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Volumn 120, Issue 5, 2017, Pages 862-875

ATF6 Decreases Myocardial Ischemia/Reperfusion Damage and Links ER Stress and Oxidative Stress Signaling Pathways in the Heart

Author keywords

ATF6; cardiac myocyte; catalase; endoplasmic reticulum stress; ischemia; ischemia reperfusion injury; oxidative stress; protein folding; unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; CATALASE; REACTIVE OXYGEN METABOLITE; TUNICAMYCIN; ATF6 PROTEIN, MOUSE;

EID: 85007198697     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.116.310266     Document Type: Article
Times cited : (234)

References (41)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch WE, Morimoto RI, Dillin A, Kelly JW, Adapting proteostasis for disease intervention. Science 2008 319 916 919. doi: 10.1126/science.1141448
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 84870822727 scopus 로고    scopus 로고
    • Roles for the sarco-/endoplasmic reticulum in cardiac myocyte contraction, protein synthesis, and protein quality control
    • Glembotski CC, Roles for the sarco-/endoplasmic reticulum in cardiac myocyte contraction, protein synthesis, and protein quality control. Physiology (Bethesda) 2012 27 343 350. doi: 10.1152/physiol.00034.2012
    • (2012) Physiology (Bethesda) , vol.27 , pp. 343-350
    • Glembotski, C.C.1
  • 3
    • 84880633059 scopus 로고    scopus 로고
    • Orchestration of secretory protein folding by ER chaperones
    • Gidalevitz T, Stevens F, Argon Y, Orchestration of secretory protein folding by ER chaperones. Biochim Biophys Acta 2013 1833 2410 2424. doi: 10.1016/j.bbamcr.2013.03.007
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 2410-2424
    • Gidalevitz, T.1    Stevens, F.2    Argon, Y.3
  • 4
    • 84890204277 scopus 로고    scopus 로고
    • Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system
    • Amm I, Sommer T, Wolf DH, Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta 2014 1843 182 196. doi: 10.1016/j.bbamcr.2013.06.031
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 5
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • Guerriero CJ, Brodsky JL, The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiol Rev 2012 92 537 576. doi: 10.1152/physrev.00027.2011
    • (2012) Physiol Rev , vol.92 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 6
    • 79952758037 scopus 로고    scopus 로고
    • Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease: Endoplasmic reticulum stress as a mediator of pathogenesis
    • Dickhout JG, Carlisle RE, Austin RC, Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease: endoplasmic reticulum stress as a mediator of pathogenesis. Circ Res 2011 108 629 642. doi: 10.1161/CIRCRESAHA.110.226803
    • (2011) Circ Res , vol.108 , pp. 629-642
    • Dickhout, J.G.1    Carlisle, R.E.2    Austin, R.C.3
  • 7
    • 78349265743 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease
    • Minamino T, Komuro I, Kitakaze M, Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease. Circ Res 2010 107 1071 1082. doi: 10.1161/CIRCRESAHA.110.227819
    • (2010) Circ Res , vol.107 , pp. 1071-1082
    • Minamino, T.1    Komuro, I.2    Kitakaze, M.3
  • 8
    • 84872683707 scopus 로고    scopus 로고
    • New concepts of endoplasmic reticulum function in the heart: Programmed to conserve
    • Doroudgar S, Glembotski CC, New concepts of endoplasmic reticulum function in the heart: programmed to conserve. J Mol Cell Cardiol 2013 55 85 91. doi: 10.1016/j.yjmcc.2012.10.006
    • (2013) J Mol Cell Cardiol , vol.55 , pp. 85-91
    • Doroudgar, S.1    Glembotski, C.C.2
  • 9
    • 84865412590 scopus 로고    scopus 로고
    • The endoplasmic reticulum in cardiovascular health and disease
    • Millott R, Dudek E, Michalak M, The endoplasmic reticulum in cardiovascular health and disease. Can J Physiol Pharmacol 2012 90 1209 1217. doi: 10.1139/y2012-058
    • (2012) Can J Physiol Pharmacol , vol.90 , pp. 1209-1217
    • Millott, R.1    Dudek, E.2    Michalak, M.3
  • 10
    • 84870763849 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum-associated degradation system
    • Olzmann JA, Kopito RR, Christianson JC, The mammalian endoplasmic reticulum-associated degradation system. Cold Spring Harb Perspect Biol 2012 5 a013185. doi: 10.1101/cshperspect.a013185
    • (2012) Cold Spring Harb Perspect Biol , vol.5 , pp. a013185
    • Olzmann, J.A.1    Kopito, R.R.2    Christianson, J.C.3
  • 11
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra JD, Kaufman RJ, The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 2007 18 716 731. doi: 10.1016/j.semcdb.2007.09.003
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 12
    • 36048931354 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in the heart
    • Glembotski CC, Endoplasmic reticulum stress in the heart. Circ Res 2007 101 975 984. doi: 10.1161/CIRCRESAHA.107.161273
    • (2007) Circ Res , vol.101 , pp. 975-984
    • Glembotski, C.C.1
  • 13
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D, The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011 334 1081 1086. doi: 10.1126/science.1209038
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 14
    • 0030850013 scopus 로고    scopus 로고
    • Interaction of ATF6 and serum response factor
    • Zhu C, Johansen FE, Prywes R, Interaction of ATF6 and serum response factor. Mol Cell Biol 1997 17 4957 4966
    • (1997) Mol Cell Biol , vol.17 , pp. 4957-4966
    • Zhu, C.1    Johansen, F.E.2    Prywes, R.3
  • 15
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K, Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999 10 3787 3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 16
    • 33745019669 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6
    • Martindale JJ, Fernandez R, Thuerauf D, Whittaker R, Gude N, Sussman MA, Glembotski CC, Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6. Circ Res 2006 98 1186 1193. doi: 10.1161/01.RES.0000220643.65941.8d
    • (2006) Circ Res , vol.98 , pp. 1186-1193
    • Martindale, J.J.1    Fernandez, R.2    Thuerauf, D.3    Whittaker, R.4    Gude, N.5    Sussman, M.A.6    Glembotski, C.C.7
  • 18
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto K, Sato T, Matsui T, Sato M, Okada T, Yoshida H, Harada A, Mori K, Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell 2007 13 365 376. doi: 10.1016/j.devcel.2007.07.018
    • (2007) Dev Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 19
    • 84903795970 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease
    • Cao SS, Kaufman RJ, Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease. Antioxid Redox Signal 2014 21 396 413. doi: 10.1089/ars.2014.5851
    • (2014) Antioxid Redox Signal , vol.21 , pp. 396-413
    • Cao, S.S.1    Kaufman, R.J.2
  • 20
    • 84944683146 scopus 로고    scopus 로고
    • Reperfusion injury and reactive oxygen species: The evolution of a concept
    • Granger DN, Kvietys PR, Reperfusion injury and reactive oxygen species: The evolution of a concept. Redox Biol 2015 6 524 551. doi: 10.1016/j.redox.2015.08.020
    • (2015) Redox Biol , vol.6 , pp. 524-551
    • Granger, D.N.1    Kvietys, P.R.2
  • 22
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M, Mori K, ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 2000 20 6755 6767
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 23
    • 0037036412 scopus 로고    scopus 로고
    • Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16
    • Thuerauf DJ, Morrison LE, Hoover H, Glembotski CC, Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16. J Biol Chem 2002 277 20734 20739. doi: 10.1074/jbc.M201749200
    • (2002) J Biol Chem , vol.277 , pp. 20734-20739
    • Thuerauf, D.J.1    Morrison, L.E.2    Hoover, H.3    Glembotski, C.C.4
  • 24
    • 2442647920 scopus 로고    scopus 로고
    • Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction
    • Thuerauf DJ, Morrison L, Glembotski CC, Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction. J Biol Chem 2004 279 21078 21084. doi: 10.1074/jbc.M400713200
    • (2004) J Biol Chem , vol.279 , pp. 21078-21084
    • Thuerauf, D.J.1    Morrison, L.2    Glembotski, C.C.3
  • 25
    • 84900547822 scopus 로고    scopus 로고
    • Proteomic mapping of proteins released during necrosis and apoptosis from cultured neonatal cardiac myocytes
    • Marshall KD, Edwards MA, Krenz M, Davis JW, Baines CP, Proteomic mapping of proteins released during necrosis and apoptosis from cultured neonatal cardiac myocytes. Am J Physiol Cell Physiol 2014 306 C639 C647. doi: 10.1152/ajpcell.00167.2013
    • (2014) Am J Physiol Cell Physiol , vol.306 , pp. C639-C647
    • Marshall, K.D.1    Edwards, M.A.2    Krenz, M.3    Davis, J.W.4    Baines, C.P.5
  • 26
    • 2942560510 scopus 로고    scopus 로고
    • Proteins released from degenerating neurons are surrogate markers for acute brain damage
    • Siman R, McIntosh TK, Soltesz KM, Chen Z, Neumar RW, Roberts VL, Proteins released from degenerating neurons are surrogate markers for acute brain damage. Neurobiol Dis 2004 16 311 320. doi: 10.1016/j.nbd.2004.03.016
    • (2004) Neurobiol Dis , vol.16 , pp. 311-320
    • Siman, R.1    McIntosh, T.K.2    Soltesz, K.M.3    Chen, Z.4    Neumar, R.W.5    Roberts, V.L.6
  • 27
    • 19544392547 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 mediated caspase-independent cell death after ischemia/reperfusion
    • van Wijk SJ, Hageman GJ, Poly(ADP-ribose) polymerase-1 mediated caspase-independent cell death after ischemia/reperfusion. Free Radic Biol Med 2005 39 81 90. doi: 10.1016/j.freeradbiomed.2005.03.021
    • (2005) Free Radic Biol Med , vol.39 , pp. 81-90
    • Van Wijk, S.J.1    Hageman, G.J.2
  • 28
    • 84978663224 scopus 로고    scopus 로고
    • Measurement of reactive oxygen species, reactive nitrogen species, and redox-dependent signaling in the cardiovascular system: A scientific statement from the American Heart Association
    • Griendling KK, Touyz RM, Zweier JL, Dikalov S, Chilian W, Chen YR, Harrison DG, Bhatnagar A, American Heart Association Council on Basic Cardiovascular Sciences Measurement of reactive oxygen species, reactive nitrogen species, and redox-dependent signaling in the cardiovascular system: a scientific statement from the American Heart Association. Circ Res 2016 119 e39 e75. doi: 10.1161/RES.0000000000000110
    • (2016) Circ Res , vol.119 , pp. e39-e75
    • Griendling, K.K.1    Touyz, R.M.2    Zweier, J.L.3    Dikalov, S.4    Chilian, W.5    Chen, Y.R.6    Harrison, D.G.7    Bhatnagar, A.8
  • 29
    • 84961673932 scopus 로고    scopus 로고
    • Redox signaling in the cardiomyocyte: From physiology to failure
    • Santos CX, Raza S, Shah AM, Redox signaling in the cardiomyocyte: from physiology to failure. Int J Biochem Cell Biol 2016 74 145 151. doi: 10.1016/j.biocel.2016.03.002
    • (2016) Int J Biochem Cell Biol , vol.74 , pp. 145-151
    • Santos, C.X.1    Raza, S.2    Shah, A.M.3
  • 31
    • 33751279204 scopus 로고    scopus 로고
    • Catalase-overexpressing transgenic mouse heart is resistant to ischemia-reperfusion injury
    • Li G, Chen Y, Saari JT, Kang YJ, Catalase-overexpressing transgenic mouse heart is resistant to ischemia-reperfusion injury. Am J Physiol 1997 273 H1090 H1095
    • (1997) Am J Physiol , vol.273 , pp. H1090-H1095
    • Li, G.1    Chen, Y.2    Saari, J.T.3    Kang, Y.J.4
  • 32
    • 0037785315 scopus 로고    scopus 로고
    • NADPH oxidase-derived superoxide anion mediates angiotensin II-induced cardiac hypertrophy
    • Nakagami H, Takemoto M, Liao JK, NADPH oxidase-derived superoxide anion mediates angiotensin II-induced cardiac hypertrophy. J Mol Cell Cardiol 2003 35 851 859
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 851-859
    • Nakagami, H.1    Takemoto, M.2    Liao, J.K.3
  • 34
    • 84929300310 scopus 로고    scopus 로고
    • The antioxidant machinery of the endoplasmic reticulum: Protection and signaling
    • Delaunay-Moisan A, Appenzeller-Herzog C, The antioxidant machinery of the endoplasmic reticulum: Protection and signaling. Free Radic Biol Med 2015 83 341 351. doi: 10.1016/j.freeradbiomed.2015.02.019
    • (2015) Free Radic Biol Med , vol.83 , pp. 341-351
    • Delaunay-Moisan, A.1    Appenzeller-Herzog, C.2
  • 35
    • 84861567265 scopus 로고    scopus 로고
    • Redox signaling loops in the unfolded protein response
    • Higa A, Chevet E, Redox signaling loops in the unfolded protein response. Cell Signal 2012 24 1548 1555. doi: 10.1016/j.cellsig.2012.03.011
    • (2012) Cell Signal , vol.24 , pp. 1548-1555
    • Higa, A.1    Chevet, E.2
  • 36
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu BP, Weissman JS, Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 2004 164 341 346. doi: 10.1083/jcb.200311055
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 39
    • 79960017554 scopus 로고    scopus 로고
    • Peroxiredoxin 5: Structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin
    • Knoops B, Goemaere J, Van der Eecken V, Declercq JP, Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin. Antioxid Redox Signal 2011 15 817 829. doi: 10.1089/ars.2010.3584
    • (2011) Antioxid Redox Signal , vol.15 , pp. 817-829
    • Knoops, B.1    Goemaere, J.2    Van Der Eecken, V.3    Declercq, J.P.4
  • 40
    • 84942790786 scopus 로고    scopus 로고
    • Membrane-bound selenoproteins
    • Liu J, Rozovsky S, Membrane-bound selenoproteins. Antioxid Redox Signal 2015 23 795 813. doi: 10.1089/ars.2015.6388
    • (2015) Antioxid Redox Signal , vol.23 , pp. 795-813
    • Liu, J.1    Rozovsky, S.2
  • 41
    • 67650805623 scopus 로고    scopus 로고
    • The human selenoproteome: Recent insights into functions and regulation
    • Reeves MA, Hoffmann PR, The human selenoproteome: recent insights into functions and regulation. Cell Mol Life Sci 2009 66 2457 2478. doi: 10.1007/s00018-009-0032-4
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2457-2478
    • Reeves, M.A.1    Hoffmann, P.R.2


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