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The Effects of Lycii Radicis Cortex on Inflammatory Response through an Oxidative Stress and AGEs-mediated Pathway in STZ-induced Diabetic Rats

  • Jung, Yu Sun (Department of Internal Medicine of Korean Medicine, College of Korean Medicine, Dae-gu Haany University) ;
  • Shin, Hyeon Cheol (Department of Internal Medicine of Korean Medicine, College of Korean Medicine, Dae-gu Haany University)
  • 투고 : 2016.02.15
  • 심사 : 2016.06.22
  • 발행 : 2016.06.30

초록

Objectives: This study examined whether Lycii Radicis Cortex has an inhibitory effect on inflammatory response through an oxidative stress and advanced glycation endproducts (AGEs)-mediated pathway in streptozotocin (STZ)-induced type 1 diabetic rats. Methods: Lycii Radicis Cortex was orally administered to STZ-induced diabetic rats in doses of 80 or 160 mg/kg body weight/day for 2 weeks, and its effects were compared with those of diabetic control and normal rats. Results: The administration of Lycii Radicis Cortex decreased the elevated serum urea nitrogen and renal reactive oxygen species (ROS), and reduced the increased AGEs in the serum and kidney. The elevated protein expressions of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase subunits in the kidney of diabetic control rats were significantly decreased after Lycii Radicis Cortex treatments. Moreover, the kidney of diabetic rats exhibited the up-regulation of receptor for AGEs (RAGE) and AGEs-related proteins; however, Lycii Radicis Cortex treatment also significantly reduced those expressions (excepted RAGE). In addition, the diabetic rats exhibited an up-regulation of the expression of proteins related to inflammation in the kidney, but Lycii Radicis Cortex administration reduced significantly the expression of the inflammatory proteins through the nuclear factor-kappa B (NF-${\kappa}B$) and activator protein-1 (AP-1) pathways. Conclusions: This study provides scientific evidence that Lycii Radicis Cortex exerts the antidiabetic effect by inhibiting the expressions of AGEs and NF-${\kappa}B$ in the STZ-induced diabetic rats.

키워드

참고문헌

  1. Peppa M, Vlassara H. Advanced glycation endproducts and diabetic complications: A general overview. Hormones. 2005;4:28-37. https://doi.org/10.14310/horm.2002.11140
  2. Kikkawa R, Koya D, Haneda M. Progression of diabetic nephropathy. Am. J. Kidney Dis. 2013; 41:S19-21.
  3. Forbes JM, Coughlan MT, Cooper ME. Oxidative stress as a major culprit in kidney disease in diabetes. Diabetes. 2008;57:1446-54. https://doi.org/10.2337/db08-0057
  4. Ruderman N, Wiliamson J, Brownlee M. Glucose and diabetic vascular disease. FASEB J. 1992;6:2905-14. https://doi.org/10.1096/fasebj.6.11.1644256
  5. Schmidt AM, Yan SD, Stern DM. The dark side of glucose. Nature. 1995;Med1:1002-4. https://doi.org/10.1038/nm1095-1002
  6. Neeper M, Schmidt AM, Brett J, Yan SD, Wang F, Pan YC, et al. Cloning and expression of a cell surface receptor for advanced glycosylation endproducts of proteins. J. Biol Chem. 1992; 267:14998-15004.
  7. Schmidt AM, Vianna M, Gerlach M, Brett J, Ryan J, Kao J, et al. Isolation and characterization of two binding proteins for advanced glycosylation endproducts from bovine lung which are present on the endothelial cell surface. J. Biol Chem. 1992;267:14987-97.
  8. Wautier MP, Chappey O, Corda S, Stern DM, Schmidt AM, Wautier JL. Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE. Am. J. Physiol Endocrinol Metab. 2001;280:E685-94. https://doi.org/10.1152/ajpendo.2001.280.5.E685
  9. Simm A, MuEnch G, Seif F, Schenk O, Heidland A, Richter H, et al. Advanced glycation endproducts stimulate the MAP-kinase pathway in tubulus cell line LLC-PK1. FEBS Lett. 1997;410:481-4. https://doi.org/10.1016/S0014-5793(97)00644-3
  10. Wang FY, Luo JY. Dictionary of Traditional Chinese Materia Medica. Hunan:Hunan Science and Technology Press. 2006:167.
  11. Funayama S, Yoshida K, Konno C, Hikino H. Structure of kukoamine A, a hypotensive principle of Lycium chinense root barks 1. Tetrahedron Lett. 1980;21:1355-6. https://doi.org/10.1016/S0040-4039(00)74574-6
  12. Chan JY, Leung PC, Che CT, Fung KP. Protective effects of an herbal formulation of Radix Astragali, Radix Condonopsis and Cortex Lycii on streptoaotocin-induced apaptosis in pancreatic beta-cells: an implication for its treatment of diabetes mellitus. Phytother. Rec. 2008;22:190-6. https://doi.org/10.1002/ptr.2285
  13. Cho SH, Park EJ, Kim EO, Choi SW. Study on the hypochlesterolemic and actioxidative effects of tyramine derivatives from the root bark of Lycii Radicis Cortex. Nut. Rec. Pract. 2011;5:412-20. https://doi.org/10.4162/nrp.2011.5.5.412
  14. Ye Z, Haung Q, Ni HX, Wang D. Cortex Lycii Radicis extracts improve insulin resistance and lipid metabolism in obese-diabetic rats. Phytother Res. 2008;22:1665-70. https://doi.org/10.1002/ptr.2552
  15. Jung YS, Park CH, Shin HC. Antioxidative effects of Lycium chinense Miller on cisplatin-induced nephrotoxicity in rats. Korean J. Orent. Int. Med. 2014;35:92-105.
  16. Hou DX, Yanagita T, Uto T, Masuzaki S, Fujii M. Anthocyanidins inhibt cyclooxygenase-2 expression in LPS-evoked macrophages: structure-activity relationship and molecular mechanisms involved. Biochem. Pharmacol. 2005;70:417-25. https://doi.org/10.1016/j.bcp.2005.05.003
  17. Jayaprakasam B, Vareed SK, Olson LK, Nair MG. Insulin secretion by bioactive anthocyanins and anthocyanidins present in fruits. J. Agric. Food Chem. 2005;53:28-31. https://doi.org/10.1021/jf049018+
  18. Yamakoshi J, Kataoka S, Koga T, Ariga T. Proanthocyanidin-rich extract of grape seeds attenuated the development of aortic atherosclerosis in cholesterol-fed rabbits. Atherosclerosis. 1999; 142:139-49. https://doi.org/10.1016/S0021-9150(98)00230-5
  19. Ye X, Krohn RL, Liu W, Joshi SS, Kuszynski CA, McGinn TR, et al. The cytotoxic effects of n novel IH636 grape seed proanthocyanidin extract on cultured human cancer cells. Mol. Cell. Biochem. 1999;196:99-108. https://doi.org/10.1023/A:1006926414683
  20. Ali SF, LeBel CP, Bondy SC. Reactive oxygen species formation as a biomarker of methylmercury and trimethyltin neurotoxicity. Neurotoxicology. 1992;13:637-48.
  21. McFarland KF, Catalano EW, Day JF, Thorpe SR, Baynes JW. Nonenzymatic glucosylation of serum proteins in diabetes mellitus. Diabetes. 1979;28:1011-4. https://doi.org/10.2337/diab.28.11.1011
  22. Momose T, Yano Y, Ohashi K. Organic analysis. XLIV. A new deproteinizing agent for determination of blood sugar. Chem. Pham. Bull. 1963;11: 968-72. https://doi.org/10.1248/cpb.11.968
  23. Nakayama H, Mitsuhashi T, Kuwajima S, Aoki S, Kuroda Y, Itoh Tet al. Chemical detection of advanced glycation endproducts in lens crystallins from streptozocin-induced diabetic rat. Diabetes. 1993;42:345-50. https://doi.org/10.2337/diab.42.2.345
  24. Komatsu S. Extraction of nuclear proteins. Methods Mol. Biol. 2007;355:73-7.
  25. Yokozawa T, Yamabe N, Kim HY, Kang KS, Hur JM, Park CH, et al. Protective effects of morroniside isolated from Corni Fructus against renal damage in streptozotocin-induced diabetic rats. Biol Pharm Bull. 2008;31:1422-8. https://doi.org/10.1248/bpb.31.1422
  26. Kim CM, Shin MG, Lee KS, Ahn DG. The encyclopedia of oriental herbal medicine. Seoul: Jungdam publishing group. 2004:3929-34.
  27. Al-Malki AL, Sayed AA, El Rabey HA. Proanthocyanidin attenuateion of oxidative stress and NF-${\kappa}$ B protects apolipoprotein E-deficient mice against diabetic nephropathy. Evidenc-Based Complementary and Alternative Medicine. 2013; 2013:1-8.
  28. Rosen P, Nawroth PP, King G, Moller W, Tritschler HJ, Packer L. The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society. Diabetes Metab Res Rev. 2001;17:189-212. https://doi.org/10.1002/dmrr.196
  29. Newsolme P, Haber EP, Hirabara SM, Rebelato EL, Procopio J, Morgan D et al. Diabetes associated cell stress and dysfunction: role of mitochondrial and non-mitochondrial ROS production and activity. J. Physiol. 2007;583: 9-24. https://doi.org/10.1113/jphysiol.2007.135871
  30. Kashihara N, Haruna Y, Kondeti VK, Kanwar YS. Oxidative stress in diabetic nephropathy. Curr Med Chem. 2010;17:4256-69. https://doi.org/10.2174/092986710793348581
  31. Tooke JE. Possible pathophysiological mechanisms for diabetic angiopathy in type 2 diabetes. J. Diabetes Complications. 2000;14:197-200. https://doi.org/10.1016/S1056-8727(00)00083-0
  32. Singh VP, Bali A, Singh N, Jaqqi AS. Advanced glycation endproducts and diabetic complications. Korean J Physiol Pharmacol. 2014;18:1-14. https://doi.org/10.4196/kjpp.2014.18.1.1
  33. Schinzel R, Munch G, Heidland A, Sebecova K. Advanced glycation endproducts in end-stage renal disease and their removal. Nephron. 2001; 87:295-303. https://doi.org/10.1159/000045934
  34. Horie K, Miyata T, Maeda K, Miyata S, Suqiyama S, Sakai H, et al. Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions. Implications for glycoxidative stress in the pathogenesis of diabetic nephropathy. J. Clin Invest. 1997;100: 2995-3004. https://doi.org/10.1172/JCI119853
  35. Ceriello A, Bortolotti N, Pirisi M, Crescentini A, Tonutti L, Motz E, et al. Total plasma antioxidant capacity predicts thrombosis-prone status in NDDM patients. Diabetes Care. 1997; 20:1589-93. https://doi.org/10.2337/diacare.20.10.1589
  36. Bierhaus A, Schiekofer S, Schwaninger M, Andrassy M, Humpert PM, Chen J, et al. Diabetes-associated sustained activation of the transcription factor nuclear factor-kappa B. Diabetes. 2001;50:2792-808. https://doi.org/10.2337/diabetes.50.12.2792
  37. Nagi R, Ikeda K, Higashi T, Sano H, Jinnouchi Y, Araki T, et al. Hydroxyl radical mediates N epsilon-(carboxymethyl)lysine formation from Amadori product. Biochem Biophys Res Commun. 1997;234:167-72. https://doi.org/10.1006/bbrc.1997.6608
  38. Nagi R, Unno Y, Hayashi MC, Masuda S, Hayase F, Kinae N, et al. Peroxynitrite induces formation of N(epsilon)-(carboxymethyl) lysine by the caleavage of Amadori product and generation of glucosone and glyoxal from glucose: novel pathways for protein modification by peroxynitrite. Diabetes. 2002;51:2833-89. https://doi.org/10.2337/diabetes.51.9.2833
  39. Wells-Knecht KJ, Zyzak DV, Litchfield JE, Thorpe SR, Baynes JW. Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry. 1995;34:3702-9. https://doi.org/10.1021/bi00011a027
  40. Koito W, Araki T, Horiuchi S, Nagai R. Conventional antibody against epsilon-(carboxymethyl) lysine (CML) shows cross-reaction to Nepsilon-(carboxyethyl)lysine (CEL): immnochemical quantification of CML with a specific antibody. J. Biochem. 2004;136:831-837. https://doi.org/10.1093/jb/mvh193
  41. Ahmed MU, Frye EB, Degenhardt TP, Thorpe SR, Baynes JW. Ne-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increase with age in human lens proteins. Biochem. J. 1997;324:565-70. https://doi.org/10.1042/bj3240565
  42. Lim AK, Tesch GH. Inflammation in diabetic nephropathy. Mediators Inflamm. 2012;2012: 1-12.
  43. Lee JI, Burckart GJ. Nuclear factor kappa B: important transcription factor and therapeutic target. J. Clin. Pharmacol. 1998;38:981-93. https://doi.org/10.1177/009127009803801101
  44. Baldwin AS Jr. NF-kappa B and I kappa B proteins: new discoveries and insights. Annu Rev Immunol. 1996;14:649-83. https://doi.org/10.1146/annurev.immunol.14.1.649
  45. Sanchez AP, Sharma K. Transcription factors in the pathogenesis of diabetic nephropathy. Expert Rev Mol Med. 2009;11:e13. https://doi.org/10.1017/S1462399409001057
  46. Hess J, Anqel P, Schorpp-Kistner M. AP-1 subunits: quarrel and harmony among siblings. J Cell Sci. 2004;117:5965-73. https://doi.org/10.1242/jcs.01589

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