메뉴 건너뛰기




Volumn 112, Issue 7, 2013, Pages 1046-1058

Role of the ubiquitin proteasome system in the heart

Author keywords

heart failure; ischemia; myocardial remodeling, ventricular; proteasome endopeptidase complex; ubiquitin

Indexed keywords

ATROGIN 1; BORTEZOMIB; EPOXOMICIN; MUSCLE RING FINGER 1 PROTEIN; PROTEASOME; PROTEIN MDM2; SIAH2 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 84876374189     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.112.300521     Document Type: Review
Times cited : (110)

References (147)
  • 1
    • 84855353573 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2012 update: A report from the American Heart Association
    • Roger VL, Go AS, Lloyd-Jones DM, et al.; American Heart Association Statistics Committee and Stroke Statistics Subcommittee. Heart disease and stroke statistics-2012 update: a report from the American Heart Association. Circulation. 2012;125:e2-e220.
    • (2012) Circulation. , vol.125
    • Roger, V.L.1    Go, A.S.2    Lloyd-Jones, D.M.3
  • 2
    • 20344401818 scopus 로고    scopus 로고
    • Mechanisms and models in heart failure: The biomechanical model and beyond
    • Mann DL, Bristow MR. Mechanisms and models in heart failure: the biomechanical model and beyond. Circulation. 2005;111:2837-2849.
    • (2005) Circulation. , vol.111 , pp. 2837-2849
    • Mann, D.L.1    Bristow, M.R.2
  • 5
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteo-lytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteo-lytic pathway: destruction for the sake of construction. Physiol Rev. 2002;82:373-428.
    • (2002) Physiol Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 6
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature. 2003;426:895-899.
    • (2003) Nature. , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 8
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: Tipping the scales of cancer
    • Frescas D, Pagano M. Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat Rev Cancer. 2008;8:438-449.
    • (2008) Nat Rev Cancer. , vol.8 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 10
    • 25144443718 scopus 로고    scopus 로고
    • The ubiquitin system for protein degradation and some of its roles in the control of the cell-division cycle (Nobel lecture)
    • Hershko A. The ubiquitin system for protein degradation and some of its roles in the control of the cell-division cycle (Nobel lecture). Angew Chem Int Ed Engl. 2005;44:5932-5943.
    • (2005) Angew Chem Int Ed Engl. , vol.44 , pp. 5932-5943
    • Hershko, A.1
  • 11
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol. 2005;6:9-20.
    • (2005) Nat Rev Mol Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 15
    • 79951778377 scopus 로고    scopus 로고
    • Myocardial remodeling: Cellular and extracellular events and targets
    • Dixon JA, Spinale FG. Myocardial remodeling: cellular and extracellular events and targets. Annu Rev Physiol. 2011;73:47-68.
    • (2011) Annu Rev Physiol. , vol.73 , pp. 47-68
    • Dixon, J.A.1    Spinale, F.G.2
  • 16
    • 0016681078 scopus 로고
    • Wall stress and patterns of hypertrophy in the human left ventricle
    • Grossman W, Jones D, McLaurin LP. Wall stress and patterns of hypertrophy in the human left ventricle. J Clin Invest. 1975;56:56-64.
    • (1975) J Clin Invest. , vol.56 , pp. 56-64
    • Grossman, W.1    Jones, D.2    McLaurin, L.P.3
  • 18
    • 0025280867 scopus 로고
    • Prognostic implications of echocardiographically determined left ventricular mass in the Framingham Heart Study
    • Levy D, Garrison RJ, Savage DD, Kannel WB, Castelli WP. Prognostic implications of echocardiographically determined left ventricular mass in the Framingham Heart Study. N Engl J Med. 1990;322:1561-1566.
    • (1990) N Engl J Med. , vol.322 , pp. 1561-1566
    • Levy, D.1    Garrison, R.J.2    Savage, D.D.3    Kannel, W.B.4    Castelli, W.P.5
  • 23
    • 30544446127 scopus 로고    scopus 로고
    • Depression of pro-teasome activities during the progression of cardiac dysfunction in pressure-overloaded heart of mice
    • Tsukamoto O, Minamino T, Okada K, et al. Depression of pro-teasome activities during the progression of cardiac dysfunction in pressure-overloaded heart of mice. Biochem Biophys Res Commun. 2006;340:1125-1133.
    • (2006) Biochem Biophys Res Commun. , vol.340 , pp. 1125-1133
    • Tsukamoto, O.1    Minamino, T.2    Okada, K.3
  • 31
    • 77957356238 scopus 로고    scopus 로고
    • Proteasome functional insuffciency activates the calcineu-rin-NFAT pathway in cardiomyocytes and promotes maladaptive remodelling of stressed mouse hearts
    • Tang M, Li J, Huang W, Su H, Liang Q, Tian Z, Horak KM, Molkentin JD, Wang X. Proteasome functional insuffciency activates the calcineu-rin-NFAT pathway in cardiomyocytes and promotes maladaptive remodelling of stressed mouse hearts. Cardiovasc Res. 2010;88:424-433.
    • (2010) Cardiovasc Res. , vol.88 , pp. 424-433
    • Tang, M.1    Li, J.2    Huang, W.3    Su, H.4    Liang, Q.5    Tian, Z.6    Horak, K.M.7    Molkentin, J.D.8    Wang, X.9
  • 32
    • 78149295963 scopus 로고    scopus 로고
    • Too much of a good thing is bad: Proteasome inhibition induces stressed hearts to fail
    • Carrier L. Too much of a good thing is bad: proteasome inhibition induces stressed hearts to fail. Cardiovasc Res. 2010;88:389-390.
    • (2010) Cardiovasc Res. , vol.88 , pp. 389-390
    • Carrier, L.1
  • 34
    • 0036143851 scopus 로고    scopus 로고
    • Genetic alterations that inhibit in vivo pressure-overload hypertrophy prevent cardiac dysfunction despite increased wall stress
    • Esposito G, Rapacciuolo A, Naga Prasad SV, Takaoka H, Thomas SA, Koch WJ, Rockman HA. Genetic alterations that inhibit in vivo pressure-overload hypertrophy prevent cardiac dysfunction despite increased wall stress. Circulation. 2002;105:85-92.
    • (2002) Circulation. , vol.105 , pp. 85-92
    • Esposito, G.1    Rapacciuolo, A.2    Naga Prasad, S.V.3    Takaoka, H.4    Thomas, S.A.5    Koch, W.J.6    Rockman, H.A.7
  • 35
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li HH, Kedar V, Zhang C, McDonough H, Arya R, Wang DZ, Patterson C. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J Clin Invest. 2004;114:1058-1071.
    • (2004) J Clin Invest. , vol.114 , pp. 1058-1071
    • Li, H.H.1    Kedar, V.2    Zhang, C.3    McDonough, H.4    Arya, R.5    Wang, D.Z.6    Patterson, C.7
  • 36
    • 36049026136 scopus 로고    scopus 로고
    • Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of Forkhead proteins
    • Li HH, Willis MS, Lockyer P, Miller N, McDonough H, Glass DJ, Patterson C. Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of Forkhead proteins. J Clin Invest. 2007;117:3211-3223.
    • (2007) J Clin Invest. , vol.117 , pp. 3211-3223
    • Li, H.H.1    Willis, M.S.2    Lockyer, P.3    Miller, N.4    McDonough, H.5    Glass, D.J.6    Patterson, C.7
  • 39
    • 33645055949 scopus 로고    scopus 로고
    • Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes
    • Liu J, Tang M, Mestril R, Wang X. Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes. J Mol Cell Cardiol. 2006;40:451-454.
    • (2006) J Mol Cell Cardiol. , vol.40 , pp. 451-454
    • Liu, J.1    Tang, M.2    Mestril, R.3    Wang, X.4
  • 40
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • Liu J, Chen Q, Huang W, Horak KM, Zheng H, Mestril R, Wang X. Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J. 2006;20:362-364.
    • (2006) FASEB J. , vol.20 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5    Mestril, R.6    Wang, X.7
  • 42
    • 0036790590 scopus 로고    scopus 로고
    • Mouse heat shock transcription factor 1 defciency alters cardiac redox ho-meostasis and increases mitochondrial oxidative damage
    • Yan LJ, Christians ES, Liu L, Xiao X, Sohal RS, Benjamin IJ. Mouse heat shock transcription factor 1 defciency alters cardiac redox ho-meostasis and increases mitochondrial oxidative damage. EMBO J. 2002;21:5164-5172.
    • (2002) EMBO J. , vol.21 , pp. 5164-5172
    • Yan, L.J.1    Christians, E.S.2    Liu, L.3    Xiao, X.4    Sohal, R.S.5    Benjamin, I.J.6
  • 44
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice
    • Wang X, Osinska H, Klevitsky R, Gerdes AM, Nieman M, Lorenz J, Hewett T, Robbins J. Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice. Circ Res. 2001;89:84-91.
    • (2001) Circ Res. , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8
  • 47
    • 78149416783 scopus 로고    scopus 로고
    • Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways
    • Zhang H, Rajasekaran NS, Orosz A, Xiao X, Rechsteiner M, Benjamin IJ. Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways. J Mol Cell Cardiol. 2010;49:918-930.
    • (2010) J Mol Cell Cardiol. , vol.49 , pp. 918-930
    • Zhang, H.1    Rajasekaran, N.S.2    Orosz, A.3    Xiao, X.4    Rechsteiner, M.5    Benjamin, I.J.6
  • 48
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitina-tion
    • den Engelsman J, Keijsers V, de Jong WW, Boelens WC. The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitina-tion. J Biol Chem. 2003;278:4699-4704.
    • (2003) J Biol Chem. , vol.278 , pp. 4699-4704
    • Den Engelsman, J.1    Keijsers, V.2    De Jong, W.W.3    Boelens, W.C.4
  • 50
    • 84860498637 scopus 로고    scopus 로고
    • Genetics of hypertrophic and dilated cardiomy-opathy
    • Friedrich FW, Carrier L. Genetics of hypertrophic and dilated cardiomy-opathy. Curr Pharm Biotechnol. 2012;13:2467-2476.
    • (2012) Curr Pharm Biotechnol. , vol.13 , pp. 2467-2476
    • Friedrich, F.W.1    Carrier, L.2
  • 53
    • 84866533811 scopus 로고    scopus 로고
    • Human molecular genetic and functional studies identify TRIM63, encoding Muscle RING Finger Protein 1, as a novel gene for human hypertrophic cardiomyopathy
    • Chen SN, Czernuszewicz G, Tan Y, Lombardi R, Jin J, Willerson JT, Marian AJ. Human molecular genetic and functional studies identify TRIM63, encoding Muscle RING Finger Protein 1, as a novel gene for human hypertrophic cardiomyopathy. Circ Res. 2012;111:907-919.
    • (2012) Circ Res. , vol.111 , pp. 907-919
    • Chen, S.N.1    Czernuszewicz, G.2    Tan, Y.3    Lombardi, R.4    Jin, J.5    Willerson, J.T.6    Marian, A.J.7
  • 54
    • 85047678791 scopus 로고
    • Reperfusion induced injury: Manifestations, mechanisms, and clinical relevance
    • Hearse DJ, Bolli R. Reperfusion induced injury: manifestations, mechanisms, and clinical relevance. Cardiovasc Res. 1992;26:101-108.
    • (1992) Cardiovasc Res. , vol.26 , pp. 101-108
    • Hearse, D.J.1    Bolli, R.2
  • 56
    • 0033083426 scopus 로고    scopus 로고
    • Cardioprotective effects of a novel proteasome inhibitor following ischemia and reperfusion in the isolated perfused rat heart
    • Campbell B, Adams J, Shin YK, Lefer AM. Cardioprotective effects of a novel proteasome inhibitor following ischemia and reperfusion in the isolated perfused rat heart. J Mol Cell Cardiol. 1999;31:467-476.
    • (1999) J Mol Cell Cardiol. , vol.31 , pp. 467-476
    • Campbell, B.1    Adams, J.2    Shin, Y.K.3    Lefer, A.M.4
  • 58
    • 34250368734 scopus 로고    scopus 로고
    • Proteasome inhibition attenuates infarct size and preserves cardiac function in a mu-rine model of myocardial ischemia-reperfusion injury
    • Stansfeld WE, Moss NC, Willis MS, Tang R, Selzman CH. Proteasome inhibition attenuates infarct size and preserves cardiac function in a mu-rine model of myocardial ischemia-reperfusion injury. Ann Thorac Surg. 2007;84:120-125.
    • (2007) Ann Thorac Surg. , vol.84 , pp. 120-125
    • Stansfeld, W.E.1    Moss, N.C.2    Willis, M.S.3    Tang, R.4    Selzman, C.H.5
  • 62
    • 33845774348 scopus 로고    scopus 로고
    • Optimal determination of heart tissue 26S-proteasome activity requires maximal stimulating ATP concentrations
    • Powell SR, Davies KJ, Divald A. Optimal determination of heart tissue 26S-proteasome activity requires maximal stimulating ATP concentrations. J Mol Cell Cardiol. 2007;42:265-269.
    • (2007) J Mol Cell Cardiol. , vol.42 , pp. 265-269
    • Powell, S.R.1    Davies, K.J.2    Divald, A.3
  • 63
    • 39149124870 scopus 로고    scopus 로고
    • Oxidative injury induces selective rather than global inhibition of proteasomal activity
    • Gurusamy N, Goswami S, Malik G, Das DK. Oxidative injury induces selective rather than global inhibition of proteasomal activity. J Mol Cell Cardiol. 2008;44:419-428.
    • (2008) J Mol Cell Cardiol. , vol.44 , pp. 419-428
    • Gurusamy, N.1    Goswami, S.2    Malik, G.3    Das, D.K.4
  • 64
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and isch-emia/reperfusion injury in mice
    • Li J, Horak KM, Su H, Sanbe A, Robbins J, Wang X. Enhancement of proteasomal function protects against cardiac proteinopathy and isch-emia/reperfusion injury in mice. J Clin Invest. 2011;121:3689-3700.
    • (2011) J Clin Invest. , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 65
    • 77954215848 scopus 로고    scopus 로고
    • Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits
    • Divald A, Kivity S, Wang P, Hochhauser E, Roberts B, Teichberg S, Gomes AV, Powell SR. Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits. Circ Res. 2010;106:1829-1838.
    • (2010) Circ Res. , vol.106 , pp. 1829-1838
    • Divald, A.1    Kivity, S.2    Wang, P.3    Hochhauser, E.4    Roberts, B.5    Teichberg, S.6    Gomes, A.V.7    Powell, S.R.8
  • 66
    • 0026663450 scopus 로고
    • Post-transient ischemia increase in ubiq-uitin conjugates in the early reperfusion
    • Hayashi T, Takada K, Matsuda M. Post-transient ischemia increase in ubiq-uitin conjugates in the early reperfusion. Neuroreport. 1992;3:519-520.
    • (1992) Neuroreport. , vol.3 , pp. 519-520
    • Hayashi, T.1    Takada, K.2    Matsuda, M.3
  • 67
    • 0033588087 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteoly-sis during oxidative stress. Identifcation of proteasomes as target molecules
    • Okada K, Wangpoengtrakul C, Osawa T, Toyokuni S, Tanaka K, Uchida K. 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteoly-sis during oxidative stress. Identifcation of proteasomes as target molecules. J Biol Chem. 1999;274:23787-23793.
    • (1999) J Biol Chem. , vol.274 , pp. 23787-23793
    • Okada, K.1    Wangpoengtrakul, C.2    Osawa, T.3    Toyokuni, S.4    Tanaka, K.5    Uchida, K.6
  • 68
  • 70
    • 78649894468 scopus 로고    scopus 로고
    • Physiological levels of ATP negatively regulate proteasome function
    • Huang H, Zhang X, Li S, et al. Physiological levels of ATP negatively regulate proteasome function. Cell Res. 2010;20:1372-1385.
    • (2010) Cell Res. , vol.20 , pp. 1372-1385
    • Huang, H.1    Zhang, X.2    Li, S.3
  • 72
    • 84865497050 scopus 로고    scopus 로고
    • Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocar-dial ischemia-reperfusion injury in mice
    • Tian Z, Zheng H, Li J, Li Y, Su H, Wang X. Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocar-dial ischemia-reperfusion injury in mice. Circ Res. 2012;111:532-542.
    • (2012) Circ Res. , vol.111 , pp. 532-542
    • Tian, Z.1    Zheng, H.2    Li, J.3    Li, Y.4    Su, H.5    Wang, X.6
  • 74
    • 56649108096 scopus 로고    scopus 로고
    • Acute severe cardiac failure in a myeloma patient due to proteasome inhibitor bortezomib
    • Hacihanefoglu A, Tarkun P, Gonullu E. Acute severe cardiac failure in a myeloma patient due to proteasome inhibitor bortezomib. Int J Hematol. 2008;88:219-222.
    • (2008) Int J Hematol. , vol.88 , pp. 219-222
    • Hacihanefoglu, A.1    Tarkun, P.2    Gonullu, E.3
  • 75
    • 57349164418 scopus 로고    scopus 로고
    • Ischemic preconditioning-induced cardioprotection is lost in mice with immunoproteasome subunit low molecular mass polypeptide-2 defciency
    • Cai ZP, Shen Z, Van Kaer L, Becker LC. Ischemic preconditioning-induced cardioprotection is lost in mice with immunoproteasome subunit low molecular mass polypeptide-2 defciency. FASEB J. 2008;22:4248-4257.
    • (2008) FASEB J. , vol.22 , pp. 4248-4257
    • Cai, Z.P.1    Shen, Z.2    Van Kaer, L.3    Becker, L.C.4
  • 78
    • 79955146992 scopus 로고    scopus 로고
    • Heterogeneous cardiac proteasomes: Mandated by diverse substrates?
    • Scruggs SB, Ping P, Zong C. Heterogeneous cardiac proteasomes: mandated by diverse substrates? Physiology (Bethesda). 2011;26:106-114.
    • (2011) Physiology (Bethesda). , vol.26 , pp. 106-114
    • Scruggs, S.B.1    Ping, P.2    Zong, C.3
  • 79
    • 43049092644 scopus 로고    scopus 로고
    • Understanding proteasome assembly and regulation: Importance to cardiovascular medicine
    • Young GW, Wang Y, Ping P. Understanding proteasome assembly and regulation: importance to cardiovascular medicine. Trends Cardiovasc Med. 2008;18:93-98.
    • (2008) Trends Cardiovasc Med. , vol.18 , pp. 93-98
    • Young, G.W.1    Wang, Y.2    Ping, P.3
  • 80
    • 72949105782 scopus 로고    scopus 로고
    • Multiple cardiac protea-some subtypes differ in their susceptibility to proteasome inhibitors
    • Kloss A, Meiners S, Ludwig A, Dahlmann B. Multiple cardiac protea-some subtypes differ in their susceptibility to proteasome inhibitors. Cardiovasc Res. 2010;85:367-375.
    • (2010) Cardiovasc Res. , vol.85 , pp. 367-375
    • Kloss, A.1    Meiners, S.2    Ludwig, A.3    Dahlmann, B.4
  • 81
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class i molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 1994;78:761-771.
    • (1994) Cell. , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 82
    • 0021917182 scopus 로고
    • The ATP dependence of the degradation of short-and long-lived proteins in growing fbroblasts
    • Gronostajski RM, Pardee AB, Goldberg AL. The ATP dependence of the degradation of short-and long-lived proteins in growing fbroblasts. J Biol Chem. 1985;260:3344-3349.
    • (1985) J Biol Chem. , vol.260 , pp. 3344-3349
    • Gronostajski, R.M.1    Pardee, A.B.2    Goldberg, A.L.3
  • 83
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofbrillar proteins in rabbit muscle extracts
    • Solomon V, Goldberg AL. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofbrillar proteins in rabbit muscle extracts. J Biol Chem. 1996;271:26690-26697.
    • (1996) J Biol Chem. , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 85
  • 89
    • 0035941020 scopus 로고    scopus 로고
    • Identifcation of ubiquitin ligas-es required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, et al. Identifcation of ubiquitin ligas-es required for skeletal muscle atrophy. Science. 2001;294:1704-1708.
    • (2001) Science. , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 90
    • 79960343312 scopus 로고    scopus 로고
    • Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-kappaB
    • Usui S, Maejima Y, Pain J, Hong C, Cho J, Park JY, Zablocki D, Tian B, Glass DJ, Sadoshima J. Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-kappaB. Circ Res. 2011;109:161-171.
    • (2011) Circ Res. , vol.109 , pp. 161-171
    • Usui, S.1    Maejima, Y.2    Pain, J.3    Hong, C.4    Cho, J.5    Park, J.Y.6    Zablocki, D.7    Tian, B.8    Glass, D.J.9    Sadoshima, J.10
  • 91
    • 79960376749 scopus 로고    scopus 로고
    • Atrogin1/MAFbx: What atrophy, hypertrophy, and cardiac failure have in common
    • Lee D, Goldberg A. Atrogin1/MAFbx: what atrophy, hypertrophy, and cardiac failure have in common. Circ Res. 2011;109:123-126.
    • (2011) Circ Res. , vol.109 , pp. 123-126
    • Lee, D.1    Goldberg, A.2
  • 95
    • 11244260636 scopus 로고    scopus 로고
    • Muscle ring fnger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy
    • Arya R, Kedar V, Hwang JR, McDonough H, Li HH, Taylor J, Patterson C. Muscle ring fnger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy. J Cell Biol. 2004;167:1147-1159.
    • (2004) J Cell Biol. , vol.167 , pp. 1147-1159
    • Arya, R.1    Kedar, V.2    Hwang, J.R.3    McDonough, H.4    Li, H.H.5    Taylor, J.6    Patterson, C.7
  • 96
    • 79952748998 scopus 로고    scopus 로고
    • The ubiquitin ligase MuRF1 protects against cardiac ischemia/reperfusion injury by its proteasome-dependent degradation of phospho-c-Jun
    • Li HH, Du J, Fan YN, Zhang ML, Liu DP, Li L, Lockyer P, Kang EY, Patterson C, Willis MS. The ubiquitin ligase MuRF1 protects against cardiac ischemia/reperfusion injury by its proteasome-dependent degradation of phospho-c-Jun. Am J Pathol. 2011;178:1043-1058.
    • (2011) Am J Pathol. , vol.178 , pp. 1043-1058
    • Li, H.H.1    Du, J.2    Fan, Y.N.3    Zhang, M.L.4    Liu, D.P.5    Li, L.6    Lockyer, P.7    Kang, E.Y.8    Patterson, C.9    Willis, M.S.10
  • 98
    • 79960675340 scopus 로고    scopus 로고
    • Analysis of p53 and NF-κB signaling in modulating the cardiomyocyte fate during hypertrophy
    • Chatterjee A, Mir SA, Dutta D, Mitra A, Pathak K, Sarkar S. Analysis of p53 and NF-κB signaling in modulating the cardiomyocyte fate during hypertrophy. J Cell Physiol. 2011;226:2543-2554.
    • (2011) J Cell Physiol. , vol.226 , pp. 2543-2554
    • Chatterjee, A.1    Mir, S.A.2    Dutta, D.3    Mitra, A.4    Pathak, K.5    Sarkar, S.6
  • 100
    • 79960346500 scopus 로고    scopus 로고
    • Puma deletion delays cardiac dysfunction in murine heart failure models through attenuation of apoptosis
    • Mandl A, Huong Pham L, Toth K, Zambetti G, Erhardt P. Puma deletion delays cardiac dysfunction in murine heart failure models through attenuation of apoptosis. Circulation. 2011;124:31-39.
    • (2011) Circulation. , vol.124 , pp. 31-39
    • Mandl, A.1    Huong Pham, L.2    Toth, K.3    Zambetti, G.4    Erhardt, P.5
  • 101
    • 77955871461 scopus 로고    scopus 로고
    • The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
    • Manfredi JJ. The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor. Genes Dev. 2010;24:1580-1589.
    • (2010) Genes Dev. , vol.24 , pp. 1580-1589
    • Manfredi, J.J.1
  • 102
    • 33645643078 scopus 로고    scopus 로고
    • Differential regulation of cardio-myocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase
    • Toth A, Nickson P, Qin LL, Erhardt P. Differential regulation of cardio-myocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase. J Biol Chem. 2006;281:3679-3689.
    • (2006) J Biol Chem. , vol.281 , pp. 3679-3689
    • Toth, A.1    Nickson, P.2    Qin, L.L.3    Erhardt, P.4
  • 103
    • 34247158646 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2
    • Foo RS, Chan LK, Kitsis RN, Bennett MR. Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2. J Biol Chem. 2007;282:5529-5535.
    • (2007) J Biol Chem. , vol.282 , pp. 5529-5535
    • Foo, R.S.1    Chan, L.K.2    Kitsis, R.N.3    Bennett, M.R.4
  • 104
    • 70350447388 scopus 로고    scopus 로고
    • Regulation of expression of the rat orthologue of mouse double minute 2 (MDM2) by H(2)O(2)-induced oxidative stress in neonatal rat cardiac myocytes
    • Pikkarainen S, Kennedy RA, Marshall AK, Tham el L, Lay K, Kriz TA, Handa BS, Clerk A, Sugden PH. Regulation of expression of the rat orthologue of mouse double minute 2 (MDM2) by H(2)O(2)-induced oxidative stress in neonatal rat cardiac myocytes. J Biol Chem. 2009;284:27195-27210.
    • (2009) J Biol Chem. , vol.284 , pp. 27195-27210
    • Pikkarainen, S.1    Kennedy, R.A.2    Marshall, A.K.3    Tham El, L.4    Lay, K.5    Kriz, T.A.6    Handa, B.S.7    Clerk, A.8    Sugden, P.H.9
  • 105
    • 79951828819 scopus 로고    scopus 로고
    • Identifcation of a mechanism underlying regulation of the anti-angio-genic forkhead transcription factor FoxO1 in cultured endothelial cells and ischemic muscle
    • Milkiewicz M, Roudier E, Doyle JL, Trifonova A, Birot O, Haas TL. Identifcation of a mechanism underlying regulation of the anti-angio-genic forkhead transcription factor FoxO1 in cultured endothelial cells and ischemic muscle. Am J Pathol. 2011;178:935-944.
    • (2011) Am J Pathol. , vol.178 , pp. 935-944
    • Milkiewicz, M.1    Roudier, E.2    Doyle, J.L.3    Trifonova, A.4    Birot, O.5    Haas, T.L.6
  • 106
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin
    • Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ. Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. Science. 2001;294:1307-1313.
    • (2001) Science. , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 108
    • 19344370546 scopus 로고    scopus 로고
    • CHIP, a cochaper-one/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice
    • Zhang C, Xu Z, He XR, Michael LH, Patterson C. CHIP, a cochaper-one/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice. Am J Physiol Heart Circ Physiol. 2005;288:H2836-H2842.
    • (2005) Am J Physiol Heart Circ Physiol. , vol.288
    • Zhang, C.1    Xu, Z.2    He, X.R.3    Michael, L.H.4    Patterson, C.5
  • 109
    • 65449173266 scopus 로고    scopus 로고
    • CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation
    • Xie P, Fan Y, Zhang H, Zhang Y, She M, Gu D, Patterson C, Li H. CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation. Mol Cell Biol. 2009;29:2398-2408.
    • (2009) Mol Cell Biol. , vol.29 , pp. 2398-2408
    • Xie, P.1    Fan, Y.2    Zhang, H.3    Zhang, Y.4    She, M.5    Gu, D.6    Patterson, C.7    Li, H.8
  • 110
    • 67749099783 scopus 로고    scopus 로고
    • C terminus of Hsc70-interacting protein promotes smooth muscle cell proliferation and survival through ubiquitin-mediated degradation of FoxO1
    • Li F, Xie P, Fan Y, Zhang H, Zheng L, Gu D, Patterson C, Li H. C terminus of Hsc70-interacting protein promotes smooth muscle cell proliferation and survival through ubiquitin-mediated degradation of FoxO1. J Biol Chem. 2009;284:20090-20098.
    • (2009) J Biol Chem. , vol.284 , pp. 20090-20098
    • Li, F.1    Xie, P.2    Fan, Y.3    Zhang, H.4    Zheng, L.5    Gu, D.6    Patterson, C.7    Li, H.8
  • 111
    • 79451475816 scopus 로고    scopus 로고
    • Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiq-uitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice
    • Su H, Li J, Menon S, Liu J, Kumarapeli AR, Wei N, Wang X. Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiq-uitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice. Circ Res. 2011;108:40-50.
    • (2011) Circ Res. , vol.108 , pp. 40-50
    • Su, H.1    Li, J.2    Menon, S.3    Liu, J.4    Kumarapeli, A.R.5    Wei, N.6    Wang, X.7
  • 112
    • 80855148621 scopus 로고    scopus 로고
    • COP9 signalosome regulates autophagosome maturation
    • Su H, Li F, Ranek MJ, Wei N, Wang X. COP9 signalosome regulates autophagosome maturation. Circulation. 2011;124:2117-2128.
    • (2011) Circulation. , vol.124 , pp. 2117-2128
    • Su, H.1    Li, F.2    Ranek, M.J.3    Wei, N.4    Wang, X.5
  • 113
    • 33745050483 scopus 로고    scopus 로고
    • Altered S-phase kinase-associated protein-2 levels are a major mediator of cyclic nucleotide-in-duced inhibition of vascular smooth muscle cell proliferation
    • Wu YJ, Bond M, Sala-Newby GB, Newby AC. Altered S-phase kinase-associated protein-2 levels are a major mediator of cyclic nucleotide-in-duced inhibition of vascular smooth muscle cell proliferation. Circ Res. 2006;98:1141-1150.
    • (2006) Circ Res. , vol.98 , pp. 1141-1150
    • Wu, Y.J.1    Bond, M.2    Sala-Newby, G.B.3    Newby, A.C.4
  • 114
    • 9644281053 scopus 로고    scopus 로고
    • Down-regulation of p27Kip1 promotes cell proliferation of rat neonatal cardiomyocytes induced by nuclear expression of cyclin D1 and CDK4. Evidence for impaired Skp2-dependent degradation of p27 in terminal differentiation
    • Tamamori-Adachi M, Hayashida K, Nobori K, Omizu C, Yamada K, Sakamoto N, Kamura T, Fukuda K, Ogawa S, Nakayama KI, Kitajima S. Down-regulation of p27Kip1 promotes cell proliferation of rat neonatal cardiomyocytes induced by nuclear expression of cyclin D1 and CDK4. Evidence for impaired Skp2-dependent degradation of p27 in terminal differentiation. J Biol Chem. 2004;279:50429-50436.
    • (2004) J Biol Chem. , vol.279 , pp. 50429-50436
    • Tamamori-Adachi, M.1    Hayashida, K.2    Nobori, K.3    Omizu, C.4    Yamada, K.5    Sakamoto, N.6    Kamura, T.7    Fukuda, K.8    Ogawa, S.9    Nakayama, K.I.10    Kitajima, S.11
  • 116
    • 79955896887 scopus 로고    scopus 로고
    • P38 MAPK regulates G1-S transition in hypoxic cardiac fbroblasts
    • Pillai MS, Sapna S, Shivakumar K. p38 MAPK regulates G1-S transition in hypoxic cardiac fbroblasts. Int J Biochem Cell Biol. 2011;43:919-927.
    • (2011) Int J Biochem Cell Biol. , vol.43 , pp. 919-927
    • Pillai, M.S.1    Sapna, S.2    Shivakumar, K.3
  • 117
    • 34548164780 scopus 로고    scopus 로고
    • Notch signaling in vascular development and physiology
    • Gridley T. Notch signaling in vascular development and physiology. Development. 2007;134:2709-2718.
    • (2007) Development. , vol.134 , pp. 2709-2718
    • Gridley, T.1
  • 118
    • 0037080811 scopus 로고    scopus 로고
    • LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation
    • Nie J, McGill MA, Dermer M, Dho SE, Wolting CD, McGlade CJ. LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation. EMBO J. 2002;21:93-102.
    • (2002) EMBO J. , vol.21 , pp. 93-102
    • Nie, J.1    McGill, M.A.2    Dermer, M.3    Dho, S.E.4    Wolting, C.D.5    McGlade, C.J.6
  • 120
    • 1342275412 scopus 로고    scopus 로고
    • The ubiqui-tin ligase SCFFbw7 antagonizes apoptotic JNK signaling
    • Nateri AS, Riera-Sans L, Da Costa C, Behrens A. The ubiqui-tin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science. 2004;303:1374-1378.
    • (2004) Science. , vol.303 , pp. 1374-1378
    • Nateri, A.S.1    Riera-Sans, L.2    Da Costa, C.3    Behrens, A.4
  • 123
    • 50549100537 scopus 로고    scopus 로고
    • AIP4/Itch regulates Notch receptor degradation in the absence of ligand
    • Chastagner P, Israël A, Brou C. AIP4/Itch regulates Notch receptor degradation in the absence of ligand. PLoS ONE. 2008;3:e2735.
    • (2008) PLoS ONE. , vol.3
    • Chastagner, P.1    Israël, A.2    Brou, C.3
  • 124
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis RJ. A mammalian scaffold complex that selectively mediates MAP kinase activation. Science. 1998;281:1671-1674.
    • (1998) Science. , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavanagh, J.2    Tournier, C.3    Yasuda, J.4    Davis, R.J.5
  • 127
    • 0033959480 scopus 로고    scopus 로고
    • Regulation of the cardiac voltage-gated Na+ channel (H1) by the ubiquitin-protein ligase Nedd4
    • Abriel H, Kamynina E, Horisberger JD, Staub O. Regulation of the cardiac voltage-gated Na+ channel (H1) by the ubiquitin-protein ligase Nedd4. FEBS Lett. 2000;466:377-380.
    • (2000) FEBS Lett. , vol.466 , pp. 377-380
    • Abriel, H.1    Kamynina, E.2    Horisberger, J.D.3    Staub, O.4
  • 129
    • 79956326435 scopus 로고    scopus 로고
    • Nedd4-2-dependent ubiqui-tylation and regulation of the cardiac potassium channel hERG1
    • Albesa M, Grilo LS, Gavillet B, Abriel H. Nedd4-2-dependent ubiqui-tylation and regulation of the cardiac potassium channel hERG1. J Mol Cell Cardiol. 2011;51:90-98.
    • (2011) J Mol Cell Cardiol. , vol.51 , pp. 90-98
    • Albesa, M.1    Grilo, L.S.2    Gavillet, B.3    Abriel, H.4
  • 131
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • Semenza GL. Hypoxia-inducible factors in physiology and medicine. Cell. 2012;148:399-408.
    • (2012) Cell. , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 132
    • 33947520124 scopus 로고    scopus 로고
    • P53-induced inhibition of Hif-1 causes cardiac dysfunction during pressure overload
    • Sano M, Minamino T, Toko H, et al. p53-induced inhibition of Hif-1 causes cardiac dysfunction during pressure overload. Nature. 2007;446:444-448.
    • (2007) Nature. , vol.446 , pp. 444-448
    • Sano, M.1    Minamino, T.2    Toko, H.3
  • 135
    • 84864448811 scopus 로고    scopus 로고
    • Proteasome deubiquitinases as novel targets for cancer therapy
    • D'Arcy P, Linder S. Proteasome deubiquitinases as novel targets for cancer therapy. Int J Biochem Cell Biol. 2012;44:1729-1738.
    • (2012) Int J Biochem Cell Biol. , vol.44 , pp. 1729-1738
    • D'Arcy, P.1    Linder, S.2
  • 138
    • 40449122286 scopus 로고    scopus 로고
    • Protein kinase CK2 links extracellular growth factor signaling with the control of p27(Kip1) stability in the heart
    • Hauck L, Harms C, An J, Rohne J, Gertz K, Dietz R, Endres M, von Harsdorf R. Protein kinase CK2 links extracellular growth factor signaling with the control of p27(Kip1) stability in the heart. Nat Med. 2008;14:315-324.
    • (2008) Nat Med. , vol.14 , pp. 315-324
    • Hauck, L.1    Harms, C.2    An, J.3    Rohne, J.4    Gertz, K.5    Dietz, R.6    Endres, M.7    Von Harsdorf, R.8
  • 139
    • 84861355524 scopus 로고    scopus 로고
    • Post-myocardial infarct p27 fusion protein intravenous delivery averts adverse remodelling and improves heart function and survival in rodents
    • Konecny F, Zou J, Husain M, von Harsdorf R. Post-myocardial infarct p27 fusion protein intravenous delivery averts adverse remodelling and improves heart function and survival in rodents. Cardiovasc Res. 2012;94:492-500.
    • (2012) Cardiovasc Res. , vol.94 , pp. 492-500
    • Konecny, F.1    Zou, J.2    Husain, M.3    Von Harsdorf, R.4
  • 141
    • 0029761411 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding a human ubiquitin-conjugat-ing enzyme similar to the Drosophila bendless gene product
    • Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S. Cloning and expression of cDNA encoding a human ubiquitin-conjugat-ing enzyme similar to the Drosophila bendless gene product. J Biochem. 1996;120:494-497.
    • (1996) J Biochem. , vol.120 , pp. 494-497
    • Yamaguchi, T.1    Kim, N.S.2    Sekine, S.3    Seino, H.4    Osaka, F.5    Yamao, F.6    Kato, S.7
  • 144
    • 0032127179 scopus 로고    scopus 로고
    • Identifcation, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene
    • Katsanis N, Fisher EM. Identifcation, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene. Genomics. 1998;51:128-131.
    • (1998) Genomics. , vol.51 , pp. 128-131
    • Katsanis, N.1    Fisher, E.M.2
  • 145
    • 65549097264 scopus 로고    scopus 로고
    • Atrogin-1/MAFbx enhances simulated ischemia/reperfusion-induced apoptosis in cardiomyocytes through degradation of MAPK phosphatase-1 and sustained JNK activation
    • Xie P, Guo S, Fan Y, Zhang H, Gu D, Li H. Atrogin-1/MAFbx enhances simulated ischemia/reperfusion-induced apoptosis in cardiomyocytes through degradation of MAPK phosphatase-1 and sustained JNK activation. J Biol Chem. 2009;284:5488-5496.
    • (2009) J Biol Chem. , vol.284 , pp. 5488-5496
    • Xie, P.1    Guo, S.2    Fan, Y.3    Zhang, H.4    Gu, D.5    Li, H.6
  • 146
    • 84875976019 scopus 로고    scopus 로고
    • The Roles of VHL-Dependent Ubiquitination in Signaling and Cancer
    • Zhang Q, Yang H. The Roles of VHL-Dependent Ubiquitination in Signaling and Cancer. Front Oncol. 2012;2:35.
    • (2012) Front Oncol. , vol.2 , pp. 35
    • Zhang, Q.1    Yang, H.2
  • 147
    • 28144439277 scopus 로고    scopus 로고
    • CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha
    • Fan M, Park A, Nephew KP. CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha. Mol Endocrinol. 2005;19: 2901-2914.
    • (2005) Mol Endocrinol. , vol.19 , pp. 2901-2914
    • Fan, M.1    Park, A.2    Nephew, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.