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Volumn 71, Issue 4, 2010, Pages 291-296

Antioxidant protection of Malaysian tualang honey in pancreas of normal and streptozotocin-induced diabetic rats;Action protectrice anti-oxydante du miel malésien Tualang sur le pancréas de rats normaux ou diabétiques induits par la streptozotocine

Author keywords

Diabetes mellitus; Glucotoxicity; Oxidative stress; Pancreas; Streptozotocin; Tualang honey

Indexed keywords

AGROMAS; ANTIOXIDANT; CATALASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; MALONALDEHYDE; STREPTOZOCIN; SUPEROXIDE DISMUTASE; TAULANG HONEY; UNCLASSIFIED DRUG;

EID: 77956232225     PISSN: 00034266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ando.2010.03.003     Document Type: Article
Times cited : (96)

References (39)
  • 1
    • 0023770113 scopus 로고
    • Free radicals and diabetes
    • Oberley L.W. Free radicals and diabetes. Free Radic Biol Med 1988, 5:113-124.
    • (1988) Free Radic Biol Med , vol.5 , pp. 113-124
    • Oberley, L.W.1
  • 2
    • 0030048496 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications (Review)
    • Giugliano D., Ceriello A., Paolisso G. Oxidative stress and diabetic complications (Review). Diabetes Care 1996, 19:257-267.
    • (1996) Diabetes Care , vol.19 , pp. 257-267
    • Giugliano, D.1    Ceriello, A.2    Paolisso, G.3
  • 3
    • 0038825044 scopus 로고    scopus 로고
    • Glucotoxicity and beta-cell failure in type 2 diabetes mellitus
    • Kaiser N., Leibowitz G., Nesher R. Glucotoxicity and beta-cell failure in type 2 diabetes mellitus. J Pediatr Endocrinol Metab 2003, 16:5-22.
    • (2003) J Pediatr Endocrinol Metab , vol.16 , pp. 5-22
    • Kaiser, N.1    Leibowitz, G.2    Nesher, R.3
  • 4
    • 0032998220 scopus 로고    scopus 로고
    • Hyperglycemia causes oxidative stress in pancreatic β-cells of GK rats, a model of type 2 diabetes
    • Ihara Y., Toyokuni S., Uchida K., Odaka H., Tanaka T., Ikeda H., et al. Hyperglycemia causes oxidative stress in pancreatic β-cells of GK rats, a model of type 2 diabetes. Diabetes 1999, 48:927-932.
    • (1999) Diabetes , vol.48 , pp. 927-932
    • Ihara, Y.1    Toyokuni, S.2    Uchida, K.3    Odaka, H.4    Tanaka, T.5    Ikeda, H.6
  • 5
    • 0019852821 scopus 로고
    • CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse
    • Grankvist K., Marklund S.L., Taljedal I.B. CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse. Biochem J 1981, 199:393-398.
    • (1981) Biochem J , vol.199 , pp. 393-398
    • Grankvist, K.1    Marklund, S.L.2    Taljedal, I.B.3
  • 6
    • 0032844258 scopus 로고    scopus 로고
    • Supplementation of N-acetylcysteine inhibits NFkappaB activation and protects against alloxan-induced diabetes in CD-1 mice
    • Ho E., Chen G., Bray T.M. Supplementation of N-acetylcysteine inhibits NFkappaB activation and protects against alloxan-induced diabetes in CD-1 mice. FASEB J 1999, 13:1845-1854.
    • (1999) FASEB J , vol.13 , pp. 1845-1854
    • Ho, E.1    Chen, G.2    Bray, T.M.3
  • 7
    • 0030798658 scopus 로고    scopus 로고
    • Targeted over-expression of Cu/Zn superoxide dismutase protects pancreatic β-cells against oxidative stress
    • Kubisch H.M., Wang J., Bray T.M., Phillips J.P. Targeted over-expression of Cu/Zn superoxide dismutase protects pancreatic β-cells against oxidative stress. Diabetes 1997, 46:1563-1566.
    • (1997) Diabetes , vol.46 , pp. 1563-1566
    • Kubisch, H.M.1    Wang, J.2    Bray, T.M.3    Phillips, J.P.4
  • 8
    • 15644375700 scopus 로고    scopus 로고
    • Adenovirus-mediated catalase gene transfer reduces oxidant stress in human, porcine and rat pancreatic islets
    • Benhamou P.Y., Moriscot C., Richard M.J., Beatrix O., Badet L., Pattou F., et al. Adenovirus-mediated catalase gene transfer reduces oxidant stress in human, porcine and rat pancreatic islets. Diabetologia 1998, 41:1093-1100.
    • (1998) Diabetologia , vol.41 , pp. 1093-1100
    • Benhamou, P.Y.1    Moriscot, C.2    Richard, M.J.3    Beatrix, O.4    Badet, L.5    Pattou, F.6
  • 9
    • 0001281521 scopus 로고
    • Composition of honey
    • Heinemann, London, E. Carne (Ed.)
    • White J.W. Composition of honey. Honey: A comprehensive survey 1979, 157-207. Heinemann, London. E. Carne (Ed.).
    • (1979) Honey: A comprehensive survey , pp. 157-207
    • White, J.W.1
  • 10
    • 0037048732 scopus 로고    scopus 로고
    • Identification and quantification of antioxidant components of honeys from various floral sources
    • Gheldof N., Wang X.H., Engeseth N.J. Identification and quantification of antioxidant components of honeys from various floral sources. J Agric Food Chem 2002, 50:5870-5877.
    • (2002) J Agric Food Chem , vol.50 , pp. 5870-5877
    • Gheldof, N.1    Wang, X.H.2    Engeseth, N.J.3
  • 11
    • 0344911324 scopus 로고
    • Honey catalase: occurrence and some kinetic properties
    • Schepartz A.I. Honey catalase: occurrence and some kinetic properties. J Apic Res 1966, 5:167-176.
    • (1966) J Apic Res , vol.5 , pp. 167-176
    • Schepartz, A.I.1
  • 13
    • 0942289870 scopus 로고    scopus 로고
    • Evaluation of the phenolic contents and antioxidant capacities of two Malaysian floral honeys
    • Aljadi A.M., Kamaruddin M.Y. Evaluation of the phenolic contents and antioxidant capacities of two Malaysian floral honeys. Food Chem 2004, 85:513-518.
    • (2004) Food Chem , vol.85 , pp. 513-518
    • Aljadi, A.M.1    Kamaruddin, M.Y.2
  • 16
    • 0032340039 scopus 로고    scopus 로고
    • Antioxidant capacity and correlated characteristics of 14 unifloral honeys
    • Frankel S., Robinson G.E., Berenbaum M.R. Antioxidant capacity and correlated characteristics of 14 unifloral honeys. J Apic Res 1998, 37(1):27-31.
    • (1998) J Apic Res , vol.37 , Issue.1 , pp. 27-31
    • Frankel, S.1    Robinson, G.E.2    Berenbaum, M.R.3
  • 17
    • 29244481488 scopus 로고    scopus 로고
    • Characterization of honey from different floral sources. Its functional properties and effects of honey species on storage of meat
    • Nagai T., Inoue R., Kanamori N., Suzuki N., Nagashima T. Characterization of honey from different floral sources. Its functional properties and effects of honey species on storage of meat. Food Chem 2006, 97:256-262.
    • (2006) Food Chem , vol.97 , pp. 256-262
    • Nagai, T.1    Inoue, R.2    Kanamori, N.3    Suzuki, N.4    Nagashima, T.5
  • 18
    • 0037041949 scopus 로고    scopus 로고
    • Antioxidant capacity of honeys from various floral sources based on the determination of oxygen radical absorbance capacity and inhibition of in vitro lipoprotein oxidation in human serum samples
    • Gheldof N., Engeseth N.J. Antioxidant capacity of honeys from various floral sources based on the determination of oxygen radical absorbance capacity and inhibition of in vitro lipoprotein oxidation in human serum samples. J Agric Food Chem 2002, 50:3050-3055.
    • (2002) J Agric Food Chem , vol.50 , pp. 3050-3055
    • Gheldof, N.1    Engeseth, N.J.2
  • 19
    • 77953445509 scopus 로고    scopus 로고
    • Effects of Malaysian tualang honey supplementation on glycemia, free radical scavenging enzymes and markers of oxidative stress in kidneys of normal and streptozotocin-induced diabetic rats
    • Erejuwa O.O., Sulaiman S.A., Ab Wahab M.S., Sirajudeen K.N.S., Salzihan M.S. Effects of Malaysian tualang honey supplementation on glycemia, free radical scavenging enzymes and markers of oxidative stress in kidneys of normal and streptozotocin-induced diabetic rats. Int J Cardiol 2009, 137:S45.
    • (2009) Int J Cardiol , vol.137
    • Erejuwa, O.O.1    Sulaiman, S.A.2    Ab Wahab, M.S.3    Sirajudeen, K.N.S.4    Salzihan, M.S.5
  • 20
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979, 95:351-358.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 21
    • 0026032095 scopus 로고
    • A simple method for determination of serum catalase activity and revision of reference range
    • Gott L. A simple method for determination of serum catalase activity and revision of reference range. Clin Chim Acta 1991, 196(2-3):143-151.
    • (1991) Clin Chim Acta , vol.196 , Issue.2-3 , pp. 143-151
    • Gott, L.1
  • 22
    • 0001528839 scopus 로고
    • Assay of glutathione reductase
    • Verlag Chemie Deerfield Beach, FL, H.V. Bergmeyen (Ed.)
    • Goldberg D.M., Spooner R.J. Assay of glutathione reductase. Methods of enzymatic analysis 1983, 258-265. Verlag Chemie Deerfield Beach, FL. H.V. Bergmeyen (Ed.).
    • (1983) Methods of enzymatic analysis , pp. 258-265
    • Goldberg, D.M.1    Spooner, R.J.2
  • 23
    • 0016275313 scopus 로고
    • Glutathione-S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. Glutathione-S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem 1974, 249:7130-7139.
    • (1974) J Biol Chem , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 25
    • 1842423094 scopus 로고    scopus 로고
    • The role of oxidative stress in diabetic complications
    • Baynes J.W., Thorpe S.R. The role of oxidative stress in diabetic complications. Curr Opin Endocrinol 1999, 3:277-284.
    • (1999) Curr Opin Endocrinol , vol.3 , pp. 277-284
    • Baynes, J.W.1    Thorpe, S.R.2
  • 26
    • 0033499583 scopus 로고    scopus 로고
    • Beneficial effects of antioxidants in diabetes: possible protection of pancreatic beta-cells against glucose toxicity
    • Kaneto H., Kajimoto Y., Miyagawa J., Matsuoka T., Fujitani Y., Umayahara Y. Beneficial effects of antioxidants in diabetes: possible protection of pancreatic beta-cells against glucose toxicity. Diabetes 1999, 48:2398-2406.
    • (1999) Diabetes , vol.48 , pp. 2398-2406
    • Kaneto, H.1    Kajimoto, Y.2    Miyagawa, J.3    Matsuoka, T.4    Fujitani, Y.5    Umayahara, Y.6
  • 27
    • 0034044814 scopus 로고    scopus 로고
    • The role of nitric oxide in the development of streptozotocin-induced diabetes mellitus: experimental and clinical implication
    • Haluzik M., Nedvidkova J. The role of nitric oxide in the development of streptozotocin-induced diabetes mellitus: experimental and clinical implication. Physiol Res 2000, 49:37-42.
    • (2000) Physiol Res , vol.49 , pp. 37-42
    • Haluzik, M.1    Nedvidkova, J.2
  • 28
    • 0023873792 scopus 로고
    • Lipid peroxidation and endothelial cell injury: implications in atherosclerosis
    • Hennig B., Chow C.K. Lipid peroxidation and endothelial cell injury: implications in atherosclerosis. Free Radic Biol Med 1988, 4:99-106.
    • (1988) Free Radic Biol Med , vol.4 , pp. 99-106
    • Hennig, B.1    Chow, C.K.2
  • 29
    • 0023239754 scopus 로고
    • Lipid peroxides and human diseases
    • Yagi K. Lipid peroxides and human diseases. Chem Phys Lipids 1987, 45:337-351.
    • (1987) Chem Phys Lipids , vol.45 , pp. 337-351
    • Yagi, K.1
  • 30
    • 34247854742 scopus 로고    scopus 로고
    • Experimental diabetes treated with Achillea santolina: Effect on pancreatic oxidative parameters
    • Razieh Y., Amin A., Shirin J. Experimental diabetes treated with Achillea santolina: Effect on pancreatic oxidative parameters. J Ethnopharmacol 2007, 112:13-18.
    • (2007) J Ethnopharmacol , vol.112 , pp. 13-18
    • Razieh, Y.1    Amin, A.2    Shirin, J.3
  • 31
    • 0031808543 scopus 로고    scopus 로고
    • Increased oxidative stress in rat liver and pancreas during progression of streptozotocin-induced diabetes
    • Kakkar R., Mantha S.V., Radhi J., Prasad K., Kalra J. Increased oxidative stress in rat liver and pancreas during progression of streptozotocin-induced diabetes. Clin Sci 1998, 94:623-632.
    • (1998) Clin Sci , vol.94 , pp. 623-632
    • Kakkar, R.1    Mantha, S.V.2    Radhi, J.3    Prasad, K.4    Kalra, J.5
  • 32
    • 0032791152 scopus 로고    scopus 로고
    • Protection against the co-operative toxicity of nitric oxide and oxygen free radicals by over-expression of antioxidant enzymes in bioengineered insulin-producing RINm5F cells
    • Tiedge M., Lortz S., Munday R., Lenzen S. Protection against the co-operative toxicity of nitric oxide and oxygen free radicals by over-expression of antioxidant enzymes in bioengineered insulin-producing RINm5F cells. Diabetologia 1999, 42:849-855.
    • (1999) Diabetologia , vol.42 , pp. 849-855
    • Tiedge, M.1    Lortz, S.2    Munday, R.3    Lenzen, S.4
  • 33
    • 23844470618 scopus 로고    scopus 로고
    • Importance of mitochondrial superoxide dismutase expression in insulin-producing cells for the toxicity of reactive oxygen species and pro-inflammatory cytokines
    • Lortz S., Gurgul-Convey E., Lenzen S., Tiedge M. Importance of mitochondrial superoxide dismutase expression in insulin-producing cells for the toxicity of reactive oxygen species and pro-inflammatory cytokines. Diabetologia 2005, 48:1541-1548.
    • (2005) Diabetologia , vol.48 , pp. 1541-1548
    • Lortz, S.1    Gurgul-Convey, E.2    Lenzen, S.3    Tiedge, M.4
  • 34
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification: The potential role of 'autoxidative glycosylation' in diabetes
    • Wolff S.P., Dean R.T. Glucose autoxidation and protein modification: The potential role of 'autoxidative glycosylation' in diabetes. Biochem J 1987, 245:243-250.
    • (1987) Biochem J , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 35
    • 0020490598 scopus 로고
    • Superoxide radical inhibits catalase
    • Kono Y., Fridovich I. Superoxide radical inhibits catalase. J Biol Chem 1982, 257:5751-5754.
    • (1982) J Biol Chem , vol.257 , pp. 5751-5754
    • Kono, Y.1    Fridovich, I.2
  • 36
    • 0031035450 scopus 로고    scopus 로고
    • The origin of the hydroxyl radical oxygen in the Fenton reaction
    • Lloyd R.V., Hanna P.M., Mason R.P. The origin of the hydroxyl radical oxygen in the Fenton reaction. Free Radic Biol Med 1997, 22:885-888.
    • (1997) Free Radic Biol Med , vol.22 , pp. 885-888
    • Lloyd, R.V.1    Hanna, P.M.2    Mason, R.P.3
  • 37
    • 0023905646 scopus 로고    scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay J.A., Chin S.M., Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 1998, 240:640-642.
    • (1998) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 38
    • 0014694711 scopus 로고
    • Reduction of linolenic acid hydroperoxide by a glutathione peroxidase
    • Christopherson B.O. Reduction of linolenic acid hydroperoxide by a glutathione peroxidase. Biochem Biophys Acta 1969, 176:463-470.
    • (1969) Biochem Biophys Acta , vol.176 , pp. 463-470
    • Christopherson, B.O.1
  • 39
    • 0022521858 scopus 로고
    • Neutrophil-endothelial cell interaction: evidence for and mechanism of the self protection of bovine microvascular endothelial cells from hydrogen peroxide induced oxidative stress
    • Dobrino A., Patriaca P. Neutrophil-endothelial cell interaction: evidence for and mechanism of the self protection of bovine microvascular endothelial cells from hydrogen peroxide induced oxidative stress. J Clin Invest 1986, 78:462-471.
    • (1986) J Clin Invest , vol.78 , pp. 462-471
    • Dobrino, A.1    Patriaca, P.2


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