메뉴 건너뛰기




Volumn 8, Issue 3-4, 1998, Pages 263-272

Imaging the mitochondrial permeability transition pore in intact cells

Author keywords

Calcein; Calcium; Cyclosporin; Mitochondria; Permeability transition pore

Indexed keywords

CALCEIN;

EID: 0032435391     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520080314     Document Type: Review
Times cited : (90)

References (38)
  • 1
    • 0018899158 scopus 로고
    • Serum-induced leakage of liposome contents
    • T.M. Allen and L.G. Cleland, Serum-induced leakage of liposome contents, Biochim. Biophys. Acta 597 (1980), 418-426.
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 418-426
    • Allen, T.M.1    Cleland, L.G.2
  • 2
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization
    • P. Bernardi, Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization, J. Biol. Chem, 267 (1992), 8834-8839.
    • (1992) J. Biol. Chem , vol.267 , pp. 8834-8839
    • Bernardi, P.1
  • 4
    • 0029998621 scopus 로고    scopus 로고
    • The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal
    • P. Bernardi and V. Petronilli, The permeability transition pore as a mitochondrial calcium release channel: a critical appraisal, J. Bioenerg. Biomembr. 28 (1996), 131-138.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 131-138
    • Bernardi, P.1    Petronilli, V.2
  • 5
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • E. Bossy Wetzel, D.D. Newmeyer and D.R. Green, Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization, EMBO J. 17 (1998), 37-49.
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 6
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • E. Carafoli, Intracellular calcium homeostasis, Ann. Rev. Biochem. 56 (1987), 395-433.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 7
    • 0023790347 scopus 로고
    • Inorganic pyrophosphate is located primarily in the mitochondria of the hepatocyte and increases in parallel with the decrease in light-scattering induced by gluconeogenic hormones, butyrate and ionophore A23187
    • A.M. Davidson and A.P. Halestrap, Inorganic pyrophosphate is located primarily in the mitochondria of the hepatocyte and increases in parallel with the decrease in light-scattering induced by gluconeogenic hormones, butyrate and ionophore A23187, Biochem. J. 254 (1988), 379-384.
    • (1988) Biochem. J. , vol.254 , pp. 379-384
    • Davidson, A.M.1    Halestrap, A.P.2
  • 8
    • 0000097444 scopus 로고    scopus 로고
    • Detection of mitochondrial depolarization during autophagy by confocal fluorescence resonance energy transfer (CFRET)
    • S.P. Elmore, T. Qian, L.C. Trost, Y. Nishimura, B. Herman and J.J. Lemasters, Detection of mitochondrial depolarization during autophagy by confocal fluorescence resonance energy transfer (CFRET), Cell Vision - J. Anal. Morphol. 4 (1997), 170-171.
    • (1997) Cell Vision - J. Anal. Morphol. , vol.4 , pp. 170-171
    • Elmore, S.P.1    Qian, T.2    Trost, L.C.3    Nishimura, Y.4    Herman, B.5    Lemasters, J.J.6
  • 9
    • 0030785799 scopus 로고    scopus 로고
    • Efficiency of P-glycoprotein-mediated exclusion of rhodamine dyes from multidrug-resistant cells is determined by their passive transmembrane movement rate
    • G.D. Eytan, R. Regev, G. Oren, C.D. Hurwitz and Y.G. Assaraf, Efficiency of P-glycoprotein-mediated exclusion of rhodamine dyes from multidrug-resistant cells is determined by their passive transmembrane movement rate, Eur. J. Biochem. 248 (1997), 104-112.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 104-112
    • Eytan, G.D.1    Regev, R.2    Oren, G.3    Hurwitz, C.D.4    Assaraf, Y.G.5
  • 10
    • 0028276439 scopus 로고
    • Immunophilins in protein folding and immunosuppression
    • D.A. Fruman, S.J. Burakoff and B.E. Bierer, Immunophilins in protein folding and immunosuppression, FASEB J. 8 (1994), 391-400.
    • (1994) FASEB J. , vol.8 , pp. 391-400
    • Fruman, D.A.1    Burakoff, S.J.2    Bierer, B.E.3
  • 11
    • 0025501351 scopus 로고
    • The photodynamic effect of rose bengal on proteins of the mitochondrial inner membrane
    • C. Giulivi, M. Sarcansky, E. Rosenfeld and A. Boveris, The photodynamic effect of rose bengal on proteins of the mitochondrial inner membrane, Photochem. Photobiol. 52 (1990), 745-751.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 745-751
    • Giulivi, C.1    Sarcansky, M.2    Rosenfeld, E.3    Boveris, A.4
  • 13
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • E.J. Griffiths and A.P. Halestrap, Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion, Biochem. J. 307 (1995), 93-98.
    • (1995) Biochem. J. , vol.307 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 14
    • 0028095807 scopus 로고
    • Mitochondrial calcium transport: Physiological and pathological relevance
    • T.E. Gunter, K.K. Gunter, S.S. Sheu and C.E. Gavin, Mitochondrial calcium transport: physiological and pathological relevance, Am. J. Physiol. 267 (1994), C313-C339.
    • (1994) Am. J. Physiol. , vol.267
    • Gunter, T.E.1    Gunter, K.K.2    Sheu, S.S.3    Gavin, C.E.4
  • 15
    • 0029958864 scopus 로고    scopus 로고
    • Apoptosis: Mitochondria resurrected?
    • P.A. Henkart and S. Grinstein, Apoptosis: mitochondria resurrected?, J. Exp. Med. 183 (1996), 1293-1295.
    • (1996) J. Exp. Med. , vol.183 , pp. 1293-1295
    • Henkart, P.A.1    Grinstein, S.2
  • 16
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • J. Hüser, C.E. Rechenmacher and L.A. Blatter, Imaging the permeability pore transition in single mitochondria, Biophys. J. 74 (1998), 2129-2137.
    • (1998) Biophys. J. , vol.74 , pp. 2129-2137
    • Hüser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 17
    • 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
  • 18
    • 0028342740 scopus 로고
    • Mitochondrial calcium spiking: A transduction mechanism based on calcium-induced permeability transition involved in cell calcium signalling
    • F. Ichas, L.S. Jouaville, S.S. Sidash, J.P. Mazat and E.L. Holmuhamedov, Mitochondrial calcium spiking: a transduction mechanism based on calcium-induced permeability transition involved in cell calcium signalling, FEBS Lett. 348 (1994), 211-215.
    • (1994) FEBS Lett. , vol.348 , pp. 211-215
    • Ichas, F.1    Jouaville, L.S.2    Sidash, S.S.3    Mazat, J.P.4    Holmuhamedov, E.L.5
  • 21
    • 0030743356 scopus 로고    scopus 로고
    • Competitive, non-competitive and cooperative interactions between substrates of P-glycoprotein as measured by its ATPase activity
    • T. Litman, T. Zeuthen, T. Skovsgaard and W.D. Stein, Competitive, non-competitive and cooperative interactions between substrates of P-glycoprotein as measured by its ATPase activity, Biochim. Biophys. Acta 1361 (1997), 169-176.
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 169-176
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 22
    • 0029816659 scopus 로고    scopus 로고
    • Cellular functions of immunophilins
    • A.R. Marks, Cellular functions of immunophilins, Physiol. Rev. 76 (1996), 631-649.
    • (1996) Physiol. Rev. , vol.76 , pp. 631-649
    • Marks, A.R.1
  • 24
    • 0028923778 scopus 로고
    • Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide
    • A.L. Nieminen, A.K. Saylor, S.A. Tesfai, B. Herman and J.J. Lemasters, Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide, Biochem. J. 307 (1995), 99-106.
    • (1995) Biochem. J. , vol.307 , pp. 99-106
    • Nieminen, A.L.1    Saylor, A.K.2    Tesfai, S.A.3    Herman, B.4    Lemasters, J.J.5
  • 25
    • 0027156357 scopus 로고
    • Cyclosporin and carnitine prevent the anoxic death of cultured hepatocytes by inhibiting the mitochondrial permeability transition
    • J.G. Pastorino, J.W. Snyder, A. Serroni, J.B. Hoek and J.L. Farber, Cyclosporin and carnitine prevent the anoxic death of cultured hepatocytes by inhibiting the mitochondrial permeability transition, J. Biol. Chem. 268 (1993), 13 791-13 798.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13791-13798
    • Pastorino, J.G.1    Snyder, J.W.2    Serroni, A.3    Hoek, J.B.4    Farber, J.L.5
  • 26
    • 0013637626 scopus 로고    scopus 로고
    • Direct evidence of the mitochondrial permeability transition pore (MTP) in single living cells
    • V. Petronilli, P. Bernardi, M. Canton, R. Colonna, G. Miotto and F. Di Lisa, Direct evidence of the mitochondrial permeability transition pore (MTP) in single living cells, Biophys. J. 74 (1998), A383.
    • (1998) Biophys. J. , vol.74
    • Petronilli, V.1    Bernardi, P.2    Canton, M.3    Colonna, R.4    Miotto, G.5    Di Lisa, F.6
  • 28
    • 0345396686 scopus 로고    scopus 로고
    • Tetramethylrhodamine (TMRM) quenching of calcein fluorescence limits the evaluation of intracellular distribution of calcein
    • V. Petronilli, G. Miotto, R. Colonna, P. Bernardi and F. Di Lisa, Tetramethylrhodamine (TMRM) quenching of calcein fluorescence limits the evaluation of intracellular distribution of calcein, Biophys. J. 70 (1997), A210.
    • (1997) Biophys. J. , vol.70
    • Petronilli, V.1    Miotto, G.2    Colonna, R.3    Bernardi, P.4    Di Lisa, F.5
  • 29
    • 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
  • 30
    • 0025187798 scopus 로고
    • Structural and functional aspects of calcium homeostasis in eukaryotic cells
    • D. Pietrobon, F. Di Virgilio and T. Pozzan, Structural and functional aspects of calcium homeostasis in eukaryotic cells, Eur. J. Biochem. 193 (1990), 599-622.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 599-622
    • Pietrobon, D.1    Di Virgilio, F.2    Pozzan, T.3
  • 32
    • 0030799117 scopus 로고    scopus 로고
    • Singlet oxygen produced by photodynamic action causes inactivation of the mitochondrial permeability transition pore
    • C. Salet, G. Moreno, F. Ricchelli and P. Bernardi, Singlet oxygen produced by photodynamic action causes inactivation of the mitochondrial permeability transition pore, J. Biol. Chem. 272 (1997), 21 938-21 943.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21938-21943
    • Salet, C.1    Moreno, G.2    Ricchelli, F.3    Bernardi, P.4
  • 33
    • 0029810095 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a primary event in glutamate neurotoxicity
    • A.F. Schinder, E.C. Olson, N.C. Spitzer and M. Montai, Mitochondrial dysfunction is a primary event in glutamate neurotoxicity, J. Neurosci. 16 (1996), 6125-6133.
    • (1996) J. Neurosci. , vol.16 , pp. 6125-6133
    • Schinder, A.F.1    Olson, E.C.2    Spitzer, N.C.3    Montai, M.4
  • 34
    • 0026703122 scopus 로고
    • Modulation of the mitochondrial megachannel by divalent cations and protons
    • I. Szabo, P. Bernardi and M. Zoratti, Modulation of the mitochondrial megachannel by divalent cations and protons, J. Biol. Chem. 267 (1992), 2940-2946.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2940-2946
    • Szabo, I.1    Bernardi, P.2    Zoratti, M.3
  • 35
    • 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
  • 36
    • 0000237793 scopus 로고
    • Fluorescence techniques in the microdetermination of metals in biological materials
    • D.F.H. Wallach and T.L. Steck, Fluorescence techniques in the microdetermination of metals in biological materials, Anal. Chem. 35 (1963), 1035-1044.
    • (1963) Anal. Chem. , vol.35 , pp. 1035-1044
    • Wallach, D.F.H.1    Steck, T.L.2
  • 38
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.