메뉴 건너뛰기




Volumn 44, Issue 2, 2008, Pages 419-428

Oxidative injury induces selective rather than global inhibition of proteasomal activity

Author keywords

I B; Ischemia reperfusion; Myoblast; Nrf2; Proteasome

Indexed keywords

EPOXOMICIN; GLUCOSE REGULATED PROTEIN 78; I KAPPA B; KELCH LIKE ECH ASSOCIATED PROTEIN 1; LACTACYSTIN; PROTEASOME; TRANSCRIPTION FACTOR NRF2;

EID: 39149124870     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2007.10.005     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0037785185 scopus 로고    scopus 로고
    • Cardiovascular disease
    • Nabel E.G. Cardiovascular disease. N Engl J Med 349 (2003) 60-72
    • (2003) N Engl J Med , vol.349 , pp. 60-72
    • Nabel, E.G.1
  • 2
    • 3342971030 scopus 로고    scopus 로고
    • Myocardial protection at a crossroads: the need for translation into clinical therapy
    • Bolli R., Becker L., Gross G., Mentzer Jr. R., Balshaw D., and Lathrop D.A. Myocardial protection at a crossroads: the need for translation into clinical therapy. Circ Res 95 (2004) 125-134
    • (2004) Circ Res , vol.95 , pp. 125-134
    • Bolli, R.1    Becker, L.2    Gross, G.3    Mentzer Jr., R.4    Balshaw, D.5    Lathrop, D.A.6
  • 3
    • 0036789917 scopus 로고    scopus 로고
    • Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3
    • Kubasiak L.A., Hernandez O.M., Bishopric N.H., and Webster K.A. Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3. Proc Natl Acad Sci U S A 99 (2002) 12825-12830
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12825-12830
    • Kubasiak, L.A.1    Hernandez, O.M.2    Bishopric, N.H.3    Webster, K.A.4
  • 4
    • 33644850965 scopus 로고    scopus 로고
    • Depletion of cardiolipin and cytochrome c during ischemia increases hydrogen peroxide production from the electron transport chain
    • Chen Q., and Lesnefsky E.J. Depletion of cardiolipin and cytochrome c during ischemia increases hydrogen peroxide production from the electron transport chain. Free Radic Biol Med 40 (2006) 976-982
    • (2006) Free Radic Biol Med , vol.40 , pp. 976-982
    • Chen, Q.1    Lesnefsky, E.J.2
  • 5
    • 28244444075 scopus 로고    scopus 로고
    • Mitochondrial dysfunction associated with cardiac ischemia/reperfusion can be attenuated by oxygen tension control. Role of oxygen-free radicals and cardiolipin
    • Petrosillo G., Di Venosa N., Ruggiero F.M., Pistolese M., D'Agostino D., Tiravanti E., et al. Mitochondrial dysfunction associated with cardiac ischemia/reperfusion can be attenuated by oxygen tension control. Role of oxygen-free radicals and cardiolipin. Biochim Biophys Acta 1710 (2005) 78-86
    • (2005) Biochim Biophys Acta , vol.1710 , pp. 78-86
    • Petrosillo, G.1    Di Venosa, N.2    Ruggiero, F.M.3    Pistolese, M.4    D'Agostino, D.5    Tiravanti, E.6
  • 6
    • 1942520360 scopus 로고    scopus 로고
    • Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping
    • Mason R.P. Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping. Free Radic Biol Med 36 (2004) 1214-1223
    • (2004) Free Radic Biol Med , vol.36 , pp. 1214-1223
    • Mason, R.P.1
  • 7
    • 33646679144 scopus 로고    scopus 로고
    • Overexpression of mitochondrial peroxiredoxin-3 prevents left ventricular remodeling and failure after myocardial infarction in mice
    • Matsushima S., Ide T., Yamato M., Matsusaka H., Hattori F., Ikeuchi M., et al. Overexpression of mitochondrial peroxiredoxin-3 prevents left ventricular remodeling and failure after myocardial infarction in mice. Circulation 113 (2006) 1779-1786
    • (2006) Circulation , vol.113 , pp. 1779-1786
    • Matsushima, S.1    Ide, T.2    Yamato, M.3    Matsusaka, H.4    Hattori, F.5    Ikeuchi, M.6
  • 8
    • 0037176994 scopus 로고    scopus 로고
    • Postischemic recovery of contractile function is impaired in SOD2(+/-) but not SOD1(+/-) mouse hearts
    • Asimakis G.K., Lick S., and Patterson C. Postischemic recovery of contractile function is impaired in SOD2(+/-) but not SOD1(+/-) mouse hearts. Circulation 105 (2002) 981-986
    • (2002) Circulation , vol.105 , pp. 981-986
    • Asimakis, G.K.1    Lick, S.2    Patterson, C.3
  • 9
    • 0344925103 scopus 로고    scopus 로고
    • Preconditioning potentiates redox signaling and converts death signal into survival signal
    • Das D.K., and Maulik N. Preconditioning potentiates redox signaling and converts death signal into survival signal. Arch Biochem Biophys 420 (2003) 305-311
    • (2003) Arch Biochem Biophys , vol.420 , pp. 305-311
    • Das, D.K.1    Maulik, N.2
  • 10
    • 0035980171 scopus 로고    scopus 로고
    • Reactive oxygen species mediate amplitude-dependent hypertrophic and apoptotic responses to mechanical stretch in cardiac myocytes
    • Pimentel D.R., Amin J.K., Xiao L., Miller T., Viereck J., Oliver-Krasinski J., et al. Reactive oxygen species mediate amplitude-dependent hypertrophic and apoptotic responses to mechanical stretch in cardiac myocytes. Circ Res 89 (2001) 453-460
    • (2001) Circ Res , vol.89 , pp. 453-460
    • Pimentel, D.R.1    Amin, J.K.2    Xiao, L.3    Miller, T.4    Viereck, J.5    Oliver-Krasinski, J.6
  • 11
    • 33745862737 scopus 로고    scopus 로고
    • An assessment of the role of reactive oxygen species and redox signaling in norepinephrine-induced apoptosis and hypertrophy of H9c2 cardiac myoblasts
    • Gupta M.K., Neelakantan T.V., Sanghamitra M., Tyagi R.K., Dinda A., and Maulik S. An assessment of the role of reactive oxygen species and redox signaling in norepinephrine-induced apoptosis and hypertrophy of H9c2 cardiac myoblasts. Antioxid Redox Signal 8 (2006) 1081-1093
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1081-1093
    • Gupta, M.K.1    Neelakantan, T.V.2    Sanghamitra, M.3    Tyagi, R.K.4    Dinda, A.5    Maulik, S.6
  • 12
    • 0345258505 scopus 로고    scopus 로고
    • Oxidative stress-induced signal transduction pathways in cardiac myocytes: involvement of ROS in heart diseases
    • Takano H., Zou Y., Hasegawa H., Akazawa H., Nagai T., and Komuro I. Oxidative stress-induced signal transduction pathways in cardiac myocytes: involvement of ROS in heart diseases. Antioxid Redox Signal 5 (2003) 789-794
    • (2003) Antioxid Redox Signal , vol.5 , pp. 789-794
    • Takano, H.1    Zou, Y.2    Hasegawa, H.3    Akazawa, H.4    Nagai, T.5    Komuro, I.6
  • 13
    • 33947623122 scopus 로고    scopus 로고
    • Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes
    • Kuster G.M., Siwik D.A., Pimentel D.R., and Colucci W.S. Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes. Antioxid Redox Signal 8 (2006) 2153-2159
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2153-2159
    • Kuster, G.M.1    Siwik, D.A.2    Pimentel, D.R.3    Colucci, W.S.4
  • 14
    • 34249827861 scopus 로고    scopus 로고
    • Oxidized proteins: intracellular distribution and recognition by the proteasome
    • Jung T., Bader N., and Grune T. Oxidized proteins: intracellular distribution and recognition by the proteasome. Arch Biochem Biophys 462 (2007) 231-237
    • (2007) Arch Biochem Biophys , vol.462 , pp. 231-237
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 15
    • 33745726659 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiac physiology and pathology
    • Powell S.R. The ubiquitin-proteasome system in cardiac physiology and pathology. Am J Physiol Heart Circ Physiol 291 (2006) H1-H19
    • (2006) Am J Physiol Heart Circ Physiol , vol.291
    • Powell, S.R.1
  • 16
    • 17644375852 scopus 로고    scopus 로고
    • Oxidized and ubiquitinated proteins may predict recovery of postischemic cardiac function: essential role of the proteasome
    • Powell S.R., Wang P., Katzeff H., Shringarpure R., Teoh C., Khaliulin I., et al. Oxidized and ubiquitinated proteins may predict recovery of postischemic cardiac function: essential role of the proteasome. Antioxid Redox Signal 7 (2005) 538-546
    • (2005) Antioxid Redox Signal , vol.7 , pp. 538-546
    • Powell, S.R.1    Wang, P.2    Katzeff, H.3    Shringarpure, R.4    Teoh, C.5    Khaliulin, I.6
  • 17
    • 33750023437 scopus 로고    scopus 로고
    • Keeping transcriptional activators under control
    • Kodadek T., Sikder D., and Nalley K. Keeping transcriptional activators under control. Cell 127 (2006) 261-264
    • (2006) Cell , vol.127 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 18
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome
    • Ishii T., Sakurai T., Usami H., and Uchida K. Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry 44 (2005) 13893-13901
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 19
    • 21644442676 scopus 로고    scopus 로고
    • Cardioprotection with palm tocotrienol: antioxidant activity of tocotrienol is linked with its ability to stabilize proteasomes
    • Das S., Powell S.R., Wang P., Divald A., Nesaretnam K., Tosaki A., et al. Cardioprotection with palm tocotrienol: antioxidant activity of tocotrienol is linked with its ability to stabilize proteasomes. Am J Physiol Heart Circ Physiol 289 (2005) H361-H367
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Das, S.1    Powell, S.R.2    Wang, P.3    Divald, A.4    Nesaretnam, K.5    Tosaki, A.6
  • 20
    • 27144478935 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome system in ER quality control
    • Ye Y. The role of the ubiquitin-proteasome system in ER quality control. Essays Biochem 41 (2005) 99-112
    • (2005) Essays Biochem , vol.41 , pp. 99-112
    • Ye, Y.1
  • 22
    • 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 J.J., Fernandez R., Thuerauf D., Whittaker R., Gude N., Sussman M.A., et al. 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 98 (2006) 1186-1193
    • (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
  • 23
    • 33748557190 scopus 로고    scopus 로고
    • Regulating the regulator: NF-kappaB signaling in heart
    • Hall G., Hasday J.D., and Rogers T.B. Regulating the regulator: NF-kappaB signaling in heart. J Mol Cell Cardiol 41 (2006) 580-591
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 580-591
    • Hall, G.1    Hasday, J.D.2    Rogers, T.B.3
  • 24
    • 0037440199 scopus 로고    scopus 로고
    • Regulation of nuclear translocation of nuclear factor-kappaB relA: evidence for complex dynamics at the single-cell level
    • Schooley K., Zhu P., Dower S.K., and Qwarnstrom E.E. Regulation of nuclear translocation of nuclear factor-kappaB relA: evidence for complex dynamics at the single-cell level. Biochem J 369 (2003) 331-339
    • (2003) Biochem J , vol.369 , pp. 331-339
    • Schooley, K.1    Zhu, P.2    Dower, S.K.3    Qwarnstrom, E.E.4
  • 26
    • 33845681986 scopus 로고    scopus 로고
    • Free radical scavenging inhibits STAT phosphorylation following in vivo ischemia/reperfusion injury
    • McCormick J., Barry S.P., Sivarajah A., Stefanutti G., Townsend P.A., Lawrence K.M., et al. Free radical scavenging inhibits STAT phosphorylation following in vivo ischemia/reperfusion injury. FASEB J 20 (2006) 2115-2117
    • (2006) FASEB J , vol.20 , pp. 2115-2117
    • McCormick, J.1    Barry, S.P.2    Sivarajah, A.3    Stefanutti, G.4    Townsend, P.A.5    Lawrence, K.M.6
  • 27
    • 33845759389 scopus 로고    scopus 로고
    • Induction of antioxidant and detoxification response by oxidants in cardiomyocytes: evidence from gene expression profiling and activation of Nrf2 transcription factor
    • Purdom-Dickinson S.E., Lin Y., Dedek M., Morrissy S., Johnson J., and Chen Q.M. Induction of antioxidant and detoxification response by oxidants in cardiomyocytes: evidence from gene expression profiling and activation of Nrf2 transcription factor. J Mol Cell Cardiol 42 (2007) 159-176
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 159-176
    • Purdom-Dickinson, S.E.1    Lin, Y.2    Dedek, M.3    Morrissy, S.4    Johnson, J.5    Chen, Q.M.6
  • 28
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi A., Kang M.I., Watai Y., Tong K.I., Shibata T., Uchida K., et al. Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol Cell Biol 26 (2006) 221-229
    • (2006) Mol Cell Biol , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3    Tong, K.I.4    Shibata, T.5    Uchida, K.6
  • 29
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., and Hannink M. Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J Biol Chem 280 (2005) 30091-30099
    • (2005) J Biol Chem , vol.280 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.C.2    Sun, Z.3    Habib, G.M.4    Lieberman, M.W.5    Hannink, M.6
  • 30
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • Kisselev A.F., Callard A., and Goldberg A.L. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J Biol Chem 281 (2006) 8582-8590
    • (2006) J Biol Chem , vol.281 , pp. 8582-8590
    • Kisselev, A.F.1    Callard, A.2    Goldberg, A.L.3
  • 31
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • Myung J., Kim K.B., Lindsten K., Dantuma N.P., and Crews C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol Cell 7 (2001) 411-420
    • (2001) Mol Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 32
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci U S A 96 (1999) 10403-10408
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 33
    • 17644444479 scopus 로고    scopus 로고
    • Separation of cathepsin A-like enzyme and the proteasome: evidence that lactacystin/beta-lactone is not a specific inhibitor of the proteasome
    • Ostrowska H., Wojcik C., Wilk S., Omura S., Kozlowski L., Stoklosa T., et al. Separation of cathepsin A-like enzyme and the proteasome: evidence that lactacystin/beta-lactone is not a specific inhibitor of the proteasome. Int J Biochem Cell Biol 32 (2000) 747-757
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 747-757
    • Ostrowska, H.1    Wojcik, C.2    Wilk, S.3    Omura, S.4    Kozlowski, L.5    Stoklosa, T.6
  • 34
    • 0033548055 scopus 로고    scopus 로고
    • A giant protease with potential to substitute for some functions of the proteasome
    • Geier E., Pfeifer G., Wilm M., Lucchiari-Hartz M., Baumeister W., Eichmann K., et al. A giant protease with potential to substitute for some functions of the proteasome. Science 283 (1999) 978-981
    • (1999) Science , vol.283 , pp. 978-981
    • Geier, E.1    Pfeifer, G.2    Wilm, M.3    Lucchiari-Hartz, M.4    Baumeister, W.5    Eichmann, K.6
  • 35
    • 33750443289 scopus 로고    scopus 로고
    • IkappaB kinase complexes: gateways to NF-kappaB activation and transcription
    • Scheidereit C. IkappaB kinase complexes: gateways to NF-kappaB activation and transcription. Oncogene 25 (2006) 6685-6705
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 36
    • 0033066832 scopus 로고    scopus 로고
    • Differential regulation of Bcl-2, AP-1 and NF-kappaB on cardiomyocyte apoptosis during myocardial ischemic stress adaptation
    • Maulik N., Goswami S., Galang N., and Das D.K. Differential regulation of Bcl-2, AP-1 and NF-kappaB on cardiomyocyte apoptosis during myocardial ischemic stress adaptation. FEBS Lett 443 (1999) 331-336
    • (1999) FEBS Lett , vol.443 , pp. 331-336
    • Maulik, N.1    Goswami, S.2    Galang, N.3    Das, D.K.4
  • 37
    • 34547137901 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide diminishes NF-{kappa}B activation, I{kappa}B-{alpha} degradation, and proteasome activity in neutrophils
    • Zmijewski J.W., Zhao X., Xu Z., and Abraham E. Exposure to hydrogen peroxide diminishes NF-{kappa}B activation, I{kappa}B-{alpha} degradation, and proteasome activity in neutrophils. Am J Physiol Cell Physiol 293 (2007) C255-C266
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Zmijewski, J.W.1    Zhao, X.2    Xu, Z.3    Abraham, E.4
  • 38
    • 24044488987 scopus 로고    scopus 로고
    • Mechanism of direct degradation of IkappaBalpha by 20S proteasome
    • Alvarez-Castelao B., and Castano J.G. Mechanism of direct degradation of IkappaBalpha by 20S proteasome. FEBS Lett 579 (2005) 4797-4802
    • (2005) FEBS Lett , vol.579 , pp. 4797-4802
    • Alvarez-Castelao, B.1    Castano, J.G.2
  • 39
    • 19544367587 scopus 로고    scopus 로고
    • Evidence for a phosphorylation-independent role for Ser 32 and 36 in proteasome inhibitor-resistant (PIR) IkappaBalpha degradation in B cells
    • O'Connor S., Markovina S., and Miyamoto S. Evidence for a phosphorylation-independent role for Ser 32 and 36 in proteasome inhibitor-resistant (PIR) IkappaBalpha degradation in B cells. Exp Cell Res 307 (2005) 15-25
    • (2005) Exp Cell Res , vol.307 , pp. 15-25
    • O'Connor, S.1    Markovina, S.2    Miyamoto, S.3
  • 40
    • 4544326748 scopus 로고    scopus 로고
    • An evolutionary conserved pathway of nuclear factor-kappaB activation involving caspase-mediated cleavage and N-end rule pathway-mediated degradation of IkappaBalpha
    • Rathore N., Matta H., and Chaudhary P.M. An evolutionary conserved pathway of nuclear factor-kappaB activation involving caspase-mediated cleavage and N-end rule pathway-mediated degradation of IkappaBalpha. J Biol Chem 279 (2004) 39358-39365
    • (2004) J Biol Chem , vol.279 , pp. 39358-39365
    • Rathore, N.1    Matta, H.2    Chaudhary, P.M.3
  • 41
    • 0242664121 scopus 로고    scopus 로고
    • IkappaB kinase-independent IkappaBalpha degradation pathway: functional NF-kappaB activity and implications for cancer therapy
    • Tergaonkar V., Bottero V., Ikawa M., Li Q., and Verma I.M. IkappaB kinase-independent IkappaBalpha degradation pathway: functional NF-kappaB activity and implications for cancer therapy. Mol Cell Biol 23 (2003) 8070-8083
    • (2003) Mol Cell Biol , vol.23 , pp. 8070-8083
    • Tergaonkar, V.1    Bottero, V.2    Ikawa, M.3    Li, Q.4    Verma, I.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.