메뉴 건너뛰기




Volumn 72, Issue 6, 1999, Pages 2488-2497

Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability

Author keywords

Brain; Cyclophilin D; Cyclosporin A; Mitochondria; Mitochondrial permeability transition; Neuronal death

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM CHLORIDE; CYCLOPHILIN; CYCLOSPORIN A; CYCLOSPORIN A DERIVATIVE; IMMUNOSUPPRESSIVE AGENT; N METHYLVALINE 4 CYCLOSPORINE A; PKF 220 384; UNCLASSIFIED DRUG;

EID: 0033007651     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0722488.x     Document Type: Article
Times cited : (127)

References (90)
  • 1
    • 0344679308 scopus 로고
    • Brain mitochondria
    • Lajtha A., ed, Plenum Press, New York
    • Abood L.-G. (1969) Brain mitochondria, in Handbook of Neurochemistry (Lajtha A., ed), pp. 303-326. Plenum Press, New York.
    • (1969) Handbook of Neurochemistry , pp. 303-326
    • Abood, L.-G.1
  • 3
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona M., Dypbukt J. M., Bonfoco E., Zhivotovsky B., Orrenius S., Lipton S. A., and Nicotera P. (1995) Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron 15, 961-973.
    • (1995) Neuron , vol.15 , pp. 961-973
    • Ankarcrona, M.1    Dypbukt, J.M.2    Bonfoco, E.3    Zhivotovsky, B.4    Orrenius, S.5    Lipton, S.A.6    Nicotera, P.7
  • 4
    • 0022263019 scopus 로고
    • The temporal evolution of hypoglycemic brain damage. I. Light- and electron-microscopic findings in the rat cerebral cortex
    • Auer R. N., Kalimo H., Olsson Y., and Siesjö B. K. (1985) The temporal evolution of hypoglycemic brain damage. I. Light- and electron-microscopic findings in the rat cerebral cortex. Acta Neuropathol. (Berl.) 67, 13-24.
    • (1985) Acta Neuropathol. (Berl.) , vol.67 , pp. 13-24
    • Auer, R.N.1    Kalimo, H.2    Olsson, Y.3    Siesjö, B.K.4
  • 5
    • 0030941354 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition by nitric oxide
    • Balakirev M., Khramtsov V. V., and Zimmer G. (1997) Modulation of the mitochondrial permeability transition by nitric oxide. Eur. J. Biochem. 246, 710-718.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 710-718
    • Balakirev, M.1    Khramtsov, V.V.2    Zimmer, G.3
  • 6
    • 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. (1992) Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J. Biol. Chem. 267, 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
  • 7
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P., Broekemeier K. M., and Pfeiffer D. R. (1994) Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26, 509-517.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 8
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • Beutner G., Ruck A., Riede B., and Brdiczka D. (1998) Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim. Biophys. Acta 1368, 7-18.
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 9
    • 0026063083 scopus 로고
    • Protection by acidotic pH against anoxia/reoxygenation injury to rat neonatal cardiac myocytes
    • Bond J. M., Herman B., and Lemasters J. J. (1991) Protection by acidotic pH against anoxia/reoxygenation injury to rat neonatal cardiac myocytes. Biochem. Biophys. Res. Commun. 179, 798-803.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 798-803
    • Bond, J.M.1    Herman, B.2    Lemasters, J.J.3
  • 10
    • 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. (1989) Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J. Biol. Chem. 264, 7826-7830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 12
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd S. L. and Nicholls D. G. (1996) Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67, 2282-2291.
    • (1996) J. Neurochem. , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 13
    • 0030850505 scopus 로고    scopus 로고
    • Neuroprotective actions of FK506 in experimental stroke: In vivo evidence against an antiexcitotoxic mechanism
    • Butcher S. P., Henshall D. C., Teramura Y., Iwasaki K., and Sharkey J. (1997) Neuroprotective actions of FK506 in experimental stroke: in vivo evidence against an antiexcitotoxic mechanism. J. Neurosci. 17, 6939-6946.
    • (1997) J. Neurosci. , vol.17 , pp. 6939-6946
    • Butcher, S.P.1    Henshall, D.C.2    Teramura, Y.3    Iwasaki, K.4    Sharkey, J.5
  • 14
    • 0343674241 scopus 로고
    • Brain mitochondria
    • Lajtha A., ed, Plenum Press, New York
    • Clark J. B. and Nicklas J. W. (1984) Brain mitochondria, in Handbook of Neurochemistry (Lajtha A., ed), pp. 135-159. Plenum Press, New York.
    • (1984) Handbook of Neurochemistry , pp. 135-159
    • Clark, J.B.1    Nicklas, J.W.2
  • 15
    • 0026696585 scopus 로고
    • Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
    • Connern C. P. and Halestrap A. P. (1992) Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin. Biochem. J. 284, 381-385.
    • (1992) Biochem. J. , vol.284 , pp. 381-385
    • Connern, C.P.1    Halestrap, A.P.2
  • 16
    • 0028075423 scopus 로고
    • Recruitment of mitochondrial eyclophilin to the mitochondrial inner meembrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
    • Connern C. P. and Halestrap A. P. (1994) Recruitment of mitochondrial eyclophilin to the mitochondrial inner meembrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem. J. 302, 321-324.
    • (1994) Biochem. J. , vol.302 , pp. 321-324
    • Connern, C.P.1    Halestrap, A.P.2
  • 18
    • 0023391047 scopus 로고
    • 2+-dependent pore activated by oxidative stress in heart mitochondria
    • 2+-dependent pore activated by oxidative stress in heart mitochondria. Biochem. J. 245, 915-918.
    • (1987) Biochem. J. , vol.245 , pp. 915-918
    • Crompton, M.1    Costi, A.2    Hayat, L.3
  • 19
    • 0023821864 scopus 로고
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem. J. 255, 357-360.
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 20
    • 0026027873 scopus 로고
    • Protection by acidotic ph against anoxic cell killing in perfused rat liver: Evidence for a pH paradox
    • Currin R. T., Gores G. J., Thurman R. G., and Lemasters J. J. (1991) Protection by acidotic pH against anoxic cell killing in perfused rat liver: evidence for a pH paradox. FASEB J. 5, 207-210.
    • (1991) FASEB J. , vol.5 , pp. 207-210
    • Currin, R.T.1    Gores, G.J.2    Thurman, R.G.3    Lemasters, J.J.4
  • 21
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration
    • Davey G. P., Peuchen S., and Clark J. B. (1998) Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration. J. Biol. Chem. 273, 12753-127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-13127
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 22
    • 0027244782 scopus 로고
    • Involvement of the ADP/ATP carrier in permeabilization processes of the inner mitochondrial membrane
    • de Macedo D. V., Nepomuceno M. E., and Pereira-da-Silva L. (1993) Involvement of the ADP/ATP carrier in permeabilization processes of the inner mitochondrial membrane. Eur. J. Biochem. 215, 595-600.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 595-600
    • De Macedo, D.V.1    Nepomuceno, M.E.2    Pereira-Da-Silva, L.3
  • 24
    • 0029821947 scopus 로고    scopus 로고
    • Regulation of adenine nucleotide transiocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues
    • Dummler K., Muller S., and Seitz H. J. (1996) Regulation of adenine nucleotide transiocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues. Biochem. J. 317, 913-918.
    • (1996) Biochem. J. , vol.317 , pp. 913-918
    • Dummler, K.1    Muller, S.2    Seitz, H.J.3
  • 26
    • 0032528154 scopus 로고    scopus 로고
    • Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death
    • Friberg H., Ferrand-Drake M., Bengtsson F., Halestrap A. P., and Wieloch T. (1998) Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death. J. Neurosci. 18, 5151-5159.
    • (1998) J. Neurosci. , vol.18 , pp. 5151-5159
    • Friberg, H.1    Ferrand-Drake, M.2    Bengtsson, F.3    Halestrap, A.P.4    Wieloch, T.5
  • 27
    • 0026132165 scopus 로고
    • Further evidence that cyclosporin A protects mitochondria from calcium overload by inhibiting a matrix peptidyl-prolyl cis-trans isomerase. Implications for the immunosuppressive and toxic effects of cyclosporin
    • Griffiths E. J. and Halestrap A. P. (1991) Further evidence that cyclosporin A protects mitochondria from calcium overload by inhibiting a matrix peptidyl-prolyl cis-trans isomerase. Implications for the immunosuppressive and toxic effects of cyclosporin. Biochem. J. 274, 611-614.
    • (1991) Biochem. J. , vol.274 , pp. 611-614
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 28
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • Griffiths E. J. and Halestrap A. P. (1995) Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion. Biochem. J. 307, 93-98.
    • (1995) Biochem. J. , vol.307 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 29
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter T. E. and Pfeiffer D. R. (1990) Mechanisms by which mitochondria transport calcium. Am. J. Physiol., 258, C755-C786.
    • (1990) Am. J. Physiol. , vol.258
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 30
    • 0025769501 scopus 로고
    • Calcium-dependent opening of a non-specific pore in the mitochondrial inner membrane is inhibited at pH values below 7. Implications for the protective effect of low pH against chemical and hypoxic cell damage
    • Halestrap A. P. (1991) Calcium-dependent opening of a non-specific pore in the mitochondrial inner membrane is inhibited at pH values below 7. Implications for the protective effect of low pH against chemical and hypoxic cell damage. Biochem. J. 278, 715-719.
    • (1991) Biochem. J. , vol.278 , pp. 715-719
    • Halestrap, A.P.1
  • 31
    • 0002290149 scopus 로고
    • Interaction between oxidative stress and calcium overload on mitochondrial function
    • Darley-Usmar V. and Schapira A. H. V., eds, Portland Press, London
    • Halestrap A. P. (1994) Interaction between oxidative stress and calcium overload on mitochondrial function, in Mitochondria: DNA, Proteins and Disease (Darley-Usmar V. and Schapira A. H. V., eds), pp. 113-142. Portland Press, London.
    • (1994) Mitochondria: DNA, Proteins and Disease , pp. 113-142
    • Halestrap, A.P.1
  • 32
    • 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, 153-160.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 33
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap A. P., Woodfield K. Y., and Connern C. P. (1997) Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272, 3346-3354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 34
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • Halestrap A. P., Kerr P. M., Javadov S., and Woodfield K. (1998) Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim. Biophys. Acta 1366, 79-94.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.4
  • 36
    • 0019230323 scopus 로고
    • 2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides
    • 2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides. J. Membr. Biol. 54, 231-236.
    • (1980) J. Membr. Biol. , vol.54 , pp. 231-236
    • Haworth, R.A.1    Hunter, D.R.2
  • 37
    • 0018332596 scopus 로고
    • 2+-induced membrane transition in mitochondria. I. The protective mechanisms
    • 2+-induced membrane transition in mitochondria. I. The protective mechanisms. Arch. Biochem. Biophys. 195, 453-459.
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 39
    • 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. (1997) Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell 89, 1145-1153.
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 40
    • 0016743902 scopus 로고
    • Experimental cerebral ischemia in mongolian gerbils. I. Light microscopic observations
    • Ito U., Spatz M., Walker J. T. Jr., and Klatzo I. (1975) Experimental cerebral ischemia in mongolian gerbils. I. Light microscopic observations. Acta Neuropathol. (Berl.) 32, 209-223.
    • (1975) Acta Neuropathol. (Berl.) , vol.32 , pp. 209-223
    • Ito, U.1    Spatz, M.2    Walker J.T., Jr.3    Klatzo, I.4
  • 41
    • 0000777914 scopus 로고
    • Adenosine-5′-diphosphate and adenosine-5′-monophosphate
    • Bergmeyer H. U., ed, Verlag Chemie Academic Press, Weinheim/New York
    • Jaworek D., Gruber W., and Bergmeyer H. U. (1974) Adenosine-5′-diphosphate and adenosine-5′-monophosphate, in Methods of Enzymatic Analysis, Vol. 4 (Bergmeyer H. U., ed), pp. 2127-2131. Verlag Chemie Academic Press, Weinheim/New York.
    • (1974) Methods of Enzymatic Analysis , vol.4 , pp. 2127-2131
    • Jaworek, D.1    Gruber, W.2    Bergmeyer, H.U.3
  • 44
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R. M., Bossy-Wetzel E., Green D. R., and Newmeyer D. D. (1997) The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 45
    • 0030800033 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the central nervous system: Induction by calcium cycling-dependent and -independent pathways
    • Kristal B. S. and Dubinsky J. M. (1997) Mitochondrial permeability transition in the central nervous system: induction by calcium cycling-dependent and -independent pathways. J. Neurochem. 69, 524-538.
    • (1997) J. Neurochem. , vol.69 , pp. 524-538
    • Kristal, B.S.1    Dubinsky, J.M.2
  • 47
    • 0017344533 scopus 로고
    • Synaptic and nonsynaptic mitochondria from rat brain: Isolation and characterization
    • Lai J. C., Walsh J. M., Dennis S. C., and Clark J. B. (1977) Synaptic and nonsynaptic mitochondria from rat brain: isolation and characterization. J. Neurochem. 28, 625-631.
    • (1977) J. Neurochem. , vol.28 , pp. 625-631
    • Lai, J.C.1    Walsh, J.M.2    Dennis, S.C.3    Clark, J.B.4
  • 48
    • 0028225879 scopus 로고
    • The mitochondrial permeability transition. Interactions of spermine, ADP, and inorganic phosphate
    • Lapidus R. G. and Sokolove P. M. (1994) The mitochondrial permeability transition. Interactions of spermine, ADP, and inorganic phosphate. J. Biol. Chem. 269, 18931-18936.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18931-18936
    • Lapidus, R.G.1    Sokolove, P.M.2
  • 50
    • 0023759935 scopus 로고
    • Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: Importance of the orientation of the nucleotide binding site
    • Le Quoc K. and Le Quoc D. (1988) Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: importance of the orientation of the nucleotide binding site. Arch. Biochem. Biophys. 265, 249-257.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 249-257
    • Le Quoc, K.1    Le Quoc, D.2
  • 52
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C. N., Yang J., Jemmerson R., and Wang X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 54
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., Chittenden T., Lutz R. J., Matsuda H., and Tsujimoto Y. (1998) Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 95, 14681-14686.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 55
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel
    • Nicolli A., Basso E., Petronilli V., Wenger R. M., and Bernardi P. (1996) Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel. J. Biol. Chem. 271, 2185-2192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 56
    • 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. (1992) The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A. J. Biol. Chem. 267, 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
  • 57
    • 0028340683 scopus 로고
    • Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporin A and ADP
    • Novgorodov S. A., Gudz T. I., Brierley G. P., and Pfeiffer D. R. (1994) Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporin A and ADP. Arch. Biochem. Biophys. 311, 219-228.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 219-228
    • Novgorodov, S.A.1    Gudz, T.I.2    Brierley, G.P.3    Pfeiffer, D.R.4
  • 58
    • 0028790583 scopus 로고
    • Peroxynitrite formed by simultaneous nitric oxide and superoxide generation causes cyclosporin-A-sensitive mitochondrial calcium efflux and depolarisation
    • Packer M. A. and Murphy M. P. (1995) Peroxynitrite formed by simultaneous nitric oxide and superoxide generation causes cyclosporin-A-sensitive mitochondrial calcium efflux and depolarisation. Eur. J. Biochem. 234, 231-239.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 231-239
    • Packer, M.A.1    Murphy, M.P.2
  • 59
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino J. G., Chen S. T., Tafani M., Snyder J. W., and Farber J. L. (1998) The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273, 7770-7775.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 60
    • 0021186446 scopus 로고
    • Delayed neuronal recovery and neuronal death in rat hippocampus following severe cerebral ischemia: Possible relationship to abnormalities in neuronal processes
    • Petito C. K. and Pulsinelli W. A. (1984) Delayed neuronal recovery and neuronal death in rat hippocampus following severe cerebral ischemia: possible relationship to abnormalities in neuronal processes. J. Cereb. Blood Flow Metab. 4, 194-205.
    • (1984) J. Cereb. Blood Flow Metab. , vol.4 , pp. 194-205
    • Petito, C.K.1    Pulsinelli, W.A.2
  • 61
    • 0027433653 scopus 로고
    • Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria
    • Petronilli V., Cola C., Massari S., Colonna R., and Bernardi P. (1993) Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria. J. Biol. Chem. 268, 21939-21945.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21939-21945
    • Petronilli, V.1    Cola, C.2    Massari, S.3    Colonna, R.4    Bernardi, P.5
  • 62
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • Petronilli V., Costantini P., Scorrano L., Colonna R., Passamonti S., and Bernardi P. (1994) The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J. Biol. Chem. 269, 16638-16642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 63
    • 0020067965 scopus 로고
    • Temporal profile of neuronal damage in a model of transient forebrain ischemia
    • Pulsinelli W. A., Brierley J. B., and Plum F. (1982) Temporal profile of neuronal damage in a model of transient forebrain ischemia. Ann. Neurol. 11, 491-498.
    • (1982) Ann. Neurol. , vol.11 , pp. 491-498
    • Pulsinelli, W.A.1    Brierley, J.B.2    Plum, F.3
  • 64
    • 0031407680 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in pH-dependent reperfusion injury to rat hepatocytes
    • Qian T., Nieminen A. L., Herman B., and Lemasters J. J. (1997) Mitochondrial permeability transition in pH-dependent reperfusion injury to rat hepatocytes. Am. J. Physiol. 273, C1783-C1792.
    • (1997) Am. J. Physiol. , vol.273
    • Qian, T.1    Nieminen, A.L.2    Herman, B.3    Lemasters, J.J.4
  • 65
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • Rück A., Dolder M., Wallimann T., and Brdiczka D. (1998) Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Lett. 426, 97-101.
    • (1998) FEBS Lett. , vol.426 , pp. 97-101
    • Rück, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 66
    • 0029810095 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a primary event in glutamate neurotoxicity
    • Schinder A. F., Olson E. C., Spitzer N. C., and Montal M. (1996) Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J. Neurosci. 16, 6125-6133.
    • (1996) J. Neurosci. , vol.16 , pp. 6125-6133
    • Schinder, A.F.1    Olson, E.C.2    Spitzer, N.C.3    Montal, M.4
  • 67
    • 0028786786 scopus 로고
    • Developmental changes of the adenine nucleotide translocation in rat brain
    • Schonfeld P. and Bohnensack R. (1995) Developmental changes of the adenine nucleotide translocation in rat brain. Biochim. Biophys. Acta 1232, 75-80.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 75-80
    • Schonfeld, P.1    Bohnensack, R.2
  • 68
    • 0027433539 scopus 로고
    • Increase in the adenine nucleotide translocase protein contributes to the perinatal maturation of respiration in rat liver mitochondria
    • Schonfeld P., Fritz S., Halangk W., and Bohnensack R. (1993) Increase in the adenine nucleotide translocase protein contributes to the perinatal maturation of respiration in rat liver mitochondria. Biochim. Biophys. Acta 1144, 353-358.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 353-358
    • Schonfeld, P.1    Fritz, S.2    Halangk, W.3    Bohnensack, R.4
  • 69
    • 0027418218 scopus 로고
    • Inhibition of T-cell signaling pathways by immunophilin drug complexes: Are side effects inherent to immunosuppressive properties?
    • Schreier M. H., Baumann G., and Zenke G. (1993) Inhibition of T-cell signaling pathways by immunophilin drug complexes: are side effects inherent to immunosuppressive properties? Transplant. Proc. 25, 502-507.
    • (1993) Transplant. Proc. , vol.25 , pp. 502-507
    • Schreier, M.H.1    Baumann, G.2    Zenke, G.3
  • 70
    • 0026446691 scopus 로고
    • Cyclosporin A protects against ischemia-reperfusion injury in the brain
    • Shiga Y., Onodera H., Matsuo Y., and Kogure K. (1992) Cyclosporin A protects against ischemia-reperfusion injury in the brain. Brain Res. 595, 145-148.
    • (1992) Brain Res. , vol.595 , pp. 145-148
    • Shiga, Y.1    Onodera, H.2    Matsuo, Y.3    Kogure, K.4
  • 71
    • 0025471534 scopus 로고
    • Rapid isolation of metabolically active mitochondria from rat brain and subrogions using Percoll density gradient centrifugation
    • Sims N. R. (1990) Rapid isolation of metabolically active mitochondria from rat brain and subrogions using Percoll density gradient centrifugation. J. Neurochem. 55, 698-707.
    • (1990) J. Neurochem. , vol.55 , pp. 698-707
    • Sims, N.R.1
  • 72
    • 0026010158 scopus 로고
    • Selective impairment of respiration in mitochondria isolated from brain subrogions following transient forebrain ischemia in the rat
    • Sims N. R. (1991) Selective impairment of respiration in mitochondria isolated from brain subrogions following transient forebrain ischemia in the rat. J. Neurochem. 56, 1836-1844.
    • (1991) J. Neurochem. , vol.56 , pp. 1836-1844
    • Sims, N.R.1
  • 73
    • 0021225723 scopus 로고
    • The density and distribution of ischemic brain injury in the rat following 2-10 min of forebrain ischemia
    • Smith M. L., Auer R. N., and Siesjö B. K. (1984) The density and distribution of ischemic brain injury in the rat following 2-10 min of forebrain ischemia. Acta Neuropathol (Berl.) 64, 319-332.
    • (1984) Acta Neuropathol (Berl.) , vol.64 , pp. 319-332
    • Smith, M.L.1    Auer, R.N.2    Siesjö, B.K.3
  • 74
    • 0032142911 scopus 로고    scopus 로고
    • Immunophilins in the nervous system
    • Snyder S. H., Lai M. M., and Burnett P. E. (1998) Immunophilins in the nervous system. Neuron 21, 283-294.
    • (1998) Neuron , vol.21 , pp. 283-294
    • Snyder, S.H.1    Lai, M.M.2    Burnett, P.E.3
  • 75
    • 0031940131 scopus 로고    scopus 로고
    • Mitochondrial heterogeneity in the brain at the cellular level
    • Sonnewald U., Hertz L., and Schousboe A. (1998) Mitochondrial heterogeneity in the brain at the cellular level. J. Cereb. Blood Flow Metab. 18, 231-237.
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 231-237
    • Sonnewald, U.1    Hertz, L.2    Schousboe, A.3
  • 76
    • 0014526307 scopus 로고
    • Use of the liquid scintillation spectrometer for determining adenosine triphosphate by the luciferase enzyme
    • Stanley P. E. and Williams S. G. (1969) Use of the liquid scintillation spectrometer for determining adenosine triphosphate by the luciferase enzyme. Anal. Biochem. 29, 381-392.
    • (1969) Anal. Biochem. , vol.29 , pp. 381-392
    • Stanley, P.E.1    Williams, S.G.2
  • 78
    • 0032537608 scopus 로고    scopus 로고
    • Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis
    • Stridh H., Kimland M., Jones D. P., Orrenius S., and Hampton M. B. (1998) Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis. FEBS Lett. 429, 351-355.
    • (1998) FEBS Lett. , vol.429 , pp. 351-355
    • Stridh, H.1    Kimland, M.2    Jones, D.P.3    Orrenius, S.4    Hampton, M.B.5
  • 81
    • 0029590050 scopus 로고
    • Cyclosporin A dramatically ameliorates CA1 hippocampal damage following transient forebrain ischaemia in the rat
    • Uchino H., Elmer E., Uchino K., Lindvall O., and Siesjö B. K. (1995) Cyclosporin A dramatically ameliorates CA1 hippocampal damage following transient forebrain ischaemia in the rat. Acta Physiol. Scand. 155, 469-471.
    • (1995) Acta Physiol. Scand. , vol.155 , pp. 469-471
    • Uchino, H.1    Elmer, E.2    Uchino, K.3    Lindvall, O.4    Siesjö, B.K.5
  • 82
    • 0029788243 scopus 로고    scopus 로고
    • Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure
    • White R. J. and Reynolds I. J. (1996) Mitochondrial depolarization in glutamate-stimulated neurons: an early signal specific to excitotoxin exposure. J. Neurosci. 16, 5688-5697.
    • (1996) J. Neurosci. , vol.16 , pp. 5688-5697
    • White, R.J.1    Reynolds, I.J.2
  • 84
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • Woodfield K., Rück A., Brdiczka D., and Halestrap A. P. (1998) Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochem. J. 336, 287-290.
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.1    Rück, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 85
    • 0032031920 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c
    • Yang J. C. and Cortopassi G. A. (1998) Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c. Free Radical. Biol. Med 24, 624-631.
    • (1998) Free Radical. Biol. Med , vol.24 , pp. 624-631
    • Yang, J.C.1    Cortopassi, G.A.2
  • 86
  • 87
    • 0014429125 scopus 로고
    • A specific and sensitive assay for disulfides
    • Zahler W. L. and Cleland W. W. (1968) A specific and sensitive assay for disulfides. J. Biol. Chem. 243, 716-719.
    • (1968) J. Biol. Chem. , vol.243 , pp. 716-719
    • Zahler, W.L.1    Cleland, W.W.2
  • 88
    • 0028090533 scopus 로고
    • The calcium content of mitochondria from brain subrogions following short-term forebrain ischemia and recirculation in the rat
    • Zaidan E. and Sims N. R. (1994) The calcium content of mitochondria from brain subrogions following short-term forebrain ischemia and recirculation in the rat. J. Neurochem. 63, 1812-1819.
    • (1994) J. Neurochem. , vol.63 , pp. 1812-1819
    • Zaidan, E.1    Sims, N.R.2
  • 90
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M. and Szabo I. (1995) The mitochondrial permeability transition. Biochim. Biophys. Acta 1241, 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.