메뉴 건너뛰기




Volumn 393, Issue 1-2, 2014, Pages 111-122

Redox regulation of antioxidant enzymes: Post-translational modulation of catalase and glutathione peroxidase activity by resveratrol in diabetic rat liver

Author keywords

Catalase; Diabetes; Glutathione peroxidase; Protein phosphorylation; Resveratrol

Indexed keywords

CATALASE; CYTOPLASM PROTEIN; GLUTATHIONE PEROXIDASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; RESVERATROL; SIRTUIN 1; TRANSCRIPTION FACTOR NRF2; GLUCOSE BLOOD LEVEL; NFE2L2 PROTEIN, RAT; SIRT1 PROTEIN, RAT; STILBENE DERIVATIVE; SUPEROXIDE DISMUTASE;

EID: 84903478895     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-014-2051-1     Document Type: Article
Times cited : (76)

References (51)
  • 1
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • doi:10.1161/CIRCRESAHA.110.223545
    • Giacco F, Brownlee M (2010) Oxidative stress and diabetic complications. Circ Res 107:1058-1070. doi:10.1161/CIRCRE SAHA.110.223545
    • (2010) Circ Res , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 2
    • 77953474824 scopus 로고    scopus 로고
    • Plant polyphenols as dietary antioxidants in human health and disease
    • Pandey KB (2009) Plant polyphenols as dietary antioxidants in human health and disease. Oxid Med Cell Longev 2:270-278
    • (2009) Oxid Med Cell Longev , vol.2 , pp. 270-278
    • Pandey, K.B.1
  • 3
    • 78851469053 scopus 로고    scopus 로고
    • Anti-diabetic effects of resveratrol
    • doi:10.1111/j.1749-6632.2010.05844.x
    • Szkudelski T, Szkudelska K (2011) Anti-diabetic effects of resveratrol. Ann N Y Acad Sci 1215:34-39. doi:10.1111/j.1749-6632.2010.05844.x
    • (2011) Ann N Y Acad Sci , vol.1215 , pp. 34-39
    • Szkudelski, T.1    Szkudelska, K.2
  • 4
    • 70349265983 scopus 로고    scopus 로고
    • Resveratrol: Cellular actions of a potent natural chemical that confers a diversity of health benefits
    • doi:10.1016/j.biocel.2009.06.003
    • Marques FZ, Markus MA, Morris BJ (2009) Resveratrol : cellular actions of a potent natural chemical that confers a diversity of health benefits. Int J Biochem Cell Biol 41:2125-2128. doi:10. 1016/j.biocel.2009.06.003
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2125-2128
    • Marques, F.Z.1    Markus, M.A.2    Morris, B.J.3
  • 5
    • 77952321187 scopus 로고    scopus 로고
    • Resveratrol, obesity and diabetes
    • doi:10.1016/j.ejphar.2010.02.054
    • Szkudelska K, Szkudelski T (2010) Resveratrol, obesity and diabetes. Eur J Pharmacol 635:1-8. doi:10.1016/j.ejphar.2010.02. 054
    • (2010) Eur J Pharmacol , vol.635 , pp. 1-8
    • Szkudelska, K.1    Szkudelski, T.2
  • 6
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: The in vivo evidence
    • doi:10.1038/nrd2060
    • Baur J, Sinclair D (2006) Therapeutic potential of resveratrol: the in vivo evidence. Nat Rev Drug Discov 5:493-506. doi:10.1038/ nrd2060
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 493-506
    • Baur, J.1    Sinclair, D.2
  • 7
    • 0036130279 scopus 로고    scopus 로고
    • Resveratrol and cancer: A review
    • DOI 10.1016/S0753-3322(01)00158-5
    • Savouret JF, Quesne M (2002) Resveratrol and cancer: a review. Biomed Pharmacother 56:84-87 (Pubitemid 34241562)
    • (2002) Biomedicine and Pharmacotherapy , vol.56 , Issue.2 , pp. 84-87
    • Savouret, J.F.1    Quesne, M.2
  • 8
    • 34547101726 scopus 로고    scopus 로고
    • Resveratrol alleviates cardiac dysfunction in streptozotocininduced diabetes: Role of nitric oxide, thioredoxin, and heme oxygenase
    • doi:10.1016/j.freeradbiomed.2007.05.004
    • Thirunavukkarasu M, Penumathsa SV, Koneru S et al (2007) Resveratrol alleviates cardiac dysfunction in streptozotocininduced diabetes: role of nitric oxide, thioredoxin, and heme oxygenase. Free Radic Biol Med 43:720-729. doi:10.1016/j.free radbiomed.2007.05.004
    • (2007) Free Radic Biol Med , vol.43 , pp. 720-729
    • Thirunavukkarasu, M.1    Penumathsa, S.V.2    Koneru, S.3
  • 10
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • doi:10.1016/j.ceb.2005.02.004
    • Rhee S, Kang SW, Jeong W et al (2005) Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr Opin Cell Biol 17:183-189. doi:10.1016/j.ceb.2005. 02.004
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.1    Kang, S.W.2    Jeong, W.3
  • 11
    • 0042867423 scopus 로고    scopus 로고
    • Cellular regulation by hydrogen peroxide
    • doi:10.1097/01.ASN.0000077404.45564.7E
    • Rhee SG (2003) Cellular regulation by hydrogen peroxide. J Am Soc Nephrol 14:211S-215S. doi:10.1097/01.ASN.0000077404. 45564.7E
    • (2003) J Am Soc Nephrol , vol.14
    • Rhee, S.G.1
  • 12
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of Type 2 diabetes
    • doi:10.1210/er.2001-0039
    • Evans JL (2002) Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of Type 2 diabetes. Endocr Rev 23:599-622. doi:10.1210/er.2001-0039
    • (2002) Endocr Rev , vol.23 , pp. 599-622
    • Evans, J.L.1
  • 13
    • 2342514015 scopus 로고    scopus 로고
    • An important role of Nrf2-ARE pathway in the cellular defense mechanism
    • Lee J-M, Johnson J a (2004) An important role of Nrf2-ARE pathway in the cellular defense mechanism. J Biochem Mol Biol 37:139-143
    • (2004) J Biochem Mol Biol , vol.37 , pp. 139-143
    • Lee, J.-M.1    Johnson, J.A.2
  • 14
    • 79954508354 scopus 로고    scopus 로고
    • NF-KB activation in organs from STZ-treated rats
    • doi:10.1139/H10-094
    • Locke M, Anderson J (2011) NF-KB activation in organs from STZ-treated rats. Appl Physiol Nutr Metab 36:121-127. doi:10.1139/H10-094
    • (2011) Appl Physiol Nutr Metab , vol.36 , pp. 121-127
    • Locke, M.1    Anderson, J.2
  • 15
    • 84873720266 scopus 로고    scopus 로고
    • Resveratrol improves diabetic retinopathy possibly through oxidative stress- nuclear factor KB-apoptosis pathway
    • Soufi FG, Mohammad-Nejad D, Ahmadieh H (2012) Resveratrol improves diabetic retinopathy possibly through oxidative stress- nuclear factor KB-apoptosis pathway. Pharmacol Rep 64:1505-1514
    • (2012) Pharmacol Rep , vol.64 , pp. 1505-1514
    • Soufi, F.G.1    Mohammad-Nejad, D.2    Ahmadieh, H.3
  • 16
    • 84874108083 scopus 로고    scopus 로고
    • Seven sirtuins for seven deadly diseases of aging
    • doi:10.1016/j.freeradbiomed.2012.10.525
    • Morris BJ (2013) Seven sirtuins for seven deadly diseases of aging. Free Radic Biol Med 56:133-171. doi:10.1016/j.free radbiomed.2012.10.525
    • (2013) Free Radic Biol Med , vol.56 , pp. 133-171
    • Morris, B.J.1
  • 17
    • 84866120819 scopus 로고    scopus 로고
    • Selenium downregulates RAGE and NFKB expression in diabetic rats
    • doi:10.1007/s12011-012-9401-1
    • Pillai SS, Sugathan JK, Indira M (2012) Selenium downregulates RAGE and NFKB expression in diabetic rats. Biol Trace Elem Res 149:71-77. doi:10.1007/s12011-012-9401-1
    • (2012) Biol Trace Elem Res , vol.149 , pp. 71-77
    • Pillai, S.S.1    Sugathan, J.K.2    Indira, M.3
  • 18
    • 78751703950 scopus 로고    scopus 로고
    • Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution
    • doi:10.1111/j.1365-2443.2010.01473.x
    • Taguchi K, Motohashi H, Yamamoto M (2011) Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution. Genes Cells 16:123-140. doi:10.1111/j.1365-2443.2010.01473.x
    • (2011) Genes Cells , vol.16 , pp. 123-140
    • Taguchi, K.1    Motohashi, H.2    Yamamoto, M.3
  • 19
    • 0042905738 scopus 로고    scopus 로고
    • Catalase activity is regulated by c-Abl and Arg in the oxidative stress response
    • DOI 10.1074/jbc.M301292200
    • Cao C, Leng Y, Kufe D (2003) Catalase activity is regulated by c-Abl and Arg in the oxidative stress response. J Biol Chem 278:29667-29675. doi:10.1074/jbc.M301292200 (Pubitemid 36962352)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29667-29675
    • Cao, C.1    Leng, Y.2    Kufe, D.3
  • 20
    • 0141994844 scopus 로고    scopus 로고
    • Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases
    • DOI 10.1074/jbc.M305770200
    • Cao C, Leng Y, Huang W et al (2003) Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases. J Biol Chem 278:39609-39614. doi:10.1074/jbc.M305770200 (Pubitemid 37248520)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39609-39614
    • Cao, C.1    Leng, Y.2    Huang, W.3    Liu, X.4    Kufe, D.5
  • 22
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1992) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnology 24:145-149
    • (1992) Biotechnology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 23
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 24
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak J, Lindsay RH (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal Biochem 25:192-205
    • (1968) Anal Biochem , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 25
    • 0028873551 scopus 로고
    • Elevated lipid peroxidation and vitamin E-quinone levels in heart ventricles of streptozotocintreated diabetic rats
    • Jain SK, Levine SN (1995) Elevated lipid peroxidation and vitamin E-quinone levels in heart ventricles of streptozotocintreated diabetic rats. Free Radic Biol Med 18:337-341
    • (1995) Free Radic Biol Med , vol.18 , pp. 337-341
    • Jain, S.K.1    Levine, S.N.2
  • 27
    • 0000524408 scopus 로고
    • In methods in enzymology
    • Academy Press, New York
    • Aebi H (1984) In methods in enzymology. Catalase Vitr. Academy Press, New York, pp 121-126
    • (1984) Catalase Vitr , pp. 121-126
    • Aebi, H.1
  • 28
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia D, Valentine W (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158-169
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.1    Valentine, W.2
  • 29
    • 77952549960 scopus 로고    scopus 로고
    • Resveratrol, sirtuins, and the promise of a DR mimetic
    • doi:10.1016/j.mad.2010.02.007
    • Baur JA (2010) Resveratrol, sirtuins, and the promise of a DR mimetic. Mech Ageing Dev 131:261-269. doi:10.1016/j.mad. 2010.02.007
    • (2010) Mech Ageing Dev , vol.131 , pp. 261-269
    • Baur, J.A.1
  • 30
    • 33746862126 scopus 로고    scopus 로고
    • Resveratrol inhibits insulin responses in a SirT1-independent pathway
    • doi:10.1042/BJ20050977
    • Zhang J (2006) Resveratrol inhibits insulin responses in a SirT1-independent pathway. Biochem J 397:519-527. doi:10.1042/ BJ20050977
    • (2006) Biochem J , vol.397 , pp. 519-527
    • Zhang, J.1
  • 31
    • 70350462756 scopus 로고    scopus 로고
    • Resveratrol opposite effects on rat tissue lipoperoxidation: Prooxidant during day-time and antioxidant at night
    • doi:10.1179/135100009X466131
    • Gadacha W, Ben-Attia M, Bonnefont-Rousselot D et al (2009) Resveratrol opposite effects on rat tissue lipoperoxidation: prooxidant during day-time and antioxidant at night. Redox Rep 14:154-158. doi:10.1179/135100009X466131
    • (2009) Redox Rep , vol.14 , pp. 154-158
    • Gadacha, W.1    Ben-Attia, M.2    Bonnefont-Rousselot, D.3
  • 32
    • 53049083034 scopus 로고    scopus 로고
    • Resveratrol modulates pyrogallol-induced changes in hepatic toxicity markers, xenobiotic metabolizing enzymes and oxidative stress
    • doi:10.1016/j.ejphar.2008.08.019
    • Upadhyay G, Singh AK, Kumar A et al (2008) Resveratrol modulates pyrogallol-induced changes in hepatic toxicity markers, xenobiotic metabolizing enzymes and oxidative stress. Eur J Pharmacol 596:146-152. doi:10.1016/j.ejphar. 2008.08.019
    • (2008) Eur J Pharmacol , vol.596 , pp. 146-152
    • Upadhyay, G.1    Singh, A.K.2    Kumar, A.3
  • 33
    • 11144342740 scopus 로고    scopus 로고
    • Redox regulation of protein-tyrosine phosphatases
    • DOI 10.1016/j.abb.2004.05.024, PII S0003986104003182
    • Den Hertog J, Groen A, Van Der Wijk T (2005) Redox regulation of protein-tyrosine phosphatases. Arch Biochem Biophys 434:11-15. doi:10.1016/j.abb.2004.05.024 (Pubitemid 40040465)
    • (2005) Archives of Biochemistry and Biophysics , vol.434 , Issue.1 SPEC. ISS. , pp. 11-15
    • Den, H.J.1    Groen, A.2    Van Der, W.T.3
  • 34
    • 2342468058 scopus 로고    scopus 로고
    • Effect of resveratrol and catechin on PC12 tyrosine kinase activities and their synergistic protection from beta-amyloid toxicity
    • Conte A, Pellegrini S, Tagliazucchi D (2003) Effect of resveratrol and catechin on PC12 tyrosine kinase activities and their synergistic protection from beta-amyloid toxicity. Drugs Exp Clin Res 29:243-255 (Pubitemid 38568631)
    • (2003) Drugs under Experimental and Clinical Research , vol.29 , Issue.5-6 , pp. 243-255
    • Conte, A.1    Pellegrini, S.2    Tagliazucchi, D.3
  • 35
    • 0032994036 scopus 로고    scopus 로고
    • Effect of resveratrol and some other natural compounds on tyrosine kinase activity and on cytolysis
    • Palmieri L, Mameli M, Ronca G (1999) Effect of resveratrol and some other natural compounds on tyrosine kinase activity and on cytolysis. Drugs Exp Clin Res 25:79-85 (Pubitemid 29257598)
    • (1999) Drugs under Experimental and Clinical Research , vol.25 , Issue.2-3 , pp. 79-85
    • Palmieri, L.1    Mameli, M.2    Ronca, G.3
  • 38
    • 29944442853 scopus 로고    scopus 로고
    • Glutathione homeostasis and redox-regulation by sulfhydryl groups
    • DOI 10.1007/s11120-005-8425-1
    • Meyer AJ, Hell R (2005) Glutathione homeostasis and redoxregulation by sulfhydryl groups. Photosynth Res 86:435-457. doi:10.1007/s11120-005-8425-1 (Pubitemid 43042765)
    • (2005) Photosynthesis Research , vol.86 , Issue.3 , pp. 435-457
    • Meyer, A.J.1    Hell, R.2
  • 39
    • 28844491761 scopus 로고    scopus 로고
    • Redox-based mechanisms in diabetes
    • doi:10.1089/ars.2005.7.1483
    • Stevens MJ (2005) Redox-based mechanisms in diabetes. Antioxid Redox Signal 7:1483-1485. doi:10.1089/ars.2005.7.1483
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1483-1485
    • Stevens, M.J.1
  • 40
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses
    • doi:10.1105/ tpc.105.033589
    • Foyer CH, Noctor G (2005) Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses. Plant Cell 17:1866-1875. doi:10.1105/ tpc.105.033589
    • (2005) Plant Cell , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 41
    • 0037630403 scopus 로고    scopus 로고
    • Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response
    • doi:10. 1074/jbc.M300058200
    • Cao C, Leng Y, Li C, Kufe D (2003) Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response. J Biol Chem 278:12961-12967. doi:10. 1074/jbc.M300058200
    • (2003) J Biol Chem , vol.278 , pp. 12961-12967
    • Cao, C.1    Leng, Y.2    Li, C.3    Kufe, D.4
  • 42
    • 84855848324 scopus 로고    scopus 로고
    • Effects of resveratrol on biomarkers of oxidative stress and on the activity of delta aminolevulinic acid dehydratase in liver and kidney of streptozotocin-induced diabetic rats
    • doi:10.1016/j.biochi.2011.08.005
    • Schmatz R, Perreira LB, Stefanello N et al (2012) Effects of resveratrol on biomarkers of oxidative stress and on the activity of delta aminolevulinic acid dehydratase in liver and kidney of streptozotocin-induced diabetic rats. Biochimie 94:374-383. doi:10.1016/j.biochi.2011.08.005
    • (2012) Biochimie , vol.94 , pp. 374-383
    • Schmatz, R.1    Perreira, L.B.2    Stefanello, N.3
  • 43
    • 27944474377 scopus 로고    scopus 로고
    • Redoxdependent transcriptional regulation
    • doi:10.1161/01.RES.0000188210.72062.10
    • Hongjun L, Colavitti R, Rovira II, Finkel T (2005) Redoxdependent transcriptional regulation. Circ Res 97:967-974. doi:10.1161/01.RES.0000188210. 72062.10
    • (2005) Circ Res , vol.97 , pp. 967-974
    • Hongjun, L.1    Colavitti, R.2    Rovira, I.I.3    Finkel, T.4
  • 44
    • 84875441398 scopus 로고    scopus 로고
    • Alphalipoic acid upregulates antioxidant enzyme gene expression and enzymatic activity in diabetic rat kidneys through an O-GlcNAc-dependent mechanism
    • doi:10.1007/s00394-012-0452-z
    • Arambašić J, Mihailović M, Uskoković A et al (2013) Alphalipoic acid upregulates antioxidant enzyme gene expression and enzymatic activity in diabetic rat kidneys through an O-GlcNAc-dependent mechanism. Eur J Nutr 52:1461-1473. doi:10.1007/ s00394-012-0452-z
    • (2013) Eur J Nutr , vol.52 , pp. 1461-1473
    • Arambašić, J.1    Mihailović, M.2    Uskoković, A.3
  • 45
    • 84880770415 scopus 로고    scopus 로고
    • Decreased O-GlcNAcylation of the key proteins in kinase and redox signalling pathways is a novel mechanism of the beneficial effect of α-lipoic acid in diabetic liver
    • doi:10.1017/S0007114512005429
    • Dinić S, Arambašić J, Mihailović M et al (2013) Decreased O-GlcNAcylation of the key proteins in kinase and redox signalling pathways is a novel mechanism of the beneficial effect of α-lipoic acid in diabetic liver. Br J Nutr 110(3):1-12. doi:10.1017/S0007114512005429
    • (2013) Br J Nutr , vol.110 , Issue.3 , pp. 1-12
    • Dinić, S.1    Arambašić, J.2    Mihailović, M.3
  • 46
    • 84862282913 scopus 로고    scopus 로고
    • Prevention of diabetic complications by activation of Nrf2: Diabetic cardiomyopathy and nephropathy
    • doi:10.1155/2012/216512
    • Li B, Liu S, Miao L, Cai L (2012) Prevention of diabetic complications by activation of Nrf2: diabetic cardiomyopathy and nephropathy. Exp Diabetes Res 2012:1-7. doi:10.1155/2012/216512
    • (2012) Exp Diabetes Res , vol.2012 , pp. 1-7
    • Li, B.1    Liu, S.2    Miao, L.3    Cai, L.4
  • 47
    • 79955634116 scopus 로고    scopus 로고
    • Resveratrol protects diabetic kidney by attenuating hyperglycemia- mediated oxidative stress and renal inflammatory cytokines via Nrf2-Keap1 signaling
    • doi:10.1016/j.bbadis.2011.03.008
    • Palsamy P, Subramanian S (2011) Resveratrol protects diabetic kidney by attenuating hyperglycemia-mediated oxidative stress and renal inflammatory cytokines via Nrf2-Keap1 signaling. Biochim Biophys Acta 1812:719-731. doi:10.1016/j.bbadis.2011.03.008
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 719-731
    • Palsamy, P.1    Subramanian, S.2
  • 48
    • 84859417290 scopus 로고    scopus 로고
    • Chromium picolinate and chromium histidinate protects against renal dysfunction by modulation of NF-KB pathway in high-fat diet fed and Streptozotocin-induced diabetic rats
    • doi:10.1186/1743-7075-9-30
    • Selcuk MY, Aygen B, Dogukan A et al (2012) Chromium picolinate and chromium histidinate protects against renal dysfunction by modulation of NF-KB pathway in high-fat diet fed and Streptozotocin-induced diabetic rats. Nutr Metab (Lond) 9:30. doi:10.1186/1743-7075-9-30
    • (2012) Nutr Metab (Lond) , vol.9 , pp. 30
    • Selcuk, M.Y.1    Aygen, B.2    Dogukan, A.3
  • 49
    • 78549295159 scopus 로고    scopus 로고
    • STZ-induced skeletal muscle atrophy is associated with increased p65 content and downregulation of insulin pathway without NF-KB canonical cascade activation
    • doi:10.1007/s00592-010-0209-1
    • Kelleher AR, Fairchild TJ, Keslacy S (2010) STZ-induced skeletal muscle atrophy is associated with increased p65 content and downregulation of insulin pathway without NF-KB canonical cascade activation. Acta Diabetol 47:315-323. doi:10.1007/ s00592-010-0209-1
    • (2010) Acta Diabetol , vol.47 , pp. 315-323
    • Kelleher, A.R.1    Fairchild, T.J.2    Keslacy, S.3
  • 50
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span
    • doi:10.1016/j.cell.2008.10.052
    • Kawahara TLA, Michishita E, Adler AS et al (2009) SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell 136:62-74. doi:10. 1016/j.cell.2008.10.052
    • (2009) Cell , vol.136 , pp. 62-74
    • Kawahara, T.L.A.1    Michishita, E.2    Adler, A.S.3
  • 51
    • 84865145752 scopus 로고    scopus 로고
    • The effect of resveratrol on FoxO1 expression in kidneys of diabetic nephropathy rats
    • doi:10.1007/s11033-012-1780-z
    • Wu L, Zhang Y, Ma X et al (2012) The effect of resveratrol on FoxO1 expression in kidneys of diabetic nephropathy rats. Mol Biol Rep 39:9085-9093. doi:10.1007/s11033-012-1780-z
    • (2012) Mol Biol Rep , vol.39 , pp. 9085-9093
    • Wu, L.1    Zhang, Y.2    Ma, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.