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Volumn 289, Issue 11, 2014, Pages 7293-7306

A redox-resistant Sirtuin-1 mutant protects against hepatic metabolic and oxidant stress

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOELECTRIC POTENTIALS; CELL DEATH; ENZYMES; METABOLISM; OXIDANTS; PEPTIDES;

EID: 84896292959     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520403     Document Type: Article
Times cited : (61)

References (72)
  • 1
  • 3
    • 36249016246 scopus 로고    scopus 로고
    • A therapeutic role for sirtuins in diseases of aging?
    • DOI 10.1016/j.tibs.2007.09.008, PII S0968000407002423
    • Westphal, C. H., Dipp, M. A., and Guarente, L. (2007) A therapeutic role for sirtuins in diseases of aging? Trends Biochem. Sci. 32, 555-560 (Pubitemid 350123051)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.12 , pp. 555-560
    • Westphal, C.H.1    Dipp, M.A.2    Guarente, L.3
  • 4
    • 47849088748 scopus 로고    scopus 로고
    • Emerging roles of SIRT1 in vascular endothelial homeostasis
    • Potente, M., and Dimmeler, S. (2008) Emerging roles of SIRT1 in vascular endothelial homeostasis. Cell Cycle 7, 2117-2122 (Pubitemid 352036236)
    • (2008) Cell Cycle , vol.7 , Issue.14 , pp. 2117-2122
    • Potente, M.1    Dimmeler, S.2
  • 6
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., and Li, X. (2009) Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 9, 327-338
    • (2009) Cell Metab. , vol.9 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.5    Li, X.6
  • 7
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • DOI 10.1038/sj.emboj.7600244
    • Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., and Mayo, M. W. (2004) Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23, 2369-2380 (Pubitemid 38954844)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 8
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • DOI 10.1016/S0092-8674(01)00524-4
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. (2001) Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137-148 (Pubitemid 33035941)
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.-I.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 9
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α
    • DOI 10.1074/jbc.M501485200
    • Nemoto, S., Fergusson, M. M., and Finkel, T. (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α. J. Biol. Chem. 280, 16456-16460 (Pubitemid 40616776)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 11
    • 0042165989 scopus 로고    scopus 로고
    • Hepatocyte apoptosis and Fas expression are prominent features of human nonalcoholic steatohepatitis
    • DOI 10.1016/S0016-5085(03)00907-7
    • Feldstein, A. E., Canbay, A., Angulo, P., Taniai, M., Burgart, L. J., Lindor, K. D., and Gores, G. J. (2003) Hepatocyte apoptosis and fas expression are prominent features of human nonalcoholic steatohepatitis. Gastroenterology 125, 437-443 (Pubitemid 36929425)
    • (2003) Gastroenterology , vol.125 , Issue.2 , pp. 437-443
    • Feldstein, A.E.1    Canbay, A.2    Angulo, P.3    Taniai, M.4    Burgart, L.J.5    Lindor, K.D.6    Gores, G.J.7
  • 12
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • DOI 10.1038/ncb1645, PII NCB1645
    • Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X., Nicosia, S. V., Bhalla, K., and Bai, W. (2007) SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9, 1253-1262 (Pubitemid 350042357)
    • (2007) Nature Cell Biology , vol.9 , Issue.11 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6    Bhalla, K.7    Bai, W.8
  • 13
    • 79959355078 scopus 로고    scopus 로고
    • Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity
    • Gao, Z., Zhang, J., Kheterpal, I., Kennedy, N., Davis, R. J., and Ye, J. (2011) Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity. J. Biol. Chem. 286, 22227-22234
    • (2011) J. Biol. Chem. , vol.286 , pp. 22227-22234
    • Gao, Z.1    Zhang, J.2    Kheterpal, I.3    Kennedy, N.4    Davis, R.J.5    Ye, J.6
  • 15
    • 77951225449 scopus 로고    scopus 로고
    • DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1
    • Guo, X., Williams, J. G., Schug, T. T., and Li, X. (2010) DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J. Biol. Chem. 285, 13223-13232
    • (2010) J. Biol. Chem. , vol.285 , pp. 13223-13232
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 18
    • 62049084424 scopus 로고    scopus 로고
    • Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2
    • Zschoernig, B., and Mahlknecht, U. (2009) Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2. Biochem. Biophys. Res. Commun. 381, 372-377
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 372-377
    • Zschoernig, B.1    Mahlknecht, U.2
  • 19
    • 77956180402 scopus 로고    scopus 로고
    • SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress
    • Caito, S., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., and Rahman, I. (2010) SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress. FASEB J. 24, 3145-3159
    • (2010) FASEB J. , vol.24 , pp. 3145-3159
    • Caito, S.1    Rajendrasozhan, S.2    Cook, S.3    Chung, S.4    Yao, H.5    Friedman, A.E.6    Brookes, P.S.7    Rahman, I.8
  • 27
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 28
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337, 635-645 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 30
  • 31
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • DOI 10.1016/j.cell.2005.08.011, PII S0092867405008159
    • Chen, W. Y., Wang, D. H., Yen, R. C., Luo, J., Gu, W., and Baylin, S. B. (2005) Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123, 437-448 (Pubitemid 41546674)
    • (2005) Cell , vol.123 , Issue.3 , pp. 437-448
    • Wen, Y.C.1    Wang, D.H.2    RayWhay, C.Y.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 32
    • 80052762810 scopus 로고    scopus 로고
    • High-fat diet increases and the polyphenol, S17834, decreases acetylation of the sirtuin-1-dependent lysine-382 on p53 and apoptotic signaling in atherosclerotic lesion-prone aortic endothelium of normal mice
    • Xu, S., Jiang, B., Hou, X., Shi, C., Bachschmid, M. M., Zang, M., Verbeuren, T. J., and Cohen, R. A. (2011) High-fat diet increases and the polyphenol, S17834, decreases acetylation of the sirtuin-1-dependent lysine-382 on p53 and apoptotic signaling in atherosclerotic lesion-prone aortic endothelium of normal mice. J. Cardiovasc. Pharmacol. 58, 263-271
    • (2011) J. Cardiovasc. Pharmacol. , vol.58 , pp. 263-271
    • Xu, S.1    Jiang, B.2    Hou, X.3    Shi, C.4    Bachschmid, M.M.5    Zang, M.6    Verbeuren, T.J.7    Cohen, R.A.8
  • 34
    • 34548746833 scopus 로고    scopus 로고
    • Palmitic acid induces production of proinflammatory cytokine interleukin-8 from hepatocytes
    • DOI 10.1002/hep.21752
    • Joshi-Barve, S., Barve, S. S., Amancherla, K., Gobejishvili, L., Hill, D., Cave, M., Hote, P., and McClain, C. J. (2007) Palmitic acid induces production of proinflammatory cytokine interleukin-8 from hepatocytes. Hepatology 46, 823-830 (Pubitemid 47436129)
    • (2007) Hepatology , vol.46 , Issue.3 , pp. 823-830
    • Joshi-Barve, S.1    Barve, S.S.2    Amancherla, K.3    Gobejishvili, L.4    Hill, D.5    Cave, M.6    Hote, P.7    McClain, C.J.8
  • 35
    • 84863985147 scopus 로고    scopus 로고
    • Saturated fatty acid induction of endoplasmic reticulum stress and apoptosis in human liver cells via the PERK/ATF4/CHOP signaling pathway
    • Cao, J., Dai, D.-L., Yao, L., Yu, H.-H., Ning, B., Zhang, Q., Chen, J., Cheng, W.-H., Shen, W., and Yang, Z.-X. (2012) Saturated fatty acid induction of endoplasmic reticulum stress and apoptosis in human liver cells via the PERK/ATF4/CHOP signaling pathway. Mol. Cell. Biochem. 364, 115-129
    • (2012) Mol. Cell. Biochem. , vol.364 , pp. 115-129
    • Cao, J.1    Dai, D.-L.2    Yao, L.3    Yu, H.-H.4    Ning, B.5    Zhang, Q.6    Chen, J.7    Cheng, W.-H.8    Shen, W.9    Yang, Z.-X.10
  • 39
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., and Shelton, M. D. (2008) Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 10, 1941-1988
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 41
    • 34547101692 scopus 로고    scopus 로고
    • The expression of SIRT1 in nonalcoholic fatty liver disease induced by high-fat diet in rats
    • DOI 10.1111/j.1478-3231.2007.01497.x
    • Deng, X.-Q., Chen, L.-L., and Li, N.-X. (2007) The expression of SIRT1 in nonalcoholic fatty liver disease induced by high-fat diet in rats. Liver Int. 27, 708-715 (Pubitemid 47097323)
    • (2007) Liver International , vol.27 , Issue.5 , pp. 708-715
    • Deng, X.-Q.1    Chen, L.-L.2    Li, N.-X.3
  • 42
    • 40449093056 scopus 로고    scopus 로고
    • Mammalian sirtuin 1 is involved in the protective action of dietary saturated fat against alcoholic fatty liver in mice
    • You, M., Cao, Q., Liang, X., Ajmo, J. M., and Ness, G. C. (2008) Mammalian sirtuin 1 is involved in the protective action of dietary saturated fat against alcoholic fatty liver in mice. J. Nutr. 138, 497-501 (Pubitemid 351355247)
    • (2008) Journal of Nutrition , vol.138 , Issue.3 , pp. 497-501
    • You, M.1    Cao, Q.2    Liang, X.3    Ajmo, J.M.4    Ness, G.C.5
  • 43
    • 33750616470 scopus 로고    scopus 로고
    • Oxidant stress and antioxidant status among patients with nonalcoholic fatty liver disease (NAFLD)
    • DOI 10.1097/01.mcg.0000212608.59090.08, PII 0000483620061100000011
    • Madan, K., Bhardwaj, P., Thareja, S., Gupta, S. D., and Saraya, A. (2006) Oxidant stress and antioxidant status among patients with nonalcoholic fatty liver disease (NAFLD). J. Clin. Gastroenterol. 40, 930-935 (Pubitemid 44690769)
    • (2006) Journal of Clinical Gastroenterology , vol.40 , Issue.10 , pp. 930-935
    • Madan, K.1    Bhardwaj, P.2    Thareja, S.3    Gupta, S.D.4    Saraya, A.5
  • 45
    • 9144271181 scopus 로고    scopus 로고
    • AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells
    • DOI 10.1074/jbc.M408149200
    • Zang, M., Zuccollo, A., Hou, X., Nagata, D., Walsh, K., Herscovitz, H., Brecher, P., Ruderman, N. B., and Cohen, R. A. (2004) AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells. J. Biol. Chem. 279, 47898-47905 (Pubitemid 39540941)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47898-47905
    • Zang, M.1    Zuccollo, A.2    Hou, X.3    Nagata, D.4    Walsh, K.5    Herscovitz, H.6    Brecher, P.7    Ruderman, N.B.8    Cohen, R.A.9
  • 49
    • 54249107873 scopus 로고    scopus 로고
    • The ups and downs of SIRT1
    • Kwon, H.-S., and Ott, M. (2008) The ups and downs of SIRT1. Trends Biochem. Sci. 33, 517-525
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 517-525
    • Kwon, H.-S.1    Ott, M.2
  • 50
    • 84863622561 scopus 로고    scopus 로고
    • Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase
    • Nin, V., Escande, C., Chini, C. C., Giri, S., Camacho-Pereira, J., Matalonga, J., Lou, Z., and Chini, E. N. (2012) Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase. J. Biol. Chem. 287, 23489-23501
    • (2012) J. Biol. Chem. , vol.287 , pp. 23489-23501
    • Nin, V.1    Escande, C.2    Chini, C.C.3    Giri, S.4    Camacho-Pereira, J.5    Matalonga, J.6    Lou, Z.7    Chini, E.N.8
  • 55
    • 70350436694 scopus 로고    scopus 로고
    • MicroRNA 132 regulates nutritional stress-induced chemokine production through repression of SirT1
    • Strum, J. C., Johnson, J. H., Ward, J., Xie, H., Feild, J., Hester, A., Alford, A., and Waters, K. M. (2009) MicroRNA 132 regulates nutritional stress-induced chemokine production through repression of SirT1. Mol. Endocrinol. 23, 1876-1884
    • (2009) Mol. Endocrinol. , vol.23 , pp. 1876-1884
    • Strum, J.C.1    Johnson, J.H.2    Ward, J.3    Xie, H.4    Feild, J.5    Hester, A.6    Alford, A.7    Waters, K.M.8
  • 58
    • 84878661672 scopus 로고    scopus 로고
    • Redox factor-1 activates endothelial SIRTUIN1 through reduction of conserved cysteine sulfhydryls in its deacetylase domain
    • Jung, S.-B., Kim, C.-S., Kim, Y.-R., Naqvi, A., Yamamori, T., Kumar, S., Kumar, A., and Irani, K. (2013) Redox factor-1 activates endothelial SIRTUIN1 through reduction of conserved cysteine sulfhydryls in its deacetylase domain. PLoS One 8, e65415
    • (2013) PLoS One , vol.8
    • Jung, S.-B.1    Kim, C.-S.2    Kim, Y.-R.3    Naqvi, A.4    Yamamori, T.5    Kumar, S.6    Kumar, A.7    Irani, K.8
  • 60
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C., and Sinclair, D. A. (2010) Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 72
    • 77956295588 scopus 로고    scopus 로고
    • p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase
    • Li, S., Banck, M., Mujtaba, S., Zhou, M.-M., Sugrue, M. M., and Walsh, M. J. (2010) p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase. PLoS One 5, e10486
    • (2010) PLoS One , vol.5
    • Li, S.1    Banck, M.2    Mujtaba, S.3    Zhou, M.-M.4    Sugrue, M.M.5    Walsh, M.J.6


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