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Volumn 15, Issue 10, 2010, Pages 1270-1283

Synergistic induction of apoptosis and caspase-independent autophagic cell death by a combination of nitroxide Tempo and heat shock in human leukemia U937 cells

Author keywords

Apoptosis; Autophagy; Heat stress; Necrosis; Tempo

Indexed keywords

3 METHYLADENINE; BECLIN 1; CALCIUM ION; CASPASE; CASPASE 2; CASPASE 3; CASPASE 8; CASPASE 9; CYCLOPHILIN D; CYCLOSPORIN A; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; NITROXIDE; PROPIDIUM IODIDE; PROTEIN BAX; PROTEIN BCL 2; RUTHENIUM RED; SUPEROXIDE; TEMPO; UNCLASSIFIED DRUG;

EID: 78650054032     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-010-0522-8     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev A, Yuan J (2008) Expansion and evolution of cell death programmes. Nat Rev Mol Cell Biol 9:378-390
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 378-390
    • Degterev, A.1    Yuan, J.2
  • 2
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis SN, Chen L, Dewson G et al (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19:1294-1305
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3
  • 3
    • 70449091753 scopus 로고    scopus 로고
    • Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis
    • Kim H, Tu HC, Ren D et al (2009) Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. Mol Cell 36:487-499
    • (2009) Mol Cell , vol.36 , pp. 487-499
    • Kim, H.1    Tu, H.C.2    Ren, D.3
  • 4
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9:47-59
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 5
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94:491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 6
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways
    • McStay GP, Salvesen GS, Green DR (2008) Overlapping cleavage motif selectivity of caspases: implications for analysis of apoptotic pathways. Cell Death Differ 15:322-331
    • (2008) Cell Death Differ , vol.15 , pp. 322-331
    • McStay, G.P.1    Salvesen, G.S.2    Green, D.R.3
  • 7
    • 47749089820 scopus 로고    scopus 로고
    • Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
    • Schütze S, Tchikov V, Schneider-Brachert W (2008) Regulation of TNFR1 and CD95 signalling by receptor compartmentalization. Nat Rev Mol Cell Biol 9:655-662
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 655-662
    • Schütze, S.1    Tchikov, V.2    Schneider-Brachert, W.3
  • 9
    • 29144463145 scopus 로고    scopus 로고
    • The multidomain proapoptotic molecules Bax and Bak are directly activated by heat
    • Pagliari LJ, Kuwana T, Bonzon C et al (2005) The multidomain proapoptotic molecules Bax and Bak are directly activated by heat. Proc Natl Acad Sci USA 102:17975-17980
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17975-17980
    • Pagliari, L.J.1    Kuwana, T.2    Bonzon, C.3
  • 10
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • Tu S, McStay GP, Boucher LM, Mak T, Beere HM, Green DR (2006) In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat Cell Biol 8:72-77
    • (2006) Nat Cell Biol , vol.8 , pp. 72-77
    • Tu, S.1    McStay, G.P.2    Boucher, L.M.3    Mak, T.4    Beere, H.M.5    Green, D.R.6
  • 11
    • 0036024020 scopus 로고    scopus 로고
    • Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9
    • O'Reilly LA, Ekert P, Harvey N et al
    • O'Reilly LA, Ekert P, Harvey N et al (2002) Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9. Cell Death Differ 9:832-841
    • (2002) Cell Death Differ , vol.9 , pp. 832-841
  • 12
    • 33846053961 scopus 로고    scopus 로고
    • Loss of caspase-9 reveals its essential role for caspase-2 activation and mitochondrial membrane depolarization
    • Samraj AK, Sohn D, Schulze-Osthoff K, Schmitz I (2007) Loss of caspase-9 reveals its essential role for caspase-2 activation and mitochondrial membrane depolarization. Mol Biol Cell 18:84-93
    • (2007) Mol Biol Cell , vol.18 , pp. 84-93
    • Samraj, A.K.1    Sohn, D.2    Schulze-Osthoff, K.3    Schmitz, I.4
  • 14
    • 33745739717 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis requires bid cleavage: A physiological role for bid in heat shock-induced death
    • Bonzon C, Bouchier-Hayes L, Pagliari LJ, Green DR, Newmeyer DD (2006) Caspase-2-induced apoptosis requires bid cleavage: a physiological role for bid in heat shock-induced death. Mol Biol Cell 17:2150-2157
    • (2006) Mol Biol Cell , vol.17 , pp. 2150-2157
    • Bonzon, C.1    Bouchier-Hayes, L.2    Pagliari, L.J.3    Green, D.R.4    Newmeyer, D.D.5
  • 15
    • 0034647691 scopus 로고    scopus 로고
    • Pivotal role of reactive oxygen species as intracellular mediators of hyperthermia-induced apoptosis
    • Katschinski DM, Boos K, Schindler SG, Fandrey J (2000) Pivotal role of reactive oxygen species as intracellular mediators of hyperthermia-induced apoptosis. J Biol Chem 275:21094-21098
    • (2000) J Biol Chem , vol.275 , pp. 21094-21098
    • Katschinski, D.M.1    Boos, K.2    Schindler, S.G.3    Fandrey, J.4
  • 16
    • 33644895407 scopus 로고    scopus 로고
    • Mechanism of cell death induction by nitroxide and hyperthermia
    • Zhao Q-L, Fujiwara Y, Kondo T (2006) Mechanism of cell death induction by nitroxide and hyperthermia. Free Radic Biol Med 40:1131-1143
    • (2006) Free Radic Biol Med , vol.40 , pp. 1131-1143
    • Zhao, Q.-L.1    Fujiwara, Y.2    Kondo, T.3
  • 17
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • Leung AW, Varanyuwatana P, Halestrap AP (2008) The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition. J Biol Chem 283:26312-26323
    • (2008) J Biol Chem , vol.283 , pp. 26312-26323
    • Leung, A.W.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 18
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, Kaiser RA, Purcell NH et al (2005) Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434:658-662
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 19
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T et al (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434:652-658
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3
  • 20
    • 0034042319 scopus 로고    scopus 로고
    • The pro-oxidative activity of SOD and nitroxide SOD mimics
    • Offer T, Russo A, Samuni A (2000) The pro-oxidative activity of SOD and nitroxide SOD mimics. FASEB J 14:1215-1223
    • (2000) FASEB J , vol.14 , pp. 1215-1223
    • Offer, T.1    Russo, A.2    Samuni, A.3
  • 21
    • 34247248969 scopus 로고    scopus 로고
    • The chemistry and biology of nitroxide compounds
    • Soule BP, Hyodo F, Matsumoto K et al (2007) The chemistry and biology of nitroxide compounds. Free Radic Biol Med 42:1632-1650
    • (2007) Free Radic Biol Med , vol.42 , pp. 1632-1650
    • Soule, B.P.1    Hyodo, F.2    Matsumoto, K.3
  • 23
    • 0026731503 scopus 로고
    • Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical
    • Voest EE, van Faassen E, van Asbeck BS, Neijt JP, Marx JJ (1992) Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical.Biochim Biophys Acta 1136:113-118
    • (1992) Biochim Biophys Acta , vol.1136 , pp. 113-118
    • Voest, E.E.1    Van Faassen, E.2    Van Asbeck, B.S.3    Neijt, J.P.4    Marx, J.J.5
  • 24
    • 14744268278 scopus 로고    scopus 로고
    • Nitroxide tempo, a small molecule, induces apoptosis in prostate carcinoma cells and suppresses tumor growth in athymic mice
    • Suy S, Mitchell JB, Samuni A, Mueller S, Kasid U (2005) Nitroxide tempo, a small molecule, induces apoptosis in prostate carcinoma cells and suppresses tumor growth in athymic mice. Cancer 103:1302-1313
    • (2005) Cancer , vol.103 , pp. 1302-1313
    • Suy, S.1    Mitchell, J.B.2    Samuni, A.3    Mueller, S.4    Kasid, U.5
  • 25
    • 2942581328 scopus 로고    scopus 로고
    • Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex i of the electron transport chain
    • Ricci JE, Munoz-Pinedo C, Fitzgerald P et al (2004) Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. Cell 117:773-786
    • (2004) Cell , vol.117 , pp. 773-786
    • Ricci, J.E.1    Munoz-Pinedo, C.2    Fitzgerald, P.3
  • 26
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T et al (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19:5720-5728
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3
  • 27
    • 0033021780 scopus 로고    scopus 로고
    • Transient and longlasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • Petronilli V, Miotto G, Canton M et al (1999) Transient and longlasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophys J 76:725-734
    • (1999) Biophys J , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3
  • 28
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM (1997) Caspases: the executioners of apoptosis. Biochem J 326(Pt 1):1-16
    • (1997) Biochem J , vol.326 , Issue.PART. 1 , pp. 1-16
    • Cohen, G.M.1
  • 29
    • 2342592537 scopus 로고    scopus 로고
    • Fas-disabling small exocyclic peptide mimetics limit apoptosis by an unexpected mechanism
    • Hasegawa A, Cheng X, Kajino K et al (2004) Fas-disabling small exocyclic peptide mimetics limit apoptosis by an unexpected mechanism. Proc Natl Acad Sci USA 101:6599-6604
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6599-6604
    • Hasegawa, A.1    Cheng, X.2    Kajino, K.3
  • 30
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk R, Israelson A, Garty ES, Azoulay-Zohar H, Shoshan-Barmatz V (2005) Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem J 386:73-83
    • (2005) Biochem J , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 31
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y, Krapivinsky G, Clapham DE (2004) The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427:360-364
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 33
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxiainduced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot G, Garcia-Medina R, Gounon P et al (2009) Hypoxiainduced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol Cell Biol 29:2570-2581
    • (2009) Mol Cell Biol , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3
  • 34
    • 0033942613 scopus 로고    scopus 로고
    • BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore
    • Vande Velde C, Cizeau J, Dubik D et al (2000) BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore. Mol Cell Biol 20:5454-5468
    • (2000) Mol Cell Biol , vol.20 , pp. 5454-5468
    • Vande Velde, C.1    Cizeau, J.2    Dubik, D.3
  • 35
    • 34248998801 scopus 로고    scopus 로고
    • Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1
    • Maiuri MC, Le Toumelin G, Criollo A et al (2007) Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1. EMBO J 26:2527-2539
    • (2007) EMBO J , vol.26 , pp. 2527-2539
    • Maiuri, M.C.1    Le Toumelin, G.2    Criollo, A.3
  • 36
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum JJ, Bauer DE, Kong M et al (2005) Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 120:237-248
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3
  • 37
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev A, Huang Z, Boyce M et al (2005) Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 1:112-119
    • (2005) Nat Chem Biol , vol.1 , pp. 112-119
    • Degterev, A.1    Huang, Z.2    Boyce, M.3
  • 39
    • 34249279169 scopus 로고    scopus 로고
    • GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation
    • Colell A, Ricci JE, Tait S et al (2007) GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation. Cell 129:983-997
    • (2007) Cell , vol.129 , pp. 983-997
    • Colell, A.1    Ricci, J.E.2    Tait, S.3
  • 40
    • 33846189759 scopus 로고    scopus 로고
    • Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2
    • Høyer-Hansen M, Bastholm L, Szyniarowski P et al (2007) Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2. Mol Cell 25:193-205
    • (2007) Mol Cell , vol.25 , pp. 193-205
    • Høyer-Hansen, M.1    Bastholm, L.2    Szyniarowski, P.3
  • 41
    • 0035877605 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3
    • Paroni G, Henderson C, Schneider C, Brancolini C (2001) Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3. J Biol Chem 276:21907-21915
    • (2001) J Biol Chem , vol.276 , pp. 21907-21915
    • Paroni, G.1    Henderson, C.2    Schneider, C.3    Brancolini, C.4
  • 42
    • 49349112331 scopus 로고    scopus 로고
    • Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization
    • Yamaguchi R, Lartigue L, Perkins G et al (2008) Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization. Mol Cell 31:557-569
    • (2008) Mol Cell , vol.31 , pp. 557-569
    • Yamaguchi, R.1    Lartigue, L.2    Perkins, G.3


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