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Volumn 83, Issue 1, 2015, Pages 159-175

Curcumin attenuates oxidative stress and activation of redox-sensitive kinases in high fructose- and high-fat-fed male wistar rats

Author keywords

Catalase; Glutathione peroxidase; Malondialdehyde; Oxidative stress; Total oxidant status

Indexed keywords

CATALASE; CURCUMIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; MALONALDEHYDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN KINASE;

EID: 84924242545     PISSN: 00368709     EISSN: 22180532     Source Type: Journal    
DOI: 10.3797/scipharm.1408-16     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 0024370286 scopus 로고
    • Fructose-induced in vivo insulin resistance and elevated plasma triglyceride levels in rats
    • Thorburn AW, Storlien LH, Jenkins AB, Khouri S, Kraegen EW. Fructose-induced in vivo insulin resistance and elevated plasma triglyceride levels in rats. Am J Clin Nutr. 1989; 49: 1155-1163. http://www.ncbi.nlm.nih.gov/pubmed/2658534
    • (1989) Am J Clin Nutr , vol.49 , pp. 1155-1163
    • Thorburn, A.W.1    Storlien, L.H.2    Jenkins, A.B.3    Khouri, S.4    Kraegen, E.W.5
  • 2
    • 82255165038 scopus 로고    scopus 로고
    • Effect of eveningrose oil on activities of oxygen free radical scaverging-related enzymes and hepatic morphosis in rats on high lipid diet
    • Yang JJ, Li GL, Liu HR, Ren BB. Effect of eveningrose oil on activities of oxygen free radical scaverging-related enzymes and hepatic morphosis in rats on high lipid diet. J Ning Xia Med Coll. 2003; 25: 244-246.
    • (2003) J Ning Xia Med Coll , vol.25 , pp. 244-246
    • Yang, J.J.1    Li, G.L.2    Liu, H.R.3    Ren, B.B.4
  • 3
    • 34047161648 scopus 로고    scopus 로고
    • Combined effects of high-fat diet and ethanol induce oxidative stress in rat liver
    • Demori I, Voci A, Fugassa E, Burlando B. Combined effects of high-fat diet and ethanol induce oxidative stress in rat liver. Alcohol. 2006; 40: 185-191. http://dx.doi:10.1016/j.alcohol.2006.12.006
    • (2006) Alcohol , vol.40 , pp. 185-191
    • Demori, I.1    Voci, A.2    Fugassa, E.3    Burlando, B.4
  • 4
    • 0032814218 scopus 로고    scopus 로고
    • Taurine supplementation attenuates erythrocyte lipid peroxidation in fructose-fed hypertensive rats
    • Balakrishnan SD, Anuradha CV. Taurine supplementation attenuates erythrocyte lipid peroxidation in fructose-fed hypertensive rats. Med Sci Res. 1999; 27: 489-492.
    • (1999) Med Sci Res , vol.27 , pp. 489-492
    • Balakrishnan, S.D.1    Anuradha, C.V.2
  • 5
    • 0004897150 scopus 로고    scopus 로고
    • Antioxidants: The basics--what they are and how to evaluate them
    • Halliwell B. Antioxidants: the basics--what they are and how to evaluate them. Adv Pharmacol. 1997; 38: 3-20. http://www.ncbi.nlm.nih.gov/pubmed/8895801
    • (1997) Adv Pharmacol , vol.38 , pp. 3-20
    • Halliwell, B.1
  • 6
    • 0034939115 scopus 로고    scopus 로고
    • The role of oxidative stress in the onset and progression of diabetes and its complications: A summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society
    • Rösen P, Nawroth PP, King G, Möller W, Tritschler HJ, Packer L. The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society. Diabetes Metab Res Rev. 2001; 17: 189-212. http://dx.doi.org/10.1002/dmrr.196
    • (2001) Diabetes Metab Res Rev , vol.17 , pp. 189-212
    • Rösen, P.1    Nawroth, P.P.2    King, G.3    Möller, W.4    Tritschler, H.J.5    Packer, L.6
  • 7
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature. 2001; 414: 813-820. http://dx.doi.org/10.1038/414813a
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 8
    • 0026634285 scopus 로고
    • Regulation of antioxidant enzymes
    • Harris ED. Regulation of antioxidant enzymes. FASEB J. 1992; 6: 2674-2678. http://www.ncbi.nlm.nih.gov/pubmed/1612291
    • (1992) FASEB J , vol.6 , pp. 2674-2678
    • Harris, E.D.1
  • 9
    • 33750909999 scopus 로고    scopus 로고
    • Reactive oxygen species-induced activation of the MAP kinase signaling pathways
    • McCubrey JA, Lahair MM, Franklin RA. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxid Redox Signal. 2006; 8: 1775-1789. http://dx.doi.org/10.1089/ars.2006.8.1775
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1775-1789
    • McCubrey, J.A.1    Lahair, M.M.2    Franklin, R.A.3
  • 10
    • 0142043984 scopus 로고    scopus 로고
    • Redox signaling and the MAP kinase pathways
    • Torres M, Forman HJ. Redox signaling and the MAP kinase pathways. Biofactors. 2003; 17: 287-296. http://dx.doi.org/10.1002/biof.5520170128
    • (2003) Biofactors , vol.17 , pp. 287-296
    • Torres, M.1    Forman, H.J.2
  • 11
    • 0028278766 scopus 로고
    • Effect of dietary turmeric (Curcuma longa) on iron-induced lipid peroxidation in the rat liver
    • Reddy AC, Lokesh BR. Effect of dietary turmeric (Curcuma longa) on iron-induced lipid peroxidation in the rat liver. Food Chem Toxicol. 1994; 32: 279-283. http://dx.doi.org/10.1016/0278-6915(94)90201-1
    • (1994) Food Chem Toxicol , vol.32 , pp. 279-283
    • Reddy, A.C.1    Lokesh, B.R.2
  • 12
    • 0031033145 scopus 로고    scopus 로고
    • Nitric oxide scavenging by curcuminoids
    • Sreejayan, Rao MN. Nitric oxide scavenging by curcuminoids. J Pharm Pharmacol. 1997; 49: 105-107. http://dx.doi.org/10.1111/j.2042-7158.1997.tb06761.x
    • (1997) J Pharm Pharmacol , vol.49 , pp. 105-107
    • Sreejayan, R.M.1
  • 13
    • 38349011007 scopus 로고    scopus 로고
    • Curcumin: Preventive and therapeutic properties in laboratory studies and clinical trials
    • Strimpakos AS, Sharma RA. Curcumin: preventive and therapeutic properties in laboratory studies and clinical trials. Antioxid Redox Signal. 2008; 10: 511-545. http://dx.doi.org/10.1016/0278-6915(94)90201-1
    • (2008) Antioxid Redox Signal , vol.10 , pp. 511-545
    • Strimpakos, A.S.1    Sharma, R.A.2
  • 15
    • 0023493524 scopus 로고
    • Fructose-induced insulin resistance and hypertension in rats
    • Hwang IS, Ho H, Hoffman BB, Reaven GM. Fructose-induced insulin resistance and hypertension in rats. Hypertension. 1987: 512-516. http://dx.doi.org/10.1161/01.HYP.10.5.512
    • (1987) Hypertension , pp. 512-516
    • Hwang, I.S.1    Ho, H.2    Hoffman, B.B.3    Reaven, G.M.4
  • 16
    • 33745640962 scopus 로고    scopus 로고
    • Reduced fat mass in rats fed a high oleic acid-rich safflower oil diet is associated with changes in expression of hepatic PPARalpha and adipose SREBP-1c-regulated genes
    • Hsu S-C, Huang C-J. Reduced fat mass in rats fed a high oleic acid-rich safflower oil diet is associated with changes in expression of hepatic PPARalpha and adipose SREBP-1c-regulated genes. J Nutr. 2006; 136: 1779-1785. http://www.ncbi.nlm.nih.gov/pubmed/16772437
    • (2006) J Nutr , vol.136 , pp. 1779-1785
    • Hsu, S.-C.1    Huang, C.-J.2
  • 17
    • 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. http://dx.doi.org/10.1016/0003-2697(79)90738-3
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193: 265-275. http://www.ncbi.nlm.nih.gov/pubmed/14907713
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 19
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of “antioxidant power”: The FRAP assay
    • Benzie IF, Strain JJ. The ferric reducing ability of plasma (FRAP) as a measure of “antioxidant power”: the FRAP assay. Anal Biochem. 1996; 239: 70-76. http://dx.doi.org/10.1006/abio.1996.0292
    • (1996) Anal Biochem , vol.239 , pp. 70-76
    • Benzie, I.F.1    Strain, J.J.2
  • 20
    • 29144527533 scopus 로고    scopus 로고
    • A new automated colorimetric method for measuring total oxidant status
    • Erel O. A new automated colorimetric method for measuring total oxidant status. Clin Biochem. 2005; 38: 1103-1111. http://dx.doi.org/10.1016/j.clinbiochem.2005.08.008
    • (2005) Clin Biochem , vol.38 , pp. 1103-1111
    • Erel, O.1
  • 21
    • 73649194769 scopus 로고
    • Improved method for the determination of blood glutathione
    • Beutler E, Duron O, Kelly BM. Improved method for the determination of blood glutathione. J Lab Clin Med. 1963; 61: 882-888. http://www.ncbi.nlm.nih.gov/pubmed/13967893
    • (1963) J Lab Clin Med , vol.61 , pp. 882-888
    • Beutler, E.1    Duron, O.2    Kelly, B.M.3
  • 22
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol. 1984; 105: 121-126. http://dx.doi.org/10.1016/S0076-6879(84)05016-3
    • (1984) Methods Enzymol , vol.105 , pp. 121-126
    • Aebi, H.1
  • 23
    • 0037173514 scopus 로고    scopus 로고
    • Rapid, fluorimetric-liquid chromatographic determination of malondialdehyde in biological samples
    • Agarwal R, Chase SD. Rapid, fluorimetric-liquid chromatographic determination of malondialdehyde in biological samples. J Chromatogr B. 2002; 775: 121-126. http://dx.doi.org/10.1016/S1570-0232(02)00273-8
    • (2002) J Chromatogr B , vol.775 , pp. 121-126
    • Agarwal, R.1    Chase, S.D.2
  • 24
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • Wendel A. Glutathione peroxidase. Methods Enzymol. 1981; 77: 325-333. http://dx.doi.org/10.1016/S0076-6879(81)77046-0
    • (1981) Methods Enzymol , vol.77 , pp. 325-333
    • Wendel, A.1
  • 25
    • 79551470306 scopus 로고    scopus 로고
    • Oxidative stress, insulin signaling, and diabetes
    • Rains JL, Jain SK. Oxidative stress, insulin signaling, and diabetes. Free Radic Biol Med. 2011; 50: 567-575. http://dx.doi.org/10.1016/j.freeradbiomed.2010.12.006
    • (2011) Free Radic Biol Med , vol.50 , pp. 567-575
    • Rains, J.L.1    Jain, S.K.2
  • 26
    • 33644931615 scopus 로고    scopus 로고
    • Protective effects of curcumin and its analogues free radical-induced oxidative haemolysis of human red blood cells
    • Deng SL, Chen WF, Yang BZL, Liu ZL. Protective effects of curcumin and its analogues free radical-induced oxidative haemolysis of human red blood cells. Food Chem. 2006; 98: 112-119. http://dx.doi.org/10.1016/j.foodchem.2005.05.063
    • (2006) Food Chem , vol.98 , pp. 112-119
    • Deng, S.L.1    Chen, W.F.2    Yang, B.3    Liu, Z.L.4
  • 27
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification. The potential role of “autoxidative glycosylation” in diabetes
    • Wolff SP, Dean RT. Glucose autoxidation and protein modification. The potential role of “autoxidative glycosylation” in diabetes. Biochem J. 1987; 245: 243-250. http://www.ncbi.nlm.nih.gov/pubmed/3117042
    • (1987) Biochem J , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 28
    • 0027384310 scopus 로고
    • Effect of fatty acids on energy coupling processes in mitochondria
    • Wojtczak L, Schönfeld P. Effect of fatty acids on energy coupling processes in mitochondria. Biochim Biophys Acta. 1993; 1183: 41-57. http://dx.doi.org/10.1016/0005-2728(93)90004-Y
    • (1993) Biochim Biophys Acta , vol.1183 , pp. 41-57
    • Wojtczak, L.1    Schönfeld, P.2
  • 29
    • 0033305516 scopus 로고    scopus 로고
    • Sodium palmitate induces partial mitochondrial uncoupling and reactive oxygen species in rat pancreatic islets in vitro
    • Carlsson C, Borg LA, Welsh N. Sodium palmitate induces partial mitochondrial uncoupling and reactive oxygen species in rat pancreatic islets in vitro. Endocrinology. 1999; 140: 3422-3428. http://dx.doi.org/10.1210/endo.140.8.6908
    • (1999) Endocrinology , vol.140 , pp. 3422-3428
    • Carlsson, C.1    Borg, L.A.2    Welsh, N.3
  • 31
    • 54949119528 scopus 로고    scopus 로고
    • Effect of curcumin supplementation on blood glucose, plasma insulin, and glucose homeostasis related enzyme activities in diabetic db/db mice
    • Seo K-I, Choi M-S, Jung UJ, Kim H-J, Yeo J, Jeon S-M, Lee M-K. Effect of curcumin supplementation on blood glucose, plasma insulin, and glucose homeostasis related enzyme activities in diabetic db/db mice. Mol Nutr Food Res. 2008; 52: 995-1004. http://dx.doi.org/10.1002/mnfr.200700184
    • (2008) Mol Nutr Food Res , vol.52 , pp. 995-1004
    • Seo, K.-I.1    Choi, M.-S.2    Jung, U.J.3    Kim, H.-J.4    Yeo, J.5    Jeon, S.-M.6    Lee, M.-K.7
  • 32
    • 0033404125 scopus 로고    scopus 로고
    • Taurine attenuates hypertension and improves insulin sensitivity in the fructose-fed rat, an animal model of insulin resistance
    • Anuradha CV, Balakrishnan SD. Taurine attenuates hypertension and improves insulin sensitivity in the fructose-fed rat, an animal model of insulin resistance. Can J Physiol Pharmacol. 1999; 77: 749-754. http://dx.doi.org/10.1139/cjpp-77-10-749
    • (1999) Can J Physiol Pharmacol , vol.77 , pp. 749-754
    • Anuradha, C.V.1    Balakrishnan, S.D.2
  • 33
    • 0034328771 scopus 로고    scopus 로고
    • Reactive oxygen species in health and disease
    • Datta K, Sinha S, Chattopadhyay P. Reactive oxygen species in health and disease. Natl Med J India. 2000; 13: 304-310. http://www.ncbi.nlm.nih.gov/pubmed/11209486
    • (2000) Natl Med J India , vol.13 , pp. 304-310
    • Datta, K.1    Sinha, S.2    Chattopadhyay, P.3
  • 35
    • 0032424771 scopus 로고    scopus 로고
    • Lipid peroxidation and antioxidants in oral squamous cell carcinoma
    • Nagini S, Manoharan S, Ramachandran CR. Lipid peroxidation and antioxidants in oral squamous cell carcinoma. Clin Chim Acta. 1998; 273: 95-98. http://dx.doi.org/10.1016/S0009-8981(98)00023-0
    • (1998) Clin Chim Acta , vol.273 , pp. 95-98
    • Nagini, S.1    Manoharan, S.2    Ramachandran, C.R.3
  • 36
    • 27444442482 scopus 로고    scopus 로고
    • Protective role of tetrahydrocurcumin (THC) an active principle of turmeric on chloroquine induced hepatotoxicity in rats
    • Pari L, Amali DR. Protective role of tetrahydrocurcumin (THC) an active principle of turmeric on chloroquine induced hepatotoxicity in rats. J Pharmacol Pharm Sci. 2005; 8: 115-123. http://www.ncbi.nlm.nih.gov/pubmed/15946605
    • (2005) J Pharmacol Pharm Sci , vol.8 , pp. 115-123
    • Pari, L.1    Amali, D.R.2
  • 37
    • 0032908758 scopus 로고    scopus 로고
    • Relation of structure of curcumin analogs to their potencies as inducers of Phase 2 detoxification enzymes
    • Dinkova-Kostova AT, Talalay P. Relation of structure of curcumin analogs to their potencies as inducers of Phase 2 detoxification enzymes. Carcinogenesis. 1999; 20: 911-914. http://dx.doi.org/10.1093/carcin/20.5.911
    • (1999) Carcinogenesis , vol.20 , pp. 911-914
    • Dinkova-Kostova, A.T.1    Talalay, P.2
  • 38
    • 84885918282 scopus 로고    scopus 로고
    • Effect of Ginger, Curcumin and Their Mixture on Blood Glucose and Lipids in Diabetic Rats
    • Khattab HAH, Al-Amoudi NS, Al-Faleh AA. Effect of Ginger, Curcumin and Their Mixture on Blood Glucose and Lipids in Diabetic Rats. Life Sci J. 2013; 10: 428-442.
    • (2013) Life Sci J , vol.10 , pp. 428-442
    • Khattab, H.1    Al-Amoudi, N.S.2    Al-Faleh, A.A.3
  • 39
    • 7444250712 scopus 로고    scopus 로고
    • Influence of dietary curcumin, capsaicin and garlic on the antioxidant status of red blood cells and the liver in high-fat-fed rats
    • Kempaiah RK, Srinivasan K. Influence of dietary curcumin, capsaicin and garlic on the antioxidant status of red blood cells and the liver in high-fat-fed rats. Ann Nutr Metab. 2004; 48: 314-320. http://dx.doi.org/10.1159/000081198
    • (2004) Ann Nutr Metab , vol.48 , pp. 314-320
    • Kempaiah, R.K.1    Srinivasan, K.2
  • 40
    • 0034097798 scopus 로고    scopus 로고
    • MAP kinase pathways activated by stress: The p38 MAPK pathway
    • Obata T, Brown GE, Yaffe MB. MAP kinase pathways activated by stress: the p38 MAPK pathway. Crit Care Med. 2000; 28 (Suppl): N67-N77. http://www.ncbi.nlm.nih.gov/pubmed/10807318
    • (2000) Crit Care Med , vol.28 , pp. N67-N77
    • Obata, T.1    Brown, G.E.2    Yaffe, M.B.3
  • 41
    • 0037341276 scopus 로고    scopus 로고
    • Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: Potential role of p38 in the downregulation of GLUT4 expression
    • Carlson CJ, Koterski S, Sciotti RJ, Poccard GB, Rondinone CM. Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression. Diabetes. 2003; 52: 634-641. http://dx.doi.org/10.2337/diabetes.52.3.634
    • (2003) Diabetes , vol.52 , pp. 634-641
    • Carlson, C.J.1    Koterski, S.2    Sciotti, R.J.3    Poccard, G.B.4    Rondinone, C.M.5
  • 42
    • 0038321436 scopus 로고    scopus 로고
    • Reduced activation of phosphatidylinositol-3 kinase and increased serine 636 phosphorylation of insulin receptor substrate-1 in primary culture of skeletal muscle cells from patients with type 2 diabetes
    • Bouzakri K, Roques M, Gual P, Espinosa S, Guebre-Egziabher F, Riou J-P, Laville M, Le Marchand-Brustel Y, Tanti J-F, Vidal H. Reduced activation of phosphatidylinositol-3 kinase and increased serine 636 phosphorylation of insulin receptor substrate-1 in primary culture of skeletal muscle cells from patients with type 2 diabetes. Diabetes. 2003; 52: 1319-1325. http://dx.doi.org/10.2337/diabetes.52.6.1319
    • (2003) Diabetes , vol.52 , pp. 1319-1325
    • Bouzakri, K.1    Roques, M.2    Gual, P.3    Espinosa, S.4    Guebre-Egziabher, F.5    Riou, J.-P.6    Laville, M.7    Le Marchand-Brustel, Y.8    Tanti, J.-F.9    Vidal, H.10
  • 43
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles LA, Woodgett JR. The stress-activated protein kinase pathways. Cell Mol Life Sci. 1999; 55: 1230-1254. http://www.ncbi.nlm.nih.gov/pubmed/10487205
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 44
    • 0030669392 scopus 로고    scopus 로고
    • Molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz K, Hemi R, LeRoith D, Karasik A, Elhanany E, Kanety H, Zick Y. A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J Biol Chem. 1997; 272: 29911-29918. http://dx.doi.org/10.1074/jbc.272.47.29911
    • (1997) J Biol Chem , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    Leroith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.A.7


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