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Volumn 1847, Issue 2, 2015, Pages 231-240

Spermine selectively inhibits high-conductance, but not low-conductance calcium-induced permeability transition pore

Author keywords

Calcium; Mitochondrial permeability transition pore; Spermine

Indexed keywords

CALCIUM; CYCLOSPORIN A; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; SPERMINE; CARRIER PROTEIN;

EID: 84911904718     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.10.007     Document Type: Article
Times cited : (18)

References (56)
  • 4
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • C.P. Baines, R.A. Kaiser, T. Sheiko, W.J. Craigen, and J.D. Molkentin Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 9 2007 550 555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 5
    • 84883776628 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: A mystery solved?
    • P. Bernardi The mitochondrial permeability transition pore: a mystery solved? Front. Physiol. 4 2013 95
    • (2013) Front. Physiol. , vol.4 , pp. 95
    • Bernardi, P.1
  • 6
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore: A cyclosporin-sensitive pore in the inner mitochondrial membrane
    • P. Bernardi, K.M. Broekemeier, and D.R. Pfeiffer Recent progress on regulation of the mitochondrial permeability transition pore: a cyclosporin-sensitive pore in the inner mitochondrial membrane J. Bioenerg. Biomembr. 26 1994 509 517
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 7
    • 85000114986 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: Molecular nature and role as a target in cardioprotection
    • (in press)
    • P. Bernardi, and L.F. Di The mitochondrial permeability transition pore: molecular nature and role as a target in cardioprotection J. Mol. Cell. Cardiol. 2014 10.1016/j.yjmcc.2014.08.01 (in press)
    • (2014) J. Mol. Cell. Cardiol.
    • Bernardi, P.1    Di, L.F.2
  • 9
    • 84863206432 scopus 로고    scopus 로고
    • (2 +) release channel: New answers to an old question
    • (2 +) release channel: new answers to an old question Cell Calcium 52 2012 22 27
    • (2012) Cell Calcium , vol.52 , pp. 22-27
    • Bernardi, P.1    Von, S.S.2
  • 10
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 29 2000 222 230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 11
    • 85047687351 scopus 로고    scopus 로고
    • Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition
    • M. Carraro, V. Giorgio, J. Sileikyte, G. Sartori, M. Forte, G. Lippe, M. Zoratti, I. Szabo, and P. Bernardi Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition J. Biol. Chem. 289 23 2014 15980 15985
    • (2014) J. Biol. Chem. , vol.289 , Issue.23 , pp. 15980-15985
    • Carraro, M.1    Giorgio, V.2    Sileikyte, J.3    Sartori, G.4    Forte, M.5    Lippe, G.6    Zoratti, M.7    Szabo, I.8    Bernardi, P.9
  • 12
    • 84906254466 scopus 로고    scopus 로고
    • What makes you can also break you, part III: Mitochondrial permeability transition pore formation by an uncoupling channel within the C-subunit ring of the F1FO ATP synthase?
    • C. Chinopoulos, and G. Szabadkai What makes you can also break you, part III: mitochondrial permeability transition pore formation by an uncoupling channel within the C-subunit ring of the F1FO ATP synthase? Front. Oncol. 4 2014 235
    • (2014) Front. Oncol. , vol.4 , pp. 235
    • Chinopoulos, C.1    Szabadkai, G.2
  • 13
    • 84884519026 scopus 로고    scopus 로고
    • Polyhydroxybutyrate targets mammalian mitochondria and increases permeability of plasmalemmal and mitochondrial membranes
    • P.A. Elustondo, P.R. Angelova, M. Kawalec, M. Michalak, P. Kurcok, A.Y. Abramov, and E.V. Pavlov Polyhydroxybutyrate targets mammalian mitochondria and increases permeability of plasmalemmal and mitochondrial membranes PLoS One 8 2013 e75812
    • (2013) PLoS One , vol.8 , pp. 75812
    • Elustondo, P.A.1    Angelova, P.R.2    Kawalec, M.3    Michalak, M.4    Kurcok, P.5    Abramov, A.Y.6    Pavlov, E.V.7
  • 14
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • T. Finkel, and N.J. Holbrook Oxidants, oxidative stress and the biology of ageing Nature 408 2000 239 247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 17
    • 84906268632 scopus 로고    scopus 로고
    • The C ring of the F1Fo ATP synthase forms the mitochondrial permeability transition pore: A critical appraisal
    • A.P. Halestrap The C ring of the F1Fo ATP synthase forms the mitochondrial permeability transition pore: a critical appraisal Front. Oncol. 4 2014 234
    • (2014) Front. Oncol. , vol.4 , pp. 234
    • Halestrap, A.P.1
  • 18
    • 0025193488 scopus 로고
    • 2(+)-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase
    • 2(+)-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase Biochem. J. 268 1990 153 160
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 19
    • 84916620324 scopus 로고    scopus 로고
    • The mitochondrial permeability transition: A current perspective on its identity and role in ischaemia/reperfusion injury
    • (in press)
    • A.P. Halestrap, and A.P. Richardson The mitochondrial permeability transition: a current perspective on its identity and role in ischaemia/reperfusion injury J. Mol. Cell. Cardiol. 2014 10.1016/j.yjmcc.2014.08.01 (in press)
    • (2014) J. Mol. Cell. Cardiol.
    • Halestrap, A.P.1    Richardson, A.P.2
  • 21
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • D.R. Hunter, R.A. Haworth, and J.H. Southard Relationship between configuration, function, and permeability in calcium-treated mitochondria J. Biol. Chem. 251 1976 5069 5077
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 22
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • F. Ichas, L.S. Jouaville, and J.P. Mazat Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals Cell 89 1997 1145 1153
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 23
    • 0032504717 scopus 로고    scopus 로고
    • From calcium signaling to cell death: Two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state
    • F. Ichas, and J.P. Mazat From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state Biochim. Biophys. Acta 1366 1998 33 50
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 33-50
    • Ichas, F.1    Mazat, J.P.2
  • 24
    • 84904608695 scopus 로고    scopus 로고
    • Identifying the components of the elusive mitochondrial permeability transition pore
    • J. Karch, and J.D. Molkentin Identifying the components of the elusive mitochondrial permeability transition pore Proc. Natl. Acad. Sci. U. S. A. 111 2014 10396 10397
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 10396-10397
    • Karch, J.1    Molkentin, J.D.2
  • 25
    • 0024433994 scopus 로고
    • Mitochondrial channel activity studied by patch-clamping mitoplasts
    • K.W. Kinnally, M.L. Campo, and H. Tedeschi Mitochondrial channel activity studied by patch-clamping mitoplasts J. Bioenerg. Biomembr. 21 1989 497 506
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 497-506
    • Kinnally, K.W.1    Campo, M.L.2    Tedeschi, H.3
  • 29
    • 0032924757 scopus 로고    scopus 로고
    • Mitochondrial damage induced by conditions of oxidative stress
    • A.J. Kowaltowski, and A.E. Vercesi Mitochondrial damage induced by conditions of oxidative stress Free Radic. Biol. Med. 26 1999 463 471
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 463-471
    • Kowaltowski, A.J.1    Vercesi, A.E.2
  • 31
    • 0026463795 scopus 로고
    • Inhibition by spermine of the inner membrane permeability transition of isolated rat heart mitochondria
    • R.G. Lapidus, and P.M. Sokolove Inhibition by spermine of the inner membrane permeability transition of isolated rat heart mitochondria FEBS Lett. 313 1992 314 318
    • (1992) FEBS Lett. , vol.313 , pp. 314-318
    • Lapidus, R.G.1    Sokolove, P.M.2
  • 32
    • 0027501594 scopus 로고
    • Spermine inhibition of the permeability transition of isolated rat liver mitochondria: An investigation of mechanism
    • R.G. Lapidus, and P.M. Sokolove Spermine inhibition of the permeability transition of isolated rat liver mitochondria: an investigation of mechanism Arch. Biochem. Biophys. 306 1993 246 253
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 246-253
    • Lapidus, R.G.1    Sokolove, P.M.2
  • 34
    • 22144441633 scopus 로고    scopus 로고
    • A large, voltage-dependent channel, isolated from mitochondria by water-free chloroform extraction
    • E. Pavlov, E. Zakharian, C. Bladen, C.T. Diao, C. Grimbly, R.N. Reusch, and R.J. French A large, voltage-dependent channel, isolated from mitochondria by water-free chloroform extraction Biophys. J. 88 2005 2614 2625
    • (2005) Biophys. J. , vol.88 , pp. 2614-2625
    • Pavlov, E.1    Zakharian, E.2    Bladen, C.3    Diao, C.T.4    Grimbly, C.5    Reusch, R.N.6    French, R.J.7
  • 35
    • 0033021780 scopus 로고    scopus 로고
    • Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • V. Petronilli, G. Miotto, M. Canton, M. Brini, R. Colonna, P. Bernardi, and L.F. Di Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence Biophys. J. 76 1999 725 734
    • (1999) Biophys. J. , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3    Brini, M.4    Colonna, R.5    Bernardi, P.6    Di, L.F.7
  • 36
    • 0024787657 scopus 로고
    • The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria
    • V. Petronilli, I. Szabo, and M. Zoratti The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria FEBS Lett. 259 1989 137 143
    • (1989) FEBS Lett. , vol.259 , pp. 137-143
    • Petronilli, V.1    Szabo, I.2    Zoratti, M.3
  • 38
    • 0032895918 scopus 로고    scopus 로고
    • Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells
    • R.M. Ray, B.J. Zimmerman, S.A. McCormack, T.B. Patel, and L.R. Johnson Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells Am. J. Physiol. 276 1999 C684 C691
    • (1999) Am. J. Physiol. , vol.276 , pp. 684-C691
    • Ray, R.M.1    Zimmerman, B.J.2    McCormack, S.A.3    Patel, T.B.4    Johnson, L.R.5
  • 40
    • 33749251817 scopus 로고    scopus 로고
    • Free radical scavenging action of the natural polyamine spermine in rat liver mitochondria
    • I.G. Sava, V. Battaglia, C.A. Rossi, M. Salvi, and A. Toninello Free radical scavenging action of the natural polyamine spermine in rat liver mitochondria Free Radic. Biol. Med. 41 2006 1272 1281
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1272-1281
    • Sava, I.G.1    Battaglia, V.2    Rossi, C.A.3    Salvi, M.4    Toninello, A.5
  • 41
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • R.C. Scaduto Jr., and L.W. Grotyohann Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives Biophys. J. 76 1999 469 477
    • (1999) Biophys. J. , vol.76 , pp. 469-477
    • Scaduto, R.C.1    Grotyohann, L.W.2
  • 42
    • 84871456452 scopus 로고    scopus 로고
    • Inorganic polyphosphate - An unusual suspect of the mitochondrial permeability transition mystery
    • L.K. Seidlmayer, L.A. Blatter, E. Pavlov, and E.N. Dedkova Inorganic polyphosphate - an unusual suspect of the mitochondrial permeability transition mystery Channels (Austin) 6 2012
    • (2012) Channels (Austin) , vol.6
    • Seidlmayer, L.K.1    Blatter, L.A.2    Pavlov, E.3    Dedkova, E.N.4
  • 43
    • 84861120098 scopus 로고    scopus 로고
    • Inorganic polyphosphate is a potent activator of the mitochondrial permeability transition pore in cardiac myocytes
    • L.K. Seidlmayer, M.R. Gomez-Garcia, L.A. Blatter, E. Pavlov, and E.N. Dedkova Inorganic polyphosphate is a potent activator of the mitochondrial permeability transition pore in cardiac myocytes J. Gen. Physiol. 139 2012 321 331
    • (2012) J. Gen. Physiol. , vol.139 , pp. 321-331
    • Seidlmayer, L.K.1    Gomez-Garcia, M.R.2    Blatter, L.A.3    Pavlov, E.4    Dedkova, E.N.5
  • 44
    • 84871528525 scopus 로고    scopus 로고
    • Inhibition of polyphosphate as a novel strategy for preventing thrombosis and inflammation
    • S.A. Smith, S.H. Choi, J.N. Collins, R.J. Travers, B.C. Cooley, and J.H. Morrissey Inhibition of polyphosphate as a novel strategy for preventing thrombosis and inflammation Blood 120 2012 5103 5110
    • (2012) Blood , vol.120 , pp. 5103-5110
    • Smith, S.A.1    Choi, S.H.2    Collins, J.N.3    Travers, R.J.4    Cooley, B.C.5    Morrissey, J.H.6
  • 45
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • I. Szabo, and M. Zoratti The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A J. Biol. Chem. 266 1991 3376 3379
    • (1991) J. Biol. Chem. , vol.266 , pp. 3376-3379
    • Szabo, I.1    Zoratti, M.2
  • 46
    • 0026550587 scopus 로고
    • The mitochondrial megachannel is the permeability transition pore
    • I. Szabo, and M. Zoratti The mitochondrial megachannel is the permeability transition pore J. Bioenerg. Biomembr. 24 1992 111 117
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 111-117
    • Szabo, I.1    Zoratti, M.2
  • 47
    • 0027234336 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore
    • I. Szabo, and M. Zoratti The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore FEBS Lett. 330 1993 201 205
    • (1993) FEBS Lett. , vol.330 , pp. 201-205
    • Szabo, I.1    Zoratti, M.2
  • 48
    • 0030600361 scopus 로고    scopus 로고
    • The contribution of endogenous polyamines to the permeability transition of rat liver mitochondria
    • V. Tassani, M. Campagnolo, A. Toninello, and D. Siliprandi The contribution of endogenous polyamines to the permeability transition of rat liver mitochondria Biochem. Biophys. Res. Commun. 226 1996 850 854
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 850-854
    • Tassani, V.1    Campagnolo, M.2    Toninello, A.3    Siliprandi, D.4
  • 49
    • 0020448392 scopus 로고
    • Localization of polyphosphates in Saccharomyces fragilis, as revealed by 4′,6-diamidino-2-phenylindole fluorescence
    • J.P. Tijssen, H.W. Beekes, and S.J. Van Localization of polyphosphates in Saccharomyces fragilis, as revealed by 4′,6-diamidino-2-phenylindole fluorescence Biochim. Biophys. Acta 721 1982 394 398
    • (1982) Biochim. Biophys. Acta , vol.721 , pp. 394-398
    • Tijssen, J.P.1    Beekes, H.W.2    Van, S.J.3
  • 50
    • 0039007970 scopus 로고    scopus 로고
    • Kinetics and free energy profiles of spermine transport in liver mitochondria
    • A. Toninello, V.L. Dalla, R. Stevanato, and S. Yagisawa Kinetics and free energy profiles of spermine transport in liver mitochondria Biochemistry 39 2000 324 331
    • (2000) Biochemistry , vol.39 , pp. 324-331
    • Toninello, A.1    Dalla, V.L.2    Stevanato, R.3    Yagisawa, S.4
  • 51
    • 0021839729 scopus 로고
    • Uptake of spermine by rat liver mitochondria and its influence on the transport of phosphate
    • A. Toninello, L.F. Di, D. Siliprandi, and N. Siliprandi Uptake of spermine by rat liver mitochondria and its influence on the transport of phosphate Biochim. Biophys. Acta 815 1985 399 404
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 399-404
    • Toninello, A.1    Di, L.F.2    Siliprandi, D.3    Siliprandi, N.4
  • 53
    • 4444371864 scopus 로고    scopus 로고
    • Interaction of biologically active amines with mitochondria and their role in the mitochondrial-mediated pathway of apoptosis
    • A. Toninello, M. Salvi, and B. Mondovi Interaction of biologically active amines with mitochondria and their role in the mitochondrial-mediated pathway of apoptosis Curr. Med. Chem. 11 2004 2349 2374
    • (2004) Curr. Med. Chem. , vol.11 , pp. 2349-2374
    • Toninello, A.1    Salvi, M.2    Mondovi, B.3
  • 54
  • 55
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • M. Zoratti, and I. Szabo The mitochondrial permeability transition Biochim. Biophys. Acta 1241 1995 139 176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2


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