. Role of insulin, carbohydrate metabolism and ketoacidosis. Can. J. Physiol. Pharmacol., 62, 70-75.
    • (1984) Can. J. Physiol. Pharmacol. , vol.62 , pp. 70-75
    • Lemieux, G.1    Aranda, M.R.2    Fournel, P.3    Lemieux, C.4
  • 40
    • 0014082605 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson, D. H., Lund, P. and Kreps, H. A. (1967) The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem. J., 103, 514-527.
    • (1967) Biochem. J. , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Kreps, H.A.3
  • 41
    • 0002447814 scopus 로고    scopus 로고
    • Regulation of metabolic pathway in liver and kidney during experimental diabetes. Effect of antidiabetic compounds
    • Baquer, N. Z., Gupta, D. and Raju, J. (1998) Regulation of metabolic pathway in liver and kidney during experimental diabetes. Effect of antidiabetic compounds. Ind. J. Clin. Biochem., 13, 63-80.
    • (1998) Ind. J. Clin. Biochem. , vol.13 , pp. 63-80
    • Baquer, N.Z.1    Gupta, D.2    Raju, J.3
  • 42
    • 0031043189 scopus 로고    scopus 로고
    • New insight into the regulation of liver glycogen metabolism by glucose
    • Stalmans, W., Cadefau, J., Wera, S. and Bollen, M. (1997) New insight into the regulation of liver glycogen metabolism by glucose. Biochem. Soc. Trans., 25, 19-25.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 19-25
    • Stalmans, W.1    Cadefau, J.2    Wera, S.3    Bollen, M.4
  • 43
    • 0025272957 scopus 로고
    • Role of AMP on the activation of glycogen synthase and phosphorylase by adenosine, fructose and glutamine in rat hypocytes
    • Carabaza, A., Ricart, M. D., Mor, A., Guinovart, J. J. and Ciudad, C. J. (1990) Role of AMP on the activation of glycogen synthase and phosphorylase by adenosine, fructose and glutamine in rat hypocytes. J. Biol. Chem., 265, 2724-2732.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2724-2732
    • Carabaza, A.1    Ricart, M.D.2    Mor, A.3    Guinovart, J.J.4    Ciudad, C.J.5
  • 44
    • 0020532102 scopus 로고
    • Comparison of liver glycogen synthase from normal and streptozotocin-induced diabetic rats
    • Akatsuka, A., Singh, T. J. and Huang, K. P. (1983) Comparison of liver glycogen synthase from normal and streptozotocin-induced diabetic rats. Arch. Biochem. Biophys., 220, 426-434.
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 426-434
    • Akatsuka, A.1    Singh, T.J.2    Huang, K.P.3
  • 45
    • 0022444654 scopus 로고
    • Quantitation of glycogen synthase and phosphorylase protein mouse liver. Correlation between enzymatic protein and enzymatic activity
    • Roesler, W. J. and Khanderwal, R. L. (1986) Quantitation of glycogen synthase and phosphorylase protein mouse liver. Correlation between enzymatic protein and enzymatic activity. Arch. Biochem. Biophys., 244, 397-407.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 397-407
    • Roesler, W.J.1    Khanderwal, R.L.2
  • 46
    • 9144238115 scopus 로고    scopus 로고
    • Hypoglycemic effect of Eugenia jambolana seed kernels on streptozotocin-induced diabetes in rats
    • Ravi, K., Rajasekaran, S. and Subramanian, S. (2003) Hypoglycemic effect of Eugenia jambolana seed kernels on streptozotocin-induced diabetes in rats. Pharmaceutical Biol., 40, 598-603.
    • (2003) Pharmaceutical Biol. , vol.40 , pp. 598-603
    • Ravi, K.1    Rajasekaran, S.2    Subramanian, S.3
  • 47
    • 0036482644 scopus 로고    scopus 로고
    • Insulin and gluagon secretions, and morphological change of pancreatic islets in OLETF rats, a model of type 2 diabetes mellitus
    • Hong, E. G., Noh, H. Y., Lee, S. K., Chung, Y. S., Lee, K. W. and Kim, H. M. (2002) Insulin and gluagon secretions, and morphological change of pancreatic islets in OLETF rats, a model of type 2 diabetes mellitus. J. Korean Med. Sci., 17, 34-40.
    • (2002) J. Korean Med. Sci. , vol.17 , pp. 34-40
    • Hong, E.G.1    Noh, H.Y.2    Lee, S.K.3    Chung, Y.S.4    Lee, K.W.5    Kim, H.M.6
  • 48
    • 14644404899 scopus 로고    scopus 로고
    • The effects of acarbose and Rumex patientia L. on ultrastructural and biochemical changes of pancreatic β-cells in streptozotocin-induced diabetic rats
    • Desirmenci, I., Ustuner, M. C., Kalender, Y., Kalender, S. and Gunes, H. V. (2005) The effects of acarbose and Rumex patientia L. on ultrastructural and biochemical changes of pancreatic β-cells in streptozotocin-induced diabetic rats. J. Ethnopharmacol., 97, 555-559.
    • (2005) J. Ethnopharmacol. , vol.97 , pp. 555-559
    • Desirmenci, I.1    Ustuner, M.C.2    Kalender, Y.3    Kalender, S.4    Gunes, H.V.5


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