메뉴 건너뛰기




Volumn 32, Issue 1, 2008, Pages 136-145

Effect of magnesium on calcium-induced depolarisation of mitochondrial transmembrane potential

Author keywords

Calcium; Magnesium; Mitochondria; Trans membrane potential

Indexed keywords

CALCIUM; MAGNESIUM; MITOCHONDRIAL PERMEABILITY TRANSITION PORE;

EID: 39049104953     PISSN: 10656995     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellbi.2007.08.024     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0022931338 scopus 로고
    • 2+-induced permeabilisation of rat liver mitochondria
    • 2+-induced permeabilisation of rat liver mitochondria. Biochem J 239 (1986) 19-29
    • (1986) Biochem J , vol.239 , pp. 19-29
    • Al-Nasser, I.1    Crompton, M.2
  • 2
    • 0037127260 scopus 로고    scopus 로고
    • Occurrence and characteristics of the mitochondrial permeability transition in plants
    • Arpagaus S., Rawyler A., and Braendle R. Occurrence and characteristics of the mitochondrial permeability transition in plants. J Biol Chem 277 (2002) 1780-1787
    • (2002) J Biol Chem , vol.277 , pp. 1780-1787
    • Arpagaus, S.1    Rawyler, A.2    Braendle, R.3
  • 3
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines C.P., Kaiser R.A., Purcell N.H., Blair N.S., Osinska H., Hambleton M.A., et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434 (2005) 658-662
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4    Osinska, H.5    Hambleton, M.A.6
  • 4
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev 79 (1999) 1127-1155
    • (1999) Physiol Rev , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 5
    • 0026687312 scopus 로고
    • Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations
    • Bernardi P., Vassanelli S., Veronese P., Colonna R., Szabo I., and Zoratti M. Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J Biol Chem 267 (1992) 2934-2939
    • (1992) J Biol Chem , vol.267 , pp. 2934-2939
    • Bernardi, P.1    Vassanelli, S.2    Veronese, P.3    Colonna, R.4    Szabo, I.5    Zoratti, M.6
  • 6
    • 33646255246 scopus 로고    scopus 로고
    • The mitochondrial permeability transition from in vitro artifact to disease target
    • Bernardi P., Krauskopf A., Basso E., Petronilli V., Blachly-Dyson E., Di Lisa F., et al. The mitochondrial permeability transition from in vitro artifact to disease target. FEBS J 273 (2006) 2077-2099
    • (2006) FEBS J , vol.273 , pp. 2077-2099
    • Bernardi, P.1    Krauskopf, A.2    Basso, E.3    Petronilli, V.4    Blachly-Dyson, E.5    Di Lisa, F.6
  • 7
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • Berridge M.J., Lipp P., and Bootman M.D. The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol 1 (2000) 11-21
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 8
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemeier K.M., Dempsey M.E., and Pfeiffer D.R. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J Biol Chem 264 (1989) 7826-7830
    • (1989) J Biol Chem , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 9
    • 0032558403 scopus 로고    scopus 로고
    • Proton selective substrate of the mitochondrial permeability transition pore: regulation by the redox state of the electron transport chain
    • Broekemeier K.M., Klocek C.K., and Pfeiffer D.R. Proton selective substrate of the mitochondrial permeability transition pore: regulation by the redox state of the electron transport chain. Biochemistry 37 (1998) 13059-13065
    • (1998) Biochemistry , vol.37 , pp. 13059-13065
    • Broekemeier, K.M.1    Klocek, C.K.2    Pfeiffer, D.R.3
  • 11
    • 0033995265 scopus 로고    scopus 로고
    • Dual responses of CNS mitochondria to elevated calcium
    • Brustovetsky N., and Dubinsky J.M. Dual responses of CNS mitochondria to elevated calcium. J Neurosci 20 (2000) 103-113
    • (2000) J Neurosci , vol.20 , pp. 103-113
    • Brustovetsky, N.1    Dubinsky, J.M.2
  • 12
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. J Physiol 529 (2000) 11-21
    • (2000) J Physiol , vol.529 , pp. 11-21
    • Crompton, M.1
  • 13
    • 0034668833 scopus 로고    scopus 로고
    • Mitochondria and calcium: from cell signalling to cell death
    • Duchen M.R. Mitochondria and calcium: from cell signalling to cell death. J Physiol 529 (2000) 57-68
    • (2000) J Physiol , vol.529 , pp. 57-68
    • Duchen, M.R.1
  • 14
    • 0032487583 scopus 로고    scopus 로고
    • Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions
    • Eskes R., Antonsson B., Osen-Sand A., Montessuit S., Richter C., Sadoul R., et al. Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions. J Cell Biol 143 (1998) 217-224
    • (1998) J Cell Biol , vol.143 , pp. 217-224
    • Eskes, R.1    Antonsson, B.2    Osen-Sand, A.3    Montessuit, S.4    Richter, C.5    Sadoul, R.6
  • 15
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 17
    • 1142273368 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening during myocardial reperfusion-a target for cardioprotection
    • Halestrap A.P., Clarke S.J., and Javadov S.A. Mitochondrial permeability transition pore opening during myocardial reperfusion-a target for cardioprotection. Cardiovasc Res 61 (2004) 372-385
    • (2004) Cardiovasc Res , vol.61 , pp. 372-385
    • Halestrap, A.P.1    Clarke, S.J.2    Javadov, S.A.3
  • 18
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas F., Jouaville L.S., and Mazat J.-P. 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
  • 19
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming
    • Jouaville L.S., Pinton P., Bastianutto C., Rutter G.A., and Rizzuto R. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc Natl Acad Sci U S A 96 (1999) 13807-13812
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 20
    • 0024433994 scopus 로고
    • Mitochondrial channel activity studied by patch-clamping mitoplasts
    • Kinnaly K.W., Campo M.L., and Tedeschi H. Mitochondrial channel activity studied by patch-clamping mitoplasts. J Bioenerg Biomembr 21 (1989) 497-506
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 497-506
    • Kinnaly, K.W.1    Campo, M.L.2    Tedeschi, H.3
  • 21
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., and Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427 (2004) 360-364
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 22
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka J.E., Waymire K.G., Levy S.E., Sligh J.E., Cai J., Jones D.P., et al. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427 (2004) 461-465
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3    Sligh, J.E.4    Cai, J.5    Jones, D.P.6
  • 23
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87 (2007) 99-163
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 24
    • 23844482151 scopus 로고    scopus 로고
    • Mitochondrial calcium signalling in cell death
    • Leo S., Bianchi K., Brini M., and Rizzuto R. Mitochondrial calcium signalling in cell death. FEBS J 272 (2005) 4013-4022
    • (2005) FEBS J , vol.272 , pp. 4013-4022
    • Leo, S.1    Bianchi, K.2    Brini, M.3    Rizzuto, R.4
  • 25
    • 0038381516 scopus 로고    scopus 로고
    • Mitochondrial regulation of synaptic plasticity in the hippocampus
    • Levy M., Faas G.C., Saggau P., Craigen W.J., and Sweatt J.D. Mitochondrial regulation of synaptic plasticity in the hippocampus. J Biol Chem 278 (2003) 17727-17734
    • (2003) J Biol Chem , vol.278 , pp. 17727-17734
    • Levy, M.1    Faas, G.C.2    Saggau, P.3    Craigen, W.J.4    Sweatt, J.D.5
  • 26
    • 6344287496 scopus 로고    scopus 로고
    • Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis
    • Li Y., Johnson N., Capano M., Edwards M., and Crompton M. Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis. Biochem J 383 (2004) 101-109
    • (2004) Biochem J , vol.383 , pp. 101-109
    • Li, Y.1    Johnson, N.2    Capano, M.3    Edwards, M.4    Crompton, M.5
  • 27
    • 0030610547 scopus 로고    scopus 로고
    • Regulation of the mitochondrial Ca2+ uniporter by external adenine nucleotides: the uniporter behaves like a gated channel which is regulated by nucleotides and divalent cations
    • Litsky M.L., and Pfeiffer D.R. Regulation of the mitochondrial Ca2+ uniporter by external adenine nucleotides: the uniporter behaves like a gated channel which is regulated by nucleotides and divalent cations. Biochemistry 36 (1997) 7071-7080
    • (1997) Biochemistry , vol.36 , pp. 7071-7080
    • Litsky, M.L.1    Pfeiffer, D.R.2
  • 29
    • 5844266828 scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchel P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Bodmin: Glynn Research (1966)
    • (1966) Bodmin: Glynn Research
    • Mitchel, P.1
  • 30
    • 0033970293 scopus 로고    scopus 로고
    • Mysteries of magnesium homeostasis
    • Murphy E. Mysteries of magnesium homeostasis. Circ Res 86 (2000) 245-248
    • (2000) Circ Res , vol.86 , pp. 245-248
    • Murphy, E.1
  • 31
    • 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., Yamaguchi O., Otsu K., Yamagata H., et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434 (2005) 652-658
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6
  • 32
    • 0020479813 scopus 로고
    • On the relative roles of Ca2+ and Mg2+ in regulating the endogenous K+/H+ exchanger of rat liver mitochondria
    • Nakashima R.A., Dordick R.S., and Garlid K.D. On the relative roles of Ca2+ and Mg2+ in regulating the endogenous K+/H+ exchanger of rat liver mitochondria. J Biol Chem 257 (1982) 12540-12545
    • (1982) J Biol Chem , vol.257 , pp. 12540-12545
    • Nakashima, R.A.1    Dordick, R.S.2    Garlid, K.D.3
  • 33
    • 0026742968 scopus 로고
    • The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A
    • Novgorodov S.A., Gudz T.I., Milgrom Y.M., and Brierley G.P. The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A. J Biol Chem 267 (1992) 16274-16282
    • (1992) J Biol Chem , vol.267 , pp. 16274-16282
    • Novgorodov, S.A.1    Gudz, T.I.2    Milgrom, Y.M.3    Brierley, G.P.4
  • 35
    • 0029661903 scopus 로고    scopus 로고
    • Mg2+ control of respiration in isolated rat liver mitochondria
    • Panov A., and Scarpa A. Mg2+ control of respiration in isolated rat liver mitochondria. Biochemistry 35 (1996) 12849-12856
    • (1996) Biochemistry , vol.35 , pp. 12849-12856
    • Panov, A.1    Scarpa, A.2
  • 36
    • 0034521388 scopus 로고    scopus 로고
    • The comeback of mitochondria to calcium signalling
    • Pozzan T., Magalhaes P., and Rizzuto R. The comeback of mitochondria to calcium signalling. Cell Calcium 28 (2000) 279-283
    • (2000) Cell Calcium , vol.28 , pp. 279-283
    • Pozzan, T.1    Magalhaes, P.2    Rizzuto, R.3
  • 37
    • 0342432199 scopus 로고    scopus 로고
    • Modulation of oxidative phosphorylation by Mg2+ in rat heart mitochondria
    • Rodriguez-Zavala J.S., and Moreno-Sanchez R. Modulation of oxidative phosphorylation by Mg2+ in rat heart mitochondria. J Biol Chem 273 (1998) 7850-7855
    • (1998) J Biol Chem , vol.273 , pp. 7850-7855
    • Rodriguez-Zavala, J.S.1    Moreno-Sanchez, R.2
  • 38
    • 0034242456 scopus 로고    scopus 로고
    • Regulation of cellular magnesium
    • Romani A., and Scarpa A. Regulation of cellular magnesium. Front Biosci 5 (2000) D720-D734
    • (2000) Front Biosci , vol.5
    • Romani, A.1    Scarpa, A.2
  • 39
    • 3342910554 scopus 로고    scopus 로고
    • Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury
    • Starkov A.A., Chinopoulos C., and Fiskum G. Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury. Cell Calcium 36 (2004) 257-264
    • (2004) Cell Calcium , vol.36 , pp. 257-264
    • Starkov, A.A.1    Chinopoulos, C.2    Fiskum, G.3
  • 40
    • 0024787657 scopus 로고
    • The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria
    • Szabo I., and Zoratti M. 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
    • Szabo, I.1    Zoratti, M.2
  • 41
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • Szabo I., and Zoratti M. 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
  • 42
    • 0028809371 scopus 로고
    • Inhibition of mitochondrial permeability transition by polyamines and magnesium: importance of the number and distribution of electric charges
    • Tassani V., Biban C., Toninello A., and Siliprandi D. Inhibition of mitochondrial permeability transition by polyamines and magnesium: importance of the number and distribution of electric charges. Biochem Biophys Res Commun 207 (1995) 661-667
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 661-667
    • Tassani, V.1    Biban, C.2    Toninello, A.3    Siliprandi, D.4
  • 43
    • 0021114722 scopus 로고
    • On the mechanism by which Mg2+ and adenine nucleotides restore membrane potential in rat liver mitochondria deenergized by Ca2+ and phosphate
    • Toninello A., Siliprandi D., and Siliprandi N. On the mechanism by which Mg2+ and adenine nucleotides restore membrane potential in rat liver mitochondria deenergized by Ca2+ and phosphate. Biochem Biophys Res Commun 111 (1983) 792-797
    • (1983) Biochem Biophys Res Commun , vol.111 , pp. 792-797
    • Toninello, A.1    Siliprandi, D.2    Siliprandi, N.3
  • 44
    • 0015814772 scopus 로고
    • The initial velocities of calcium uptake by rat liver mitochondria
    • Vinogradov A., and Scarpa A. The initial velocities of calcium uptake by rat liver mitochondria. J Biol Chem 248 (1973) 5527-5531
    • (1973) J Biol Chem , vol.248 , pp. 5527-5531
    • Vinogradov, A.1    Scarpa, A.2
  • 45
    • 0037166318 scopus 로고    scopus 로고
    • The role of mitochondrial porins and the permeability transition pore in learning and synaptic plasticity
    • Weeber E.J., Levy M., Sampson M.J., Anflous K., Armstrong D.L., Brown S.E., et al. The role of mitochondrial porins and the permeability transition pore in learning and synaptic plasticity. J Biol Chem 277 (2002) 18891-18897
    • (2002) J Biol Chem , vol.277 , pp. 18891-18897
    • Weeber, E.J.1    Levy, M.2    Sampson, M.J.3    Anflous, K.4    Armstrong, D.L.5    Brown, S.E.6
  • 46
    • 0023020128 scopus 로고
    • Kinetics of mitochondrial calcium transport. II. A kinetic description of the sodium-dependent calcium efflux mechanism of liver mitochondria and inhibition by ruthenium red and by tetraphenylphosphonium
    • Wingrove D.E., and Gunter T.E. Kinetics of mitochondrial calcium transport. II. A kinetic description of the sodium-dependent calcium efflux mechanism of liver mitochondria and inhibition by ruthenium red and by tetraphenylphosphonium. J Biol Chem 261 (1986) 15166-15171
    • (1986) J Biol Chem , vol.261 , pp. 15166-15171
    • Wingrove, D.E.1    Gunter, T.E.2
  • 47
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., and Szabo I. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.