한국식품저장유통학회지 (Food Science and Preservation)

  • 제24권4호
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  • Pages.536-541
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  • 2017
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  • 3022-5477(pISSN)
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  • 3022-5485(eISSN)
한국식품저장유통학회 (The Korean Society of Food Preservation)
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Inhibitory effects of curcumin on high glucose-induced damages: Implications for alleviating diabetic complications

  • 투고 : 2017.05.11
  • 심사 : 2017.07.14
  • 발행 : 2017.07.30
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초록

Hyperglycemia found in diabetes mellitus causes several physiological abnormalities including the formation of advanced glycation end products (AGEs) and oxidative stress. Accumulation of AGEs and elevation of oxidative stress plays major roles in the development of diabetic complications. Adiponectin secreted from adipocytes is known to improve insulin sensitivity and blood glucose level. Curcumin (CCM), a bioactive component of turmeric, has been reported as a potent antioxidant. Present work aimed to elucidate the roles of CCM in high glucose-induced protein glycation and intracellular events in mature adipocytes. The results demonstrated that CCM inhibited the formation of fluorescent AGEs by approximated 52% at 3 weeks of bovine serum albumin (BSA) glycation with glucose. Correspondingly, CCM decreased the levels of fructosamine and ${\alpha}-dicarbonyl$ compounds during BSA glycation with glucose. These data suggested that CCM might be a new promising anti-glycation agent. Also, CCM reduced high glucose-induced oxidative stress in a dose dependent manner, whereas CCM treatment time-dependently elevated the expression of adiponectin gene in 3T3-L1 adipocytes. The findings from this study suggested the possibility of therapeutic use of CCM for the prevention of diabetic complications and obesity-related diseases.

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참고문헌

  1. Brownlee M (2001) Biochemistry and molecular cell biology of diabetic complications. Nature, 414, 813-820 https://doi.org/10.1038/414813a
  2. Giacco F, Brownlee M (2010) Oxidative stress and diabetic complications. Circ Res, 107, 1058-1070 https://doi.org/10.1161/CIRCRESAHA.110.223545
  3. Finkel T, Holbrook NJ (2000) Oxidants, oxidative stress and the biology of ageing. Nature, 408, 239-247 https://doi.org/10.1038/35041687
  4. Yan SD, Schmidt AM, Anderson GM, Zhang J, Brett J, Zou YS, Pinsky D, Stern D (1994) Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J Biol Chem, 269, 9889-9897
  5. Zhang Q, Ames JM, Smith RD, Baynes JW, Metz TO (2009) A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease. J Proteome Res, 8, 754-769 https://doi.org/10.1021/pr800858h
  6. Neelofar K, Arif Z, Alam K, Ahmad J (2016) Hyperglycemia induced structural and functional changes in human serum albumin of diabetic patients: a physico-chemical study. Mol Biosyst, 12, 2481-2489 https://doi.org/10.1039/C6MB00324A
  7. Weyer C, Funahashi T, Tanaka S, Hotta K, Matsuzawa Y, Pratley RE, Tataranni PA (2001) Hypoadiponectinemia in obesity and type 2 diabetes: close association with insulin resistance and hyperinsulinemia. J Clin Endocrinol Metab, 86, 1930-1935 https://doi.org/10.1210/jcem.86.5.7463
  8. Hu E, Liang P, Spiegelman BM (1996) AdipoQ is a novel adipose-specific gene dysregulated in obesity. J Biol Chem, 271, 10697-10703 https://doi.org/10.1074/jbc.271.18.10697
  9. Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, Mori Y, Ide T, Murakami K, Tsuboyama-Kasaoka N, Ezaki O, Akanuma Y, Gavrilova O, Vinson C, Reitman ML, Kagechika H, Shudo K, Yoda M, Nakano Y, Tobe K, Nagai R, Kimura S, Tomita M, Froguel P, Kadowaki T (2001) The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med, 7, 941-946 https://doi.org/10.1038/90984
  10. Nakagawa T, Yokozawa T, Terasawa K, Shu S, Juneja LR (2002) Protective activity of green tea against free radical-and glucose-mediated protein damage. J Agric Food Chem, 50, 2418-2422 https://doi.org/10.1021/jf011339n
  11. Vinson JA, Howard TB (1996) Inhibition of protein glycation and advanced glycation end products by ascorbic acid and other vitamins and nutrients. The J Nutr Biochem, 7, 659-663 https://doi.org/10.1016/S0955-2863(96)00128-3
  12. Shishodia S, Sethi G, Aggarwal BB (2005) Curcumin: Getting back to the roots. Ann N Y Acad Sci, 1056, 206-217 https://doi.org/10.1196/annals.1352.010
  13. Anand P, Thomas SG, Kunnumakkara AB, Sundaram C, Harikumar KB, Sung B, Tharakan ST, Misra K, Priyadarsini IK, Rajasekharan KN, Aggarwal BB (2008) Biological activities of curcumin and its analogues (Congeners) made by man and Mother Nature. Biochem Pharmacol, 76, 1590-1611 https://doi.org/10.1016/j.bcp.2008.08.008
  14. Kim CY, Le TT, Chen C, Cheng JX, Kim KH (2011) Curcumin inhibits adipocyte differentiation through modulation of mitotic clonal expansion. J Nutr Biochem, 22, 910-920 https://doi.org/10.1016/j.jnutbio.2010.08.003
  15. Wu JW, Hsieh CL, Wang HY, Chen HY (2009) Inhibitory effects of guava (Psidium guajava L.) leaf extracts and its active compounds on the glycation process of protein. Food Chem, 113, 78-84 https://doi.org/10.1016/j.foodchem.2008.07.025
  16. Mitchel R, Birnboim HC (1977) The use of Girard-T reagent in a rapid and sensitive method for measuring glyoxal and certain other ${\alpha}$-dicarbonyl compounds. Anal Biochem, 81, 47-56 https://doi.org/10.1016/0003-2697(77)90597-8
  17. Chen CY, Abell AM, Moon YS, Kim KH (2012) An advanced glycation end product (AGE)-receptor for AGEs (RAGE) axis restores adipogenic potential of senescent preadipocytes through modulation of p53 protein function. J Biol Chem, 287, 44498-44507 https://doi.org/10.1074/jbc.M112.399790
  18. Kim CY, Bordenave N, Ferruzzi MG, Safavy A, Kim KH (2011) Modification of curcumin with polyethylene glycol enhances the delivery of curcumin in preadipocytes and its antiadipogenic property. J Agric Food Chem, 59, 1012-1019 https://doi.org/10.1021/jf103873k
  19. Keen H, Fukker JH, Menzinger G (1997) Early closure of European Pimagedine trial. Lancet, 350, 214-215 https://doi.org/10.1016/S0140-6736(97)26029-0
  20. Thilavech T, Ngamukote S, Abeywardena M, Adisakwattana S (2015) Protective effects of cyanidin-3-rutinoside against monosaccharides-induced protein glycation and oxidation. Int J Biol Macromol, 75, 515-520 https://doi.org/10.1016/j.ijbiomac.2015.02.004
  21. Wang J, Sun B, Cao Y, Tian Y (2009) Protein glycation inhibitory activity of wheat bran feruloyl oligosaccharides. Food Chem, 112, 350-353 https://doi.org/10.1016/j.foodchem.2008.05.072
  22. Evert AB, Boucher JL, Cypress M, Dunbar SA, Franz MJ, Mayer-Davis EJ, Neumiller JJ, Nwankwo R, Verdi CL, Urbanski P, Yancy WS (2013) Nutrition therapy recommendations for the management of adults with diabetes. Diabetes Care, 36, 3821-3842 https://doi.org/10.2337/dc13-2042
  23. Kadowaki T, Yamauchi T (2005) Adiponectin and adiponectin receptors. Endocr Rev, 26, 439-451 https://doi.org/10.1210/er.2005-0005
  24. Hassan M, El Yazidi C, Landrier JF, Lairon D, Margotat A, Amiot MJ (2007) Phloretin enhances adipocyte differentiation and adiponectin expression in 3T3-L1 cells. Biochem Biophys Res Commun, 361, 208-213 https://doi.org/10.1016/j.bbrc.2007.07.021
  25. Sharma AK, Bharti S, Ojha S, Bhatia J, Kumar N, Ray R, Kumari S, Arya DS (2011) Up-regulation of $PPAR{\gamma}$, heat shock protein-27 and-72 by naringin attenuates insulin resistance, ${\beta}$-cell dysfunction, hepatic steatosis and kidney damage in a rat model of type 2 diabetes. Br J Nutr, 106, 1713-1723 https://doi.org/10.1017/S000711451100225X

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