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Volumn 21, Issue , 2015, Pages 87-97

Sirtuin 1: A target for kidney diseases

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN III; ANGIOTENSIN III TYPE 1 RECEPTOR; BECLIN 1; CISPLATIN; CLAUDIN 1; ENDOTHELIAL NITRIC OXIDE SYNTHASE; HIGH MOBILITY GROUP B1 PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIVER X RECEPTOR; MICRORNA; NICOTINAMIDE ADENINE DINUCLEOTIDE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEIN BCL 2; PROTEIN P53; REACTIVE OXYGEN METABOLITE; RECEPTOR; RESVERATROL; SIRTUIN 1; SMAD3 PROTEIN; SMAD4 PROTEIN; SMAD7 PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR FOXO; TRANSCRIPTION FACTOR FOXO4; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 84930203513     PISSN: 10761551     EISSN: 15283658     Source Type: Journal    
DOI: 10.2119/molmed.2014.00211     Document Type: Article
Times cited : (68)

References (154)
  • 1
    • 84904999040 scopus 로고    scopus 로고
    • Histone-acetylation: A link between Alzheimer’s disease and post-traumatic stress disorder?
    • Bahari-Javan S, Sananbenesi F, Fischer A. (2014) Histone-acetylation: a link between Alzheimer’s disease and post-traumatic stress disorder? Front. Neurosci. 8:160
    • (2014) Front. Neurosci , vol.8
    • Bahari-Javan, S.1    Sananbenesi, F.2    Fischer, A.3
  • 2
    • 84908217408 scopus 로고    scopus 로고
    • The role of dietary histone deacetylases (HDACs) inhibitors in health and disease
    • Bassett SA, Barnett MP. (2014) The role of dietary histone deacetylases (HDACs) inhibitors in health and disease. Nutrients. 6:4273–301
    • (2014) Nutrients , vol.6 , pp. 4273-4301
    • Bassett, S.A.1    Barnett, M.P.2
  • 3
    • 84874643841 scopus 로고    scopus 로고
    • Involvement of p300/CBP and epigenetic histone acetylation in TGF-beta1- mediated gene transcription in mesangial cells
    • Yuan H, et al. (2013) Involvement of p300/CBP and epigenetic histone acetylation in TGF-beta1- mediated gene transcription in mesangial cells. Am. J. Physiol. Renal. Physiol. 304:F601–13
    • (2013) Am. J. Physiol. Renal. Physiol , vol.304 , pp. F601-F613
    • Yuan, H.1
  • 4
    • 84907998067 scopus 로고    scopus 로고
    • Novel role of silent information regulator 1 in acute endothelial cell oxidative stress injury
    • Li Y, et al. (2014) Novel role of silent information regulator 1 in acute endothelial cell oxidative stress injury. Biochim. Biophys. Acta. 1842:2246–56
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 2246-2256
    • Li, Y.1
  • 5
    • 84900428277 scopus 로고    scopus 로고
    • High glucose induces Smad activation via the transcriptional coregulator p300 and contributes to cardiac fibrosis and hypertrophy
    • Bugyei-Twum A, et al. (2014) High glucose induces Smad activation via the transcriptional coregulator p300 and contributes to cardiac fibrosis and hypertrophy. Cardiovasc. Diabetol. 13:89
    • (2014) Cardiovasc. Diabetol , vol.13
    • Bugyei-Twum, A.1
  • 6
    • 84907428509 scopus 로고    scopus 로고
    • Oleanolic acid regulates NF-κB signaling by suppressing MafK expression in RAW 264.7 cells
    • Hwang YJ, Song J, Kim HR, Hwang KA. (2014) Oleanolic acid regulates NF-κB signaling by suppressing MafK expression in RAW 264.7 cells. BMB Rep. 47:524–9
    • (2014) BMB Rep , vol.47 , pp. 524-529
    • Hwang, Y.J.1    Song, J.2    Kim, H.R.3    Hwang, K.A.4
  • 7
    • 34547431097 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A novel class of therapeutic agents in diabetic nephropathy
    • Lee HB, Noh H, Seo JY, Yu MR, Ha H. (2007) Histone deacetylase inhibitors: a novel class of therapeutic agents in diabetic nephropathy. Kidney Int. S61–6
    • (2007) Kidney Int
    • Lee, H.B.1    Noh, H.2    Seo, J.Y.3    Yu, M.R.4    Ha, H.5
  • 8
    • 84555195156 scopus 로고    scopus 로고
    • Nutrient sensing, autophagy, and diabetic nephropathy
    • Kume S, Thomas MC, Koya D. (2012) Nutrient sensing, autophagy, and diabetic nephropathy. Diabetes. 61:23–9
    • (2012) Diabetes , vol.61 , pp. 23-29
    • Kume, S.1    Thomas, M.C.2    Koya, D.3
  • 9
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell. 16:4623–35
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 10
    • 84870942679 scopus 로고    scopus 로고
    • Negative regulation of inflammation by SIRT1. Pharmacol
    • Xie J, Zhang X, Zhang L. (2013) Negative regulation of inflammation by SIRT1. Pharmacol. Res. 67:60–7
    • (2013) Res , vol.67 , pp. 60-67
    • Xie, J.1    Zhang, X.2    Zhang, L.3
  • 11
    • 24344466882 scopus 로고    scopus 로고
    • DNA methylation and histone modifications: Teaming up to silence genes
    • Fuks F. (2005) DNA methylation and histone modifications: teaming up to silence genes. Curr. Opin. Genet. Dev. 15:490–5
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 490-495
    • Fuks, F.1
  • 12
    • 84887415137 scopus 로고    scopus 로고
    • Renal tubular SIRT1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes
    • Hasegawa K, et al. (2013) Renal tubular SIRT1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. Nat. Med. 19:1496–504
    • (2013) Nat. Med , vol.19 , pp. 1496-1504
    • Hasegawa, K.1
  • 13
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, et al. (2000) Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 406:593–9
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 14
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C, Zhang Y. (2005) The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell. Biol. 6:838–49
    • (2005) Nat. Rev. Mol. Cell. Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 15
    • 0035913903 scopus 로고    scopus 로고
    • HSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, et al. (2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell. 107:149–59
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 16
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaBdependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, et al. (2004) Modulation of NF-kappaBdependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23:2369–80
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1
  • 17
    • 38649092744 scopus 로고    scopus 로고
    • Regulation of protein turnover by acetyltransferases and deacetylases
    • Sadoul K, Boyault C, Pabion M, Khochbin S. (2008) Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie. 90:306–12
    • (2008) Biochimie , vol.90 , pp. 306-312
    • Sadoul, K.1    Boyault, C.2    Pabion, M.3    Khochbin, S.4
  • 19
    • 79953152333 scopus 로고    scopus 로고
    • FoxO1 mediates an autofeedback loop regulating SIRT1 expression
    • Xiong S, Salazar G, Patrushev N, Alexander RW. (2011) FoxO1 mediates an autofeedback loop regulating SIRT1 expression. J. Biol. Chem. 286:5289–99
    • (2011) J. Biol. Chem , vol.286 , pp. 5289-5299
    • Xiong, S.1    Salazar, G.2    Patrushev, N.3    Alexander, R.W.4
  • 20
    • 84897811327 scopus 로고    scopus 로고
    • Resveratrol prevention of diabetic nephropathy is associated with the suppression of renal inflammation and mesangial cell proliferation: Possible roles of Akt/NF-kappaB pathway
    • Xu F, et al. (2014) Resveratrol prevention of diabetic nephropathy is associated with the suppression of renal inflammation and mesangial cell proliferation: possible roles of Akt/NF-kappaB pathway. Int. J. Endocrinol. 2014:289327
    • (2014) Int. J. Endocrinol
    • Xu, F.1
  • 21
    • 84891621483 scopus 로고    scopus 로고
    • Resveratrol attenuates diabetic nephropathy via modulating angiogenesis
    • Wen D, et al. (2013) Resveratrol attenuates diabetic nephropathy via modulating angiogenesis. PLoS One.8:e82336
    • (2013) Plos One , vol.8
    • Wen, D.1
  • 22
    • 84919667875 scopus 로고    scopus 로고
    • Amelioration of streptozotocininduced diabetic nephropathy by melatonin, quercetin, and resveratrol in rats
    • Elbe H, et al. (2015) Amelioration of streptozotocininduced diabetic nephropathy by melatonin, quercetin, and resveratrol in rats. Hum. Exp. Toxicol. 34:100–13
    • (2015) Hum. Exp. Toxicol , vol.34 , pp. 100-113
    • Elbe, H.1
  • 23
    • 84884519280 scopus 로고    scopus 로고
    • SIRT1 resists advanced glycation end products-induced expressions of fibronectin and TGF-beta1 by activating the Nrf2/ARE pathway in glomerular mesangial cells
    • Huang K, et al. (2013) SIRT1 resists advanced glycation end products-induced expressions of fibronectin and TGF-beta1 by activating the Nrf2/ARE pathway in glomerular mesangial cells. Free Radic. Biol. Med. 65:528–40
    • (2013) Free Radic. Biol. Med , vol.65 , pp. 528-540
    • Huang, K.1
  • 24
    • 84902523833 scopus 로고    scopus 로고
    • SIRT1 deletion leads to enhanced inflammation and aggravates endotoxininduced acute kidney injury
    • Gao R, et al. (2014) SIRT1 deletion leads to enhanced inflammation and aggravates endotoxininduced acute kidney injury. PLoS One. 9:e98909
    • (2014) Plos One , vol.9
    • Gao, R.1
  • 25
    • 33644783770 scopus 로고    scopus 로고
    • Glucose-induced reactive oxygen species cause apoptosis of podocytes and podocyte depletion at the onset of diabetic nephropathy
    • Susztak K, Raff AC, Schiffer M, Bottinger EP. (2006) Glucose-induced reactive oxygen species cause apoptosis of podocytes and podocyte depletion at the onset of diabetic nephropathy. Diabetes. 55:225–33
    • (2006) Diabetes , vol.55 , pp. 225-233
    • Susztak, K.1    Raff, A.C.2    Schiffer, M.3    Bottinger, E.P.4
  • 26
    • 15744400877 scopus 로고    scopus 로고
    • Multiple metabolic hits converge on CD36 as novel mediator of tubular epithelial apoptosis in diabetic nephropathy
    • Susztak K, Ciccone E, McCue P, Sharma K, Bottinger EP. (2005) Multiple metabolic hits converge on CD36 as novel mediator of tubular epithelial apoptosis in diabetic nephropathy. PLoS Med. 2:e45
    • (2005) Plos Med , vol.2
    • Susztak, K.1    Ciccone, E.2    McCue, P.3    Sharma, K.4    Bottinger, E.P.5
  • 27
    • 84867394203 scopus 로고    scopus 로고
    • Can we target tubular damage to prevent renal function decline in diabetes?
    • Bonventre JV. (2012) Can we target tubular damage to prevent renal function decline in diabetes? Semin. Nephrol. 32:452–62
    • (2012) Semin. Nephrol , vol.32 , pp. 452-462
    • Bonventre, J.V.1
  • 28
    • 77649099572 scopus 로고    scopus 로고
    • De novo expression of podocyte proteins in parietal epithelial cells during experimental glomerular disease
    • Ohse T, et al. (2010) De novo expression of podocyte proteins in parietal epithelial cells during experimental glomerular disease. Am. J. Physiol. Renal Physiol. 298:F702–11
    • (2010) Am. J. Physiol. Renal Physiol , vol.298 , pp. F702-F711
    • Ohse, T.1
  • 29
    • 84863229342 scopus 로고    scopus 로고
    • De novo expression of podocyte proteins in parietal epithelial cells in experimental aging nephropathy
    • Zhang J, et al. (2012) De novo expression of podocyte proteins in parietal epithelial cells in experimental aging nephropathy. Am. J. Physiol. Renal Physiol. 302:F571–80
    • (2012) Am. J. Physiol. Renal Physiol , vol.302
    • Zhang, J.1
  • 30
    • 84901045119 scopus 로고    scopus 로고
    • Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis
    • Koda R, et al. (2014) Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis. Int. J. Nephrol. 2014:598670
    • (2014) Int. J. Nephrol
    • Koda, R.1
  • 31
    • 84924026400 scopus 로고    scopus 로고
    • Tamoxifen ameliorates renal tubulointerstitial fibrosis by modulation of estrogen receptor alpha-mediated transforming growth factor-beta1/Smad signaling pathway
    • Kim D, et al. (2014) Tamoxifen ameliorates renal tubulointerstitial fibrosis by modulation of estrogen receptor alpha-mediated transforming growth factor-beta1/Smad signaling pathway. Nephrol. Dial. Transplant. 29:2043–53
    • (2014) Nephrol. Dial. Transplant , vol.29 , pp. 2043-2053
    • Kim, D.1
  • 32
    • 84884805852 scopus 로고    scopus 로고
    • Knockdown of thioredoxininteracting protein ameliorates high glucoseinduced epithelial to mesenchymal transition in renal tubular epithelial cells
    • Wei J, et al. (2013) Knockdown of thioredoxininteracting protein ameliorates high glucoseinduced epithelial to mesenchymal transition in renal tubular epithelial cells. Cell Signal. 25:2788–96
    • (2013) Cell Signal , vol.25 , pp. 2788-2796
    • Wei, J.1
  • 33
    • 84892616097 scopus 로고    scopus 로고
    • Upregulation of mitochondrial Nox4 mediates TGF-beta-induced apoptosis in cultured mouse podocytes
    • Das R, et al. (2014) Upregulation of mitochondrial Nox4 mediates TGF-beta-induced apoptosis in cultured mouse podocytes. Am. J. Physiol. Renal Physiol. 306:F155–67
    • (2014) Am. J. Physiol. Renal Physiol , vol.306 , pp. F155-F167
    • Das, R.1
  • 34
    • 84882727355 scopus 로고    scopus 로고
    • Induction of renal fibrotic genes by TGF-beta1 requires EGFR activation, p53 and reactive oxygen species
    • Samarakoon R, et al. (2013) Induction of renal fibrotic genes by TGF-beta1 requires EGFR activation, p53 and reactive oxygen species. Cell Signal. 25:2198–209
    • (2013) Cell Signal , vol.25 , pp. 2198-2209
    • Samarakoon, R.1
  • 35
    • 48249109924 scopus 로고    scopus 로고
    • The role of the TGF/Smad signaling pathway in peritoneal fibrosis induced by peritoneal dialysis solutions
    • Yao Q, et al. (2008) The role of the TGF/Smad signaling pathway in peritoneal fibrosis induced by peritoneal dialysis solutions. Nephron Exp. Nephrol. 109:e71–8
    • (2008) Nephron Exp. Nephrol , vol.109
    • Yao, Q.1
  • 36
    • 84906687076 scopus 로고    scopus 로고
    • Effect of Smad pathway activation on podocyte cell cycle regulation: An immunohistochemical evaluation
    • Koutroutsos K, et al. (2014) Effect of Smad pathway activation on podocyte cell cycle regulation: an immunohistochemical evaluation. Ren. Fail. 36:1310–6
    • (2014) Ren. Fail , vol.36 , pp. 1310-1316
    • Koutroutsos, K.1
  • 37
    • 84896711717 scopus 로고    scopus 로고
    • Resveratrol as a therapeutic agent for renal fibrosis induced by unilateral ureteral obstruction
    • Liang J, Tian S, Han J, Xiong P. (2014) Resveratrol as a therapeutic agent for renal fibrosis induced by unilateral ureteral obstruction. Ren. Fail. 36:285–91
    • (2014) Ren. Fail , vol.36 , pp. 285-291
    • Liang, J.1    Tian, S.2    Han, J.3    Xiong, P.4
  • 38
    • 77956531086 scopus 로고    scopus 로고
    • Resveratrol inhibits renal fibrosis in the obstructed kidney: Potential role in deacetylation of Smad3
    • Li J, Qu X, Ricardo SD, Bertram JF, Nikolic-Paterson DJ. (2010) Resveratrol inhibits renal fibrosis in the obstructed kidney: potential role in deacetylation of Smad3. Am. J. Pathol. 177:1065–71
    • (2010) Am. J. Pathol , vol.177 , pp. 1065-1071
    • Li, J.1    Qu, X.2    Ricardo, S.D.3    Bertram, J.F.4    Nikolic-Paterson, D.J.5
  • 39
    • 84895535457 scopus 로고    scopus 로고
    • SIRT1 activation ameliorates renal fibrosis by inhibiting the TGF-beta/Smad3 pathway
    • Huang XZ, et al. (2014) SIRT1 activation ameliorates renal fibrosis by inhibiting the TGF-beta/Smad3 pathway. J. Cell. Biochem. 115:996–1005
    • (2014) J. Cell. Biochem , vol.115 , pp. 996-1005
    • Huang, X.Z.1
  • 40
    • 84876952651 scopus 로고    scopus 로고
    • SIRT1 suppresses the epithelial- to-mesenchymal transition in cancer metastasis and organ fibrosis
    • Simic P, et al. (2013) SIRT1 suppresses the epithelial- to-mesenchymal transition in cancer metastasis and organ fibrosis. Cell Rep. 3:1175–86
    • (2013) Cell Rep , vol.3 , pp. 1175-1186
    • Simic, P.1
  • 41
    • 84863011417 scopus 로고    scopus 로고
    • Apoptosis occurs differentially according to glomerular size in diabetic kidney disease
    • Jung DS, et al. (2012) Apoptosis occurs differentially according to glomerular size in diabetic kidney disease. Nephrology Dialysis Transplantation. 27:259–66
    • (2012) Nephrology Dialysis Transplantation , vol.27 , pp. 259-266
    • Jung, D.S.1
  • 42
    • 84903866014 scopus 로고    scopus 로고
    • Down-regulation of PERKATF4- CHOP pathway by astragaloside IV is associated with the inhibition of endoplasmic reticulum stress-induced podocyte apoptosis in diabetic rats
    • Chen Y, et al. (2014) Down-regulation of PERKATF4- CHOP pathway by astragaloside IV is associated with the inhibition of endoplasmic reticulum stress-induced podocyte apoptosis in diabetic rats. Cell Physiol. Biochem. 3:1975–87
    • (2014) Cell Physiol. Biochem , vol.3 , pp. 1975-1987
    • Chen, Y.1
  • 43
    • 84920270340 scopus 로고    scopus 로고
    • Hyperglycemia, p53, and mitochondrial pathway of apoptosis are involved in the susceptibility of diabetic models to ischemic acute kidney injury
    • Peng J, et al. (2015) Hyperglycemia, p53, and mitochondrial pathway of apoptosis are involved in the susceptibility of diabetic models to ischemic acute kidney injury. Kidney Int. 87:137–50
    • (2015) Kidney Int , vol.87 , pp. 137-150
    • Peng, J.1
  • 44
    • 84930200910 scopus 로고    scopus 로고
    • TRB3 mediates renal tubular cell apoptosis associated with proteinuria
    • Wang W, et al. (2015) TRB3 mediates renal tubular cell apoptosis associated with proteinuria. Clin. Exp. Med. 15:167–77
    • (2015) Clin. Exp. Med , vol.15 , pp. 167-177
    • Wang, W.1
  • 45
    • 84901659445 scopus 로고    scopus 로고
    • Ubiquitination-dependent CARM1 degradation facilitates Notch1-mediated podocyte apoptosis in diabetic nephropathy
    • Kim D, et al. (2014) Ubiquitination-dependent CARM1 degradation facilitates Notch1-mediated podocyte apoptosis in diabetic nephropathy. Cell Signal. 26:1774–82
    • (2014) Cell Signal , vol.26 , pp. 1774-1782
    • Kim, D.1
  • 46
    • 84877255276 scopus 로고    scopus 로고
    • Glomerular cell death and inflammation with high-protein diet and diabetes. Nephrol. Dial
    • Meek RL, et al. (2013) Glomerular cell death and inflammation with high-protein diet and diabetes. Nephrol. Dial. Transplant. 28:1711–20
    • (2013) Transplant , vol.28 , pp. 1711-1720
    • Meek, R.L.1
  • 47
    • 79961143570 scopus 로고    scopus 로고
    • SIRT1 activation by resveratrol ameliorates cisplatin-induced renal injury through deacetylation of p53
    • Kim DH, et al. (2011) SIRT1 activation by resveratrol ameliorates cisplatin-induced renal injury through deacetylation of p53. Am. J. Physiol. Renal Physiol. 301:F427–35
    • (2011) Am. J. Physiol. Renal Physiol , vol.301 , pp. F427-F435
    • Kim, D.H.1
  • 48
    • 48849086013 scopus 로고    scopus 로고
    • Change in histone H3 phosphorylation, MAP kinase p38, SIR 2 and p53 expression by resveratrol in preventing streptozotocin induced type I diabetic nephropathy
    • Tikoo K, Singh K, Kabra D, Sharma V, Gaikwad A. (2008) Change in histone H3 phosphorylation, MAP kinase p38, SIR 2 and p53 expression by resveratrol in preventing streptozotocin induced type I diabetic nephropathy. Free Radic. Res. 42:397–404
    • (2008) Free Radic. Res , vol.42 , pp. 397-404
    • Tikoo, K.1    Singh, K.2    Kabra, D.3    Sharma, V.4    Gaikwad, A.5
  • 49
    • 33846976509 scopus 로고    scopus 로고
    • SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation
    • Kume S, et al. (2007) SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation. J. Biol. Chem. 282:151–8
    • (2007) J. Biol. Chem , vol.282 , pp. 151-158
    • Kume, S.1
  • 50
    • 46349096040 scopus 로고    scopus 로고
    • SIRT1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression. Biochem. Biophys. Res
    • Hasegawa K, et al. (2008) SIRT1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression. Biochem. Biophys. Res. Commun. 372:51–6
    • (2008) Commun , vol.372 , pp. 51-56
    • Hasegawa, K.1
  • 51
    • 80051750952 scopus 로고    scopus 로고
    • Alteration of forkhead box O (Foxo4) acetylation mediates apoptosis of podocytes in diabetes mellitus
    • Chuang PY, et al. 2011 Alteration of forkhead box O (foxo4) acetylation mediates apoptosis of podocytes in diabetes mellitus. PLoS One. 6:e23566
    • (2011) Plos One , vol.6
    • Chuang, P.Y.1
  • 52
    • 84875190140 scopus 로고    scopus 로고
    • Notch pathway is involved in high glucose-induced apoptosis in podocytes via Bcl-2 and p53 pathways
    • Gao F, et al. (2013) Notch pathway is involved in high glucose-induced apoptosis in podocytes via Bcl-2 and p53 pathways. J. Cell. Biochem. 114:1029–38
    • (2013) J. Cell. Biochem , vol.114 , pp. 1029-1038
    • Gao, F.1
  • 53
    • 35848931880 scopus 로고    scopus 로고
    • Increased glomerular cell (Podocyte) apoptosis in rats with streptozotocininduced diabetes mellitus: Role in the development of diabetic glomerular disease
    • Menini S, et al. (2007) Increased glomerular cell (podocyte) apoptosis in rats with streptozotocininduced diabetes mellitus: role in the development of diabetic glomerular disease. Diabetologia. 50:2591–9
    • (2007) Diabetologia , vol.50 , pp. 2591-2599
    • Menini, S.1
  • 54
    • 84884793994 scopus 로고    scopus 로고
    • Transforming growth factor-beta-induced cross talk between p53 and a microRNA in the pathogenesis of diabetic nephropathy
    • Deshpande SD, et al. (2013) Transforming growth factor-beta-induced cross talk between p53 and a microRNA in the pathogenesis of diabetic nephropathy. Diabetes 62:3151–62
    • (2013) Diabetes , vol.62 , pp. 3151-3162
    • Deshpande, S.D.1
  • 55
    • 33846105394 scopus 로고    scopus 로고
    • Apoptosis by cyclosporine in mesangial cells. Transplant
    • Han SY, et al. (2006) Apoptosis by cyclosporine in mesangial cells. Transplant. Proc. 38:2244–6
    • (2006) Proc , vol.38 , pp. 2244-2246
    • Han, S.Y.1
  • 56
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, et al. (2001) Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell. 107:137–48
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 57
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, et al. (2002) Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21:2383–96
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 58
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • Brooks CL, Gu W. (2009) How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer. 9:123–8
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 59
    • 41849093037 scopus 로고    scopus 로고
    • The role of FoxO in the regulation of metabolism
    • Gross DN, van den Heuvel AP, Birnbaum MJ. (2008) The role of FoxO in the regulation of metabolism. Oncogene. 27:2320–36
    • (2008) Oncogene , vol.27 , pp. 2320-2336
    • Gross, D.N.1    Van Den Heuvel, A.P.2    Birnbaum, M.J.3
  • 60
    • 84900034723 scopus 로고    scopus 로고
    • FOXO transcription factors: Their clinical significance and regulation
    • Wang Y, Zhou Y, Graves DT. (2014) FOXO transcription factors: their clinical significance and regulation. Biomed. Res. Int. 2014:925350
    • (2014) Biomed. Res. Int
    • Wang, Y.1    Zhou, Y.2    Graves, D.T.3
  • 61
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, et al. (2004) Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science. 303:2011–5
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1
  • 62
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead- dependent pathway
    • Nemoto S, Fergusson MM, Finkel T. (2004) Nutrient availability regulates SIRT1 through a forkhead- dependent pathway. Science. 306:2105–8
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 63
    • 84868210978 scopus 로고    scopus 로고
    • Nrf2-keap1 system versus NFkappaB: The good and the evil in chronic kidney disease?
    • Pedruzzi LM, Stockler-Pinto MB, Leite M Jr, Mafra D. (2012) Nrf2-keap1 system versus NFkappaB: the good and the evil in chronic kidney disease? Biochimie. 94:2461–6
    • (2012) Biochimie , vol.94 , pp. 2461-2466
    • Pedruzzi, L.M.1    Stockler-Pinto, M.B.2    Leite, M.3    Mafra, D.4
  • 64
    • 84892534814 scopus 로고    scopus 로고
    • Transcription factor NFkappaB regulates the expression of the histone deacetylase SIRT1
    • Katto J, Engel N, Abbas W, Herbein G, Mahlknecht U. (2013) Transcription factor NFkappaB regulates the expression of the histone deacetylase SIRT1. Clin. Epigenetics. 5:11
    • (2013) Clin. Epigenetics , vol.5
    • Katto, J.1    Engel, N.2    Abbas, W.3    Herbein, G.4    Mahlknecht, U.5
  • 65
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S. (2008) Shared principles in NF-kappaB signaling. Cell. 132:344–62
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 66
    • 84904270853 scopus 로고    scopus 로고
    • Febuxostat ameliorates diabetic renal injury in a streptozotocin-induced diabetic rat model
    • Lee HJ, et al. (2014) Febuxostat ameliorates diabetic renal injury in a streptozotocin-induced diabetic rat model. Am. J. Nephrol. 40:56–63
    • (2014) Am. J. Nephrol , vol.40 , pp. 56-63
    • Lee, H.J.1
  • 67
    • 84922267842 scopus 로고    scopus 로고
    • Markers of endothelial dysfunction and inflammation predict progression of diabetic nephropathy in African Americans with type 1 diabetes
    • Roy MS, Janal MN, Crosby J, Donnelly R. (2015) Markers of endothelial dysfunction and inflammation predict progression of diabetic nephropathy in African Americans with type 1 diabetes. Kidney Int. 87:427–33
    • (2015) Kidney Int , vol.87 , pp. 427-433
    • Roy, M.S.1    Janal, M.N.2    Crosby, J.3    Donnelly, R.4
  • 68
    • 84908316746 scopus 로고    scopus 로고
    • Global tolllike receptor 4 knockout results in decreased renal inflammation, fibrosis and podocytopathy
    • Jialal I, Major AM, Devaraj S. (2014) Global tolllike receptor 4 knockout results in decreased renal inflammation, fibrosis and podocytopathy. J. Diabetes Complications. 28:755–61
    • (2014) J. Diabetes Complications , vol.28 , pp. 755-761
    • Jialal, I.1    Major, A.M.2    Devaraj, S.3
  • 69
    • 84924922747 scopus 로고    scopus 로고
    • The role of MicroRNAs in diabetic nephropathy
    • Wu H, et al. (2014) The role of MicroRNAs in diabetic nephropathy. J. Diabetes Res. 2014:920134
    • (2014) J. Diabetes Res
    • Wu, H.1
  • 70
    • 84875643469 scopus 로고    scopus 로고
    • A novel nuclear factor kappaB inhibitor, dehydroxymethylepoxyquinomicin, ameliorates puromycin aminonucleoside-induced nephrosis in mice
    • Shimo T, et al. (2013) A novel nuclear factor kappaB inhibitor, dehydroxymethylepoxyquinomicin, ameliorates puromycin aminonucleoside-induced nephrosis in mice. Am. J. Nephrol. 37:302–9
    • (2013) Am. J. Nephrol , vol.37 , pp. 302-309
    • Shimo, T.1
  • 71
    • 84865293359 scopus 로고    scopus 로고
    • Polydatin ameliorates experimental diabetes-induced fibronectin through inhibiting the activation of NF-kappaB signaling pathway in rat glomerular mesangial cells
    • Xie X, et al. (2012) Polydatin ameliorates experimental diabetes-induced fibronectin through inhibiting the activation of NF-kappaB signaling pathway in rat glomerular mesangial cells. Mol. Cell. Endocrinol. 362:183–93
    • (2012) Mol. Cell. Endocrinol , vol.362 , pp. 183-193
    • Xie, X.1
  • 72
    • 84862528465 scopus 로고    scopus 로고
    • Tanshinone IIA prevents uric acid nephropathy in rats through NF-kappaB inhibition
    • Wu X, et al. (2012) Tanshinone IIA prevents uric acid nephropathy in rats through NF-kappaB inhibition. Planta. Med. 78:866–73
    • (2012) Planta. Med , vol.78 , pp. 866-873
    • Wu, X.1
  • 73
    • 84864609051 scopus 로고    scopus 로고
    • Sodium butyrate decreases the activation of NF-kappaB reducing inflammation inflammation and oxidative damage in the kidney of rats subjected to contrast-induced nephropathy
    • Machado RA, et al. (2012) Sodium butyrate decreases the activation of NF-kappaB reducing inflammation inflammation and oxidative damage in the kidney of rats subjected to contrast-induced nephropathy. Nephrol. Dial. Transplant. 27:3136–40
    • (2012) Nephrol. Dial. Transplant , vol.27 , pp. 3136-3140
    • Machado, R.A.1
  • 74
    • 67449113506 scopus 로고    scopus 로고
    • Suppression of NF-kappaB by cyclosporin a and tacrolimus (FK506) via induction of the C/EBP family: Implication for unfolded protein response
    • Du S, et al. (2009) Suppression of NF-kappaB by cyclosporin a and tacrolimus (FK506) via induction of the C/EBP family: implication for unfolded protein response. J. Immunol. 182:7201–11
    • (2009) J. Immunol , vol.182 , pp. 7201-7211
    • Du, S.1
  • 75
    • 53149100858 scopus 로고    scopus 로고
    • SIRT1 longevity factor suppresses NF-kappaB -driven immune responses: Regulation of aging via NF-kappaB acetylation?
    • Salminen A, Kauppinen A, Suuronen T, Kaarniranta K. (2008) SIRT1 longevity factor suppresses NF-kappaB -driven immune responses: regulation of aging via NF-kappaB acetylation? Bioessays. 30:939–42
    • (2008) Bioessays , vol.30 , pp. 939-942
    • Salminen, A.1    Kauppinen, A.2    Suuronen, T.3    Kaarniranta, K.4
  • 76
    • 84862778684 scopus 로고    scopus 로고
    • SIRT1 overexpression decreases cisplatin-induced acetylation of NF-kappaB p65 subunit and cytotoxicity in renal proximal tubule cells
    • Jung YJ, et al. (2012) SIRT1 overexpression decreases cisplatin-induced acetylation of NF-kappaB p65 subunit and cytotoxicity in renal proximal tubule cells. Biochem. Biophys. Res. Commun. 419:206–10
    • (2012) Biochem. Biophys. Res. Commun , vol.419 , pp. 206-210
    • Jung, Y.J.1
  • 77
    • 81555225308 scopus 로고    scopus 로고
    • Dietary restriction ameliorates diabetic nephropathy through anti-inflammatory effects and regulation of the autophagy via restoration of SIRT1 in diabetic Wistar fatty (Fa/fa) rats: A model of type 2 diabetes
    • Kitada M, Takeda A, Nagai T, Ito H, Kanasaki K, Koya D. (2011) Dietary restriction ameliorates diabetic nephropathy through anti-inflammatory effects and regulation of the autophagy via restoration of SIRT1 in diabetic Wistar fatty (fa/fa) rats: a model of type 2 diabetes. Exp. Diabetes Res. 2011:908185
    • (2011) Exp. Diabetes Res
    • Kitada, M.1    Takeda, A.2    Nagai, T.3    Ito, H.4    Kanasaki, K.5    Koya, D.6
  • 78
    • 79961125549 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-mediated cleavage and inactivation of SIRT1 in human osteoarthritic chondrocytes
    • Dvir-Ginzberg M, et al. (2011) Tumor necrosis factor alpha-mediated cleavage and inactivation of SIRT1 in human osteoarthritic chondrocytes. Arthritis Rheum. 63:2363–73
    • (2011) Arthritis Rheum , vol.63 , pp. 2363-2373
    • Dvir-Ginzberg, M.1
  • 79
    • 84864678390 scopus 로고    scopus 로고
    • High-fat diet triggers inflammation-induced cleavage of SIRT1 in adipose tissue to promote metabolic dysfunction
    • Chalkiadaki A, Guarente L. (2012) High-fat diet triggers inflammation-induced cleavage of SIRT1 in adipose tissue to promote metabolic dysfunction. Cell Metab. 16:180–8
    • (2012) Cell Metab , vol.16 , pp. 180-188
    • Chalkiadaki, A.1    Guarente, L.2
  • 80
    • 0034753236 scopus 로고    scopus 로고
    • Dual roles for HMGB1: DNA binding and cytokine
    • Czura CJ, Wang H, Tracey KJ. (2001) Dual roles for HMGB1: DNA binding and cytokine. J. Endotoxin Res. 7:315–21
    • (2001) J. Endotoxin Res , vol.7 , pp. 315-321
    • Czura, C.J.1    Wang, H.2    Tracey, K.J.3
  • 82
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • Scaffidi P, Misteli T, Bianchi ME. (2002) Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature. 418:191–5
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 83
    • 84912097756 scopus 로고    scopus 로고
    • Resveratrol attenuates HMGB1 signaling and inflammation in house dust mite-induced atopic dermatitis in mice
    • Karuppagounder V, et al. (2014) Resveratrol attenuates HMGB1 signaling and inflammation in house dust mite-induced atopic dermatitis in mice. Int. Immunopharmacol. 23:617–23
    • (2014) Int. Immunopharmacol , vol.23 , pp. 617-623
    • Karuppagounder, V.1
  • 84
    • 84920288890 scopus 로고    scopus 로고
    • High-mobility group box 1 is a novel deacetylation target of Sirtuin1
    • Rabadi MM, et al. (2015) High-mobility group box 1 is a novel deacetylation target of Sirtuin1. Kidney Int. 87:95–108
    • (2015) Kidney Int , vol.87 , pp. 95-108
    • Rabadi, M.M.1
  • 85
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima N, Komatsu M. (2011) Autophagy: renovation of cells and tissues. Cell. 147:728–41
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 86
    • 77951157657 scopus 로고    scopus 로고
    • Calorie restriction enhances cell adaptation to hypoxia through SIRT1-dependent mitochondrial autophagy in mouse aged kidney
    • Kume S, et al. (2010) Calorie restriction enhances cell adaptation to hypoxia through SIRT1-dependent mitochondrial autophagy in mouse aged kidney. J. Clin. Invest. 120:1043–55
    • (2010) J. Clin. Invest , vol.120 , pp. 1043-1055
    • Kume, S.1
  • 87
    • 77951169411 scopus 로고    scopus 로고
    • Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice
    • Hartleben B, et al. (2010) Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J. Clin. Invest. 120:1084–96
    • (2010) J. Clin. Invest , vol.120 , pp. 1084-1096
    • Hartleben, B.1
  • 88
    • 77749264299 scopus 로고    scopus 로고
    • Autophagy is a renoprotective mechanism during in vitro hypoxia and in vivo ischemia-reperfusion injury
    • Jiang M, Liu K, Luo J, Dong Z. (2010) Autophagy is a renoprotective mechanism during in vitro hypoxia and in vivo ischemia-reperfusion injury. Am. J. Pathol. 176:1181–92
    • (2010) Am. J. Pathol , vol.176 , pp. 1181-1192
    • Jiang, M.1    Liu, K.2    Luo, J.3    Dong, Z.4
  • 89
    • 79955626606 scopus 로고    scopus 로고
    • Autophagy protects the proximal tubule from degeneration and acute ischemic injury
    • Kimura T, et al. (2011) Autophagy protects the proximal tubule from degeneration and acute ischemic injury. J. Am. Soc. Nephrol. 22:902–13
    • (2011) J. Am. Soc. Nephrol , vol.22 , pp. 902-913
    • Kimura, T.1
  • 90
    • 49749120592 scopus 로고    scopus 로고
    • Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells
    • Periyasamy-Thandavan S, et al. (2008) Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells. Kidney Int. 74:631–40
    • (2008) Kidney Int , vol.74 , pp. 631-640
    • Periyasamy-Thandavan, S.1
  • 91
    • 77952875466 scopus 로고    scopus 로고
    • Cisplatin-induced macroautophagy occurs prior to apoptosis in proximal tubules in vivo
    • Inoue K, et al. (2010) Cisplatin-induced macroautophagy occurs prior to apoptosis in proximal tubules in vivo. Clin. Exp. Nephrol. 14:112–22
    • (2010) Clin. Exp. Nephrol , vol.14 , pp. 112-122
    • Inoue, K.1
  • 92
    • 84870622028 scopus 로고    scopus 로고
    • Autophagy protects proximal tubular cells from injury and apoptosis
    • Kaushal GP. (2012) Autophagy protects proximal tubular cells from injury and apoptosis. Kidney Int. 82:1250–3
    • (2012) Kidney Int , vol.82 , pp. 1250-1253
    • Kaushal, G.P.1
  • 93
    • 41549138483 scopus 로고    scopus 로고
    • A role for the NAD-dependent deacetylase SIRT1 in the regulation of autophagy
    • Lee IH, et al. (2008) A role for the NAD-dependent deacetylase SIRT1 in the regulation of autophagy. Proc. Natl. Acad. Sci. U. S. A. 105:3374–9
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 3374-3379
    • Lee, I.H.1
  • 94
    • 84893744708 scopus 로고    scopus 로고
    • The role of autophagy in the pathogenesis of diabetic nephropathy
    • Yamahara K, et al. (2013) The role of autophagy in the pathogenesis of diabetic nephropathy. J. Diabetes Res. 2013:193757
    • (2013) J. Diabetes Res , vol.19 , pp. 2013
    • Yamahara, K.1
  • 95
    • 84876117324 scopus 로고    scopus 로고
    • Autophagy attenuates diabetic glomerular damage through protection of hyperglycemia-induced podocyte injury
    • Fang L, et al. (2013) Autophagy attenuates diabetic glomerular damage through protection of hyperglycemia-induced podocyte injury. PLoS One. 8:e60546
    • (2013) Plos One , vol.8
    • Fang, L.1
  • 96
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot G, et al. (2009) Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol. Cell. Biol. 29:2570–81
    • (2009) Mol. Cell. Biol , vol.29 , pp. 2570-2581
    • Bellot, G.1
  • 97
    • 78650691023 scopus 로고    scopus 로고
    • Deacetylation of FoxO by SIRT1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes
    • Hariharan N, et al. (2010) Deacetylation of FoxO by SIRT1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes. Circ. Res. 107:1470–82
    • (2010) Circ. Res , vol.107 , pp. 1470-1482
    • Hariharan, N.1
  • 98
    • 84865145752 scopus 로고    scopus 로고
    • The effect of resveratrol on FoxO1 expression in kidneys of diabetic nephropathy rats
    • Wu L, Zhang Y, Ma X, Zhang N, Qin G. (2012) The effect of resveratrol on FoxO1 expression in kidneys of diabetic nephropathy rats. Mol. Biol. Rep. 39:9085–93
    • (2012) Mol. Biol. Rep , vol.39 , pp. 9085-9093
    • Wu, L.1    Zhang, Y.2    Ma, X.3    Zhang, N.4    Qin, G.5
  • 99
    • 84877093032 scopus 로고    scopus 로고
    • Role of SIRT1 and FOXO factors in eNOS transcriptional activation by resveratrol
    • Xia N, et al. (2013) Role of SIRT1 and FOXO factors in eNOS transcriptional activation by resveratrol. Nitric Oxide. 32:29–35
    • (2013) Nitric Oxide , vol.32 , pp. 29-35
    • Xia, N.1
  • 100
    • 67650091375 scopus 로고    scopus 로고
    • Resveratrol induces mitochondrial biogenesis in endothelial cells
    • Csiszar A, et al. (2009) Resveratrol induces mitochondrial biogenesis in endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 297:H13–20
    • (2009) Am. J. Physiol. Heart Circ. Physiol , vol.297
    • Csiszar, A.1
  • 101
    • 26844558334 scopus 로고    scopus 로고
    • Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS
    • Nisoli E, et al. (2005) Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS. Science. 310:314–7
    • (2005) Science , vol.310 , pp. 314-317
    • Nisoli, E.1
  • 103
    • 78650522881 scopus 로고    scopus 로고
    • Endothelial dysfunction as a potential contributor in diabetic nephropathy
    • Nakagawa T, et al. (2011) Endothelial dysfunction as a potential contributor in diabetic nephropathy. Nat. Rev. Nephrol. 7:36–44
    • (2011) Nat. Rev. Nephrol , vol.7 , pp. 36-44
    • Nakagawa, T.1
  • 104
    • 33749236623 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase deficiency produces accelerated nephropathy in diabetic mice
    • Zhao HJ, et al. (2006) Endothelial nitric oxide synthase deficiency produces accelerated nephropathy in diabetic mice. J. Am. Soc. Nephrol. 17:2664–9
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 2664-2669
    • Zhao, H.J.1
  • 105
    • 33846701668 scopus 로고    scopus 로고
    • Diabetic endothelial nitric oxide synthase knockout mice develop advanced diabetic nephropathy
    • Nakagawa T, et al. (2007) Diabetic endothelial nitric oxide synthase knockout mice develop advanced diabetic nephropathy. J. Am. Soc. Nephrol. 18:539–50
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 539-550
    • Nakagawa, T.1
  • 106
    • 35549008884 scopus 로고    scopus 로고
    • SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase
    • Mattagajasingh I, et al. (2007) SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase. Proc. Natl. Acad. Sci. U. S. A. 104:14855–60
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 14855-14860
    • Mattagajasingh, I.1
  • 107
    • 46249095235 scopus 로고    scopus 로고
    • SIRT1, a longevity gene, downregulates angiotensin II type 1 receptor expression in vascular smooth muscle cells
    • Miyazaki R, et al. (2008) SIRT1, a longevity gene, downregulates angiotensin II type 1 receptor expression in vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 28:1263–9
    • (2008) Arterioscler. Thromb. Vasc. Biol , vol.28 , pp. 1263-1269
    • Miyazaki, R.1
  • 108
    • 0033538473 scopus 로고    scopus 로고
    • Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
    • Wu Z, et al. (1999) Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell. 98:115–24
    • (1999) Cell , vol.98 , pp. 115-124
    • Wu, Z.1
  • 109
    • 33847306780 scopus 로고    scopus 로고
    • Signaling of mitochondrial biogenesis following oxidant injury
    • Rasbach KA, Schnellmann RG. (2007) Signaling of mitochondrial biogenesis following oxidant injury. J. Biol. Chem. 282:2355–62
    • (2007) J. Biol. Chem , vol.282 , pp. 2355-2362
    • Rasbach, K.A.1    Schnellmann, R.G.2
  • 110
    • 0033803048 scopus 로고    scopus 로고
    • Peroxisome proliferatoractivated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis
    • Lehman JJ, et al. (2000) Peroxisome proliferatoractivated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis. J. Clin. Invest. 106:847–56
    • (2000) J. Clin. Invest , vol.106 , pp. 847-856
    • Lehman, J.J.1
  • 111
    • 84861534662 scopus 로고    scopus 로고
    • Mitochondrial dysfunction accounts for aldosterone-induced epithelial-tomesenchymal transition of renal proximal tubular epithelial cells
    • Yuan Y, et al. (2012) Mitochondrial dysfunction accounts for aldosterone-induced epithelial-tomesenchymal transition of renal proximal tubular epithelial cells. Free Radic. Biol. Med. 53:30–43
    • (2012) Free Radic. Biol. Med , vol.53 , pp. 30-43
    • Yuan, Y.1
  • 112
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC- 1α
    • Nemoto S, Fergusson MM, Finkel T. (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC- 1α. J. Biol. Chem. 280:16456–60
    • (2005) J. Biol. Chem , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 113
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC- 1alpha and SIRT1
    • Rodgers JT, et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC- 1alpha and SIRT1. Nature. 434:113–8
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1
  • 114
    • 84866377470 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor-gamma coactivator 1alpha ameliorates mitochondrial dysfunction and protects podocytes from aldosteroneinduced injury
    • Yuan Y, et al. (2012) Activation of peroxisome proliferator-activated receptor-gamma coactivator 1alpha ameliorates mitochondrial dysfunction and protects podocytes from aldosteroneinduced injury. Kidney Int. 82:771–89
    • (2012) Kidney Int , vol.82 , pp. 771-789
    • Yuan, Y.1
  • 115
    • 77951049870 scopus 로고    scopus 로고
    • SRT1720 induces mitochondrial biogenesis and rescues mitochondrial function after oxidant injury in renal proximal tubule cells
    • Funk JA, Odejinmi S, Schnellmann RG. (2010) SRT1720 induces mitochondrial biogenesis and rescues mitochondrial function after oxidant injury in renal proximal tubule cells. J. Pharmacol. Exp. Ther. 333:593–601
    • (2010) J. Pharmacol. Exp. Ther , vol.333 , pp. 593-601
    • Funk, J.A.1    Odejinmi, S.2    Schnellmann, R.G.3
  • 116
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1alpha (HIF-1alpha) and HIF-2alpha in hypoxic gene regulation
    • Hu CJ, Wang LY, Chodosh LA, Keith B, Simon MC. (2003) Differential roles of hypoxia-inducible factor 1alpha (HIF-1alpha) and HIF-2alpha in hypoxic gene regulation. Mol. Cell. Biol. 23:9361–74
    • (2003) Mol. Cell. Biol , vol.23 , pp. 9361-9374
    • Hu, C.J.1    Wang, L.Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 117
    • 0037416792 scopus 로고    scopus 로고
    • HLF/HIF-2alpha is a key factor in retinopathy of prematurity in association with erythropoietin
    • Morita M, et al. (2003) HLF/HIF-2alpha is a key factor in retinopathy of prematurity in association with erythropoietin. EMBO J. 22:1134–46
    • (2003) EMBO J , vol.22 , pp. 1134-1146
    • Morita, M.1
  • 118
    • 9444283176 scopus 로고    scopus 로고
    • Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: Erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells
    • Warnecke C, et al. (2004) Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells. FASEB J. 18:1462–4
    • (2004) FASEB J , vol.18 , pp. 1462-1464
    • Warnecke, C.1
  • 119
    • 33746655373 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in the kidney
    • Haase VH. (2006) Hypoxia-inducible factors in the kidney. Am. J. Physiol. Renal Physiol. 291:F271–81
    • (2006) Am. J. Physiol. Renal Physiol , vol.291 , pp. F271-F281
    • Haase, V.H.1
  • 120
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxiainducible factor 1alpha
    • Lim JH, Lee YM, Chun YS, Chen J, Kim JE, Park JW. (2010) Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxiainducible factor 1alpha. Mol. Cell. 38:864–78
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6
  • 121
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxiainducible factor 2alpha signaling by the stressresponsive deacetylase sirtuin 1
    • Dioum EM, et al. (2009) Regulation of hypoxiainducible factor 2alpha signaling by the stressresponsive deacetylase sirtuin 1. Science. 324:1289–93
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1
  • 122
  • 123
    • 77954488637 scopus 로고    scopus 로고
    • Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP
    • Walker AK, et al. (2010) Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP. Genes Dev. 24:1403–17
    • (2010) Genes Dev , vol.24 , pp. 1403-1417
    • Walker, A.K.1
  • 124
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol
    • Li X, et al. (2007) SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell. 28:91–106
    • (2007) Cell , vol.28 , pp. 91-106
    • Li, X.1
  • 125
    • 70350606061 scopus 로고    scopus 로고
    • FXR acetylation is normally dynamically regulated by p300 and SIRT1 but constitutively elevated in metabolic disease states
    • Kemper JK, et al. (2009) FXR acetylation is normally dynamically regulated by p300 and SIRT1 but constitutively elevated in metabolic disease states. Cell Metab. 10:392–404
    • (2009) Cell Metab , vol.10 , pp. 392-404
    • Kemper, J.K.1
  • 126
    • 36348974168 scopus 로고    scopus 로고
    • The direct involvement of SIRT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation
    • Zhang J. (2007) The direct involvement of SIRT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J. Biol. Chem. 282:34356–64
    • (2007) J. Biol. Chem , vol.282 , pp. 34356-34364
    • Zhang, J.1
  • 127
    • 84905028707 scopus 로고    scopus 로고
    • Blocking sirtuin 1 and 2 inhibits renal interstitial fibroblast activation and attenuates renal interstitial fibrosis in obstructive nephropathy
    • Ponnusamy M, et al. (2014) Blocking sirtuin 1 and 2 inhibits renal interstitial fibroblast activation and attenuates renal interstitial fibrosis in obstructive nephropathy. J. Pharmacol. Exp. Ther. 350:243–56
    • (2014) J. Pharmacol. Exp. Ther , vol.350 , pp. 243-256
    • Ponnusamy, M.1
  • 128
    • 80053920774 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice
    • Yoshino J, Mills KF, Yoon MJ, Imai S. (2011) Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice. Cell Metab. 14:528–36
    • (2011) Cell Metab , vol.14 , pp. 528-536
    • Yoshino, J.1    Mills, K.F.2    Yoon, M.J.3    Imai, S.4
  • 129
    • 84905005034 scopus 로고    scopus 로고
    • Grape seed proanthocyanidin extracts ameliorate podocyte injury by activating peroxisome proliferator-activated receptorgamma coactivator 1alpha in low-dose streptozotocin- and high-carbohydrate/high-fat diet-induced diabetic rats
    • Bao L, et al. (2014) Grape seed proanthocyanidin extracts ameliorate podocyte injury by activating peroxisome proliferator-activated receptorgamma coactivator 1alpha in low-dose streptozotocin- and high-carbohydrate/high-fat diet-induced diabetic rats. Food Funct. 5:1872–80
    • (2014) Food Funct , vol.5 , pp. 1872-1880
    • Bao, L.1
  • 130
    • 46249100836 scopus 로고    scopus 로고
    • Tissue-specific regulation of SIRT1 by calorie restriction
    • Chen D, et al. (2008) Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 22:1753–7
    • (2008) Genes Dev , vol.22 , pp. 1753-1757
    • Chen, D.1
  • 131
    • 84906123510 scopus 로고    scopus 로고
    • Exercise training enhanced SIRT1 longevity signaling replaces the IGF1 survival pathway to attenuate aging-induced rat heart apoptosis
    • Lai CH, et al. (2014) Exercise training enhanced SIRT1 longevity signaling replaces the IGF1 survival pathway to attenuate aging-induced rat heart apoptosis. Age (Dordr). 36:9706
    • (2014) Age (Dordr) , vol.36
    • Lai, C.H.1
  • 132
    • 84906082309 scopus 로고    scopus 로고
    • Calorie restriction mimicking effects of roflumilast prevents diabetic nephropathy
    • Tikoo K, Lodea S, Karpe PA, Kumar S. (2014) Calorie restriction mimicking effects of roflumilast prevents diabetic nephropathy. Biochem. Biophys. Res. Commun. 450:1581–6
    • (2014) Biochem. Biophys. Res. Commun , vol.450 , pp. 1581-1586
    • Tikoo, K.1    Lodea, S.2    Karpe, P.A.3    Kumar, S.4
  • 133
    • 77952288176 scopus 로고    scopus 로고
    • Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice. Mol
    • Hayashida S, et al. (2010) Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice. Mol. Cell Biochem. 339:285–92
    • (2010) Cell Biochem , vol.339 , pp. 285-292
    • Hayashida, S.1
  • 134
    • 80053564714 scopus 로고    scopus 로고
    • CREB and ChREBP oppositely regulate SIRT1 expression in response to energy availability
    • Noriega LG, et al. (2011) CREB and ChREBP oppositely regulate SIRT1 expression in response to energy availability. EMBO Rep. 12:1069–76
    • (2011) EMBO Rep , vol.12 , pp. 1069-1076
    • Noriega, L.G.1
  • 135
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, et al. (2004) Mammalian SIRT1 represses forkhead transcription factors. Cell. 116:551–63
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1
  • 136
    • 33644875936 scopus 로고    scopus 로고
    • Cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1
    • Voelter-Mahlknecht S, Mahlknecht U. (2006) Cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1. Int. J. Mol. Med. 17:59–67
    • (2006) Int. J. Mol. Med , vol.17 , pp. 59-67
    • Voelter-Mahlknecht, S.1    Mahlknecht, U.2
  • 137
    • 77954218572 scopus 로고    scopus 로고
    • Involvement of the p65/RelA subunit of NF-kappaB in TNF-alphainduced SIRT1 expression in vascular smooth muscle cells
    • Zhang HN, et al. (2010) Involvement of the p65/RelA subunit of NF-kappaB in TNF-alphainduced SIRT1 expression in vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 397:569–75
    • (2010) Biochem. Biophys. Res. Commun , vol.397 , pp. 569-575
    • Zhang, H.N.1
  • 138
    • 84875831763 scopus 로고    scopus 로고
    • Regulation of TREM2 expression by an NF-small ka, CyrillicB-sensitive miRNA-34a
    • Zhao Y, et al. (2013) Regulation of TREM2 expression by an NF-small ka, CyrillicB-sensitive miRNA-34a. Neuroreport. 24:318–23
    • (2013) Neuroreport , vol.24 , pp. 318-323
    • Zhao, Y.1
  • 139
    • 84863993239 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV)-induced tumor suppressor microRNA MiR-34a is growth promoting in EBV-infected B cells
    • Forte E, et al. (2012) The Epstein-Barr virus (EBV)-induced tumor suppressor microRNA MiR-34a is growth promoting in EBV-infected B cells. J. Virol. 86:6889–98
    • (2012) J. Virol , vol.86 , pp. 6889-6898
    • Forte, E.1
  • 141
    • 84856347212 scopus 로고    scopus 로고
    • Transcriptional activation of microRNA-34a by NF-kappa B in human esophageal cancer cells
    • Li J, et al. (2012) Transcriptional activation of microRNA-34a by NF-kappa B in human esophageal cancer cells. BMC Mol. Biol. 13:4
    • (2012) BMC Mol. Biol , vol.13
    • Li, J.1
  • 142
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham A, et al. (2009) Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 9:327–38
    • (2009) Cell Metab , vol.9 , pp. 327-338
    • Purushotham, A.1
  • 143
    • 77953633702 scopus 로고    scopus 로고
    • PPARbeta/delta regulates the human SIRT1 gene transcription via Sp1
    • Okazaki M, et al. (2010) PPARbeta/delta regulates the human SIRT1 gene transcription via Sp1. Endocr. J. 57:403–13
    • (2010) Endocr. J , vol.57 , pp. 403-413
    • Okazaki, M.1
  • 144
    • 78649852533 scopus 로고    scopus 로고
    • SIRT1 is regulated by a PPARγ-SIRT1 negative feedback loop associated with senescence
    • Han L, et al. (2010) SIRT1 is regulated by a PPARγ-SIRT1 negative feedback loop associated with senescence. Nucleic Acids Res. 38:7458–71
    • (2010) Nucleic Acids Res , vol.38 , pp. 7458-7471
    • Han, L.1
  • 145
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C, et al. (2009) AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature. 458:1056–60
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1
  • 146
    • 84863622561 scopus 로고    scopus 로고
    • Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMPactivated protein kinase
    • Nin V, et al. (2012) Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMPactivated protein kinase. J. Biol. Chem. 287:23489–501
    • (2012) J. Biol. Chem , vol.287 , pp. 23489-23501
    • Nin, V.1
  • 147
    • 50649112638 scopus 로고    scopus 로고
    • SIRT1 regulates hepatocyte lipid metabolism through activating AMPactivated protein kinase
    • Hou X, et al. (2008) SIRT1 regulates hepatocyte lipid metabolism through activating AMPactivated protein kinase. J. Biol. Chem. 283:20015–26
    • (2008) J. Biol. Chem , vol.283 , pp. 20015-20026
    • Hou, X.1
  • 148
    • 55549096745 scopus 로고    scopus 로고
    • SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1: Possible role in AMP-activated protein kinase activation
    • Lan F, Cacicedo JM, Ruderman N, Ido Y. (2008) SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1: possible role in AMP-activated protein kinase activation. J. Biol. Chem. 283:27628–35
    • (2008) J. Biol. Chem , vol.283 , pp. 27628-27635
    • Lan, F.1    Cacicedo, J.M.2    Ruderman, N.3    Ido, Y.4
  • 149
    • 41649094992 scopus 로고    scopus 로고
    • SIRT1 acts as a nutrientsensitive growth suppressor and its loss is associated with increased AMPK and telomerase activity
    • Narala SR, et al. (2008) SIRT1 acts as a nutrientsensitive growth suppressor and its loss is associated with increased AMPK and telomerase activity. Mol. Biol. Cell. 19:1210–9
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1210-1219
    • Narala, S.R.1
  • 150
    • 80052908737 scopus 로고    scopus 로고
    • MicroRNA-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating SIRT1
    • Zhu H, et al. (2011) MicroRNA-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating SIRT1. Cardiovasc. Res. 92:75–84
    • (2011) Cardiovasc. Res , vol.92 , pp. 75-84
    • Zhu, H.1
  • 151
    • 79959343572 scopus 로고    scopus 로고
    • The controversial links among calorie restriction, SIRT1, and resveratrol
    • Hu Y, Liu J, Wang J, Liu Q. (2011) The controversial links among calorie restriction, SIRT1, and resveratrol. Free Radic. Biol. Med. 51:250–6
    • (2011) Free Radic. Biol. Med , vol.51 , pp. 250-256
    • Hu, Y.1    Liu, J.2    Wang, J.3    Liu, Q.4
  • 152
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL. (2001) Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276:38837–43
    • (2001) J. Biol. Chem , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 154
    • 28144438533 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors
    • Mai A, et al. (2005) Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors. J. Med. Chem. 48:7789–95.
    • (2005) J. Med. Chem , vol.48 , pp. 7789-7795
    • Mai, A.1


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