메뉴 건너뛰기




Volumn 212, Issue 3, 2006, Pages 199-210

Selective cytochrome c displacement by phosphate and Ca2+ in brain mitochondria

Author keywords

Brain mitochondria; Cardiolipin; Cytochrome c; Liposome; Mitochondrial membrane potential

Indexed keywords

BROMINE DERIVATIVE; CALCIUM ION; CARDIOLIPIN; CHOLINE DERIVATIVE; CYTOCHROME C; CYTOCHROME C OXIDASE; LIPOSOME; PHOSPHATE; SULFONIC ACID DERIVATIVE;

EID: 33947095425     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-006-0015-4     Document Type: Article
Times cited : (5)

References (52)
  • 1
    • 0031788661 scopus 로고    scopus 로고
    • Cytochrome c release from brain mitochondria is independent of the mitochondrial permeability transition
    • Andreyev, A.Y., Fahy, B., Fiskum, G. 1998. Cytochrome c release from brain mitochondria is independent of the mitochondrial permeability transition. FEBS Lett. 439:373-376
    • (1998) FEBS Lett , vol.439 , pp. 373-376
    • Andreyev, A.Y.1    Fahy, B.2    Fiskum, G.3
  • 2
    • 0034711236 scopus 로고    scopus 로고
    • Cytochrome c is released from mitochondria in a reactive oxygen species (ROS)-dependent fashion and can operate as a ROS scavenger and as a respiratory substrate in cerebellar neurons undergoing excitotoxic death
    • Atlante, A., Calissano, P., Bobba, A., Azzariti, A., Marra, E., Passarella, S. 2000. Cytochrome c is released from mitochondria in a reactive oxygen species (ROS)-dependent fashion and can operate as a ROS scavenger and as a respiratory substrate in cerebellar neurons undergoing excitotoxic death. J. Biol. Chem 275:37159-37166
    • (2000) J. Biol. Chem , vol.275 , pp. 37159-37166
    • Atlante, A.1    Calissano, P.2    Bobba, A.3    Azzariti, A.4    Marra, E.5    Passarella, S.6
  • 3
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G.R. 1959. Phosphorus assay in column chromatography J. Biol. Chem. 234:466-468
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 4
    • 0019888247 scopus 로고
    • Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes
    • Bernardi, P., Azzone, G.F. 1981. Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes. J. Biol. Chem. 256:7187-7192
    • (1981) J. Biol. Chem , vol.256 , pp. 7187-7192
    • Bernardi, P.1    Azzone, G.F.2
  • 6
    • 0036313059 scopus 로고    scopus 로고
    • Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane
    • Brustovetsky, N., Brustovetsky, T., Jemmerson, R., Dubinsky, J.M. 2002. Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane. J. Neurochem. 80:207-218
    • (2002) J. Neurochem , vol.80 , pp. 207-218
    • Brustovetsky, N.1    Brustovetsky, T.2    Jemmerson, R.3    Dubinsky, J.M.4
  • 8
    • 0032485854 scopus 로고    scopus 로고
    • Multiple conformations of physiological membrane-bound cytochrome c
    • Cortese, J.D., Voglino, A.L., Hackenbrock, C.R. 1998. Multiple conformations of physiological membrane-bound cytochrome c.. Biochemistry 37:6402-6409
    • (1998) Biochemistry , vol.37 , pp. 6402-6409
    • Cortese, J.D.1    Voglino, A.L.2    Hackenbrock, C.R.3
  • 9
    • 0030057708 scopus 로고    scopus 로고
    • Functional heterogeneity of an isolated mitochondrial population revealed by cytofluorometric analysis at the single organelle level
    • Cossarizza, A., Ceccarelli, D., Masini, A. 1996. Functional heterogeneity of an isolated mitochondrial population revealed by cytofluorometric analysis at the single organelle level. Exp. Cell Res. 222:84-94
    • (1996) Exp. Cell Res , vol.222 , pp. 84-94
    • Cossarizza, A.1    Ceccarelli, D.2    Masini, A.3
  • 10
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. 1999. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341:233-249
    • (1999) Biochem. J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 12
    • 0023807789 scopus 로고
    • Synthesis of cardiolipin derivatives with protection of the free hydroxyl: Its application to the study of cardiolipin stimulation of cytochrome c oxidase
    • Dale, M.P., Robinson, N.C. 1988. Synthesis of cardiolipin derivatives with protection of the free hydroxyl: Its application to the study of cardiolipin stimulation of cytochrome c oxidase. Biochemistry 27:8270-8275
    • (1988) Biochemistry , vol.27 , pp. 8270-8275
    • Dale, M.P.1    Robinson, N.C.2
  • 13
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes. Biochemistry 24:3099-3106
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 15
    • 0017253440 scopus 로고
    • Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase
    • Ferguson-Miller, S., Brautigan, D.L., Margoliash, E. 1976. Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase J. Biol. Chem. 251:1104-1115
    • (1976) J. Biol. Chem , vol.251 , pp. 1104-1115
    • Ferguson-Miller, S.1    Brautigan, D.L.2    Margoliash, E.3
  • 16
    • 0035861553 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor blocks the mitochondrial pathway of apoptosis signaling in breast cancer cells
    • Gao, M., Fan, S., Goldberg, I.D., Laterra, J., Kitsis, R.N., Rosen, E.M. 2001. Hepatocyte growth factor/scatter factor blocks the mitochondrial pathway of apoptosis signaling in breast cancer cells. J. Biol. Chem. 276:47257-47265
    • (2001) J. Biol. Chem , vol.276 , pp. 47257-47265
    • Gao, M.1    Fan, S.2    Goldberg, I.D.3    Laterra, J.4    Kitsis, R.N.5    Rosen, E.M.6
  • 17
    • 0025113386 scopus 로고
    • Structure-function studies of adenine nucleotide transport in mitochondria. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast
    • Gawaz, M., Douglas, M.G., Klingemberg, M. 1990. Structure-function studies of adenine nucleotide transport in mitochondria. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast. J. Biol. Chem. 265:14202-14208
    • (1990) J. Biol. Chem , vol.265 , pp. 14202-14208
    • Gawaz, M.1    Douglas, M.G.2    Klingemberg, M.3
  • 18
    • 0032787283 scopus 로고    scopus 로고
    • Structure of cytochrome c complexes with phospholipids as revealed by resonance energy transfer
    • Gorbenko, G.P. 1999. Structure of cytochrome c complexes with phospholipids as revealed by resonance energy transfer. Biochim. Biophys. Acta 1420:1-13
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 1-13
    • Gorbenko, G.P.1
  • 19
    • 0037466114 scopus 로고    scopus 로고
    • Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: Resonance energy transfer study
    • Gorbenko, G.P., Domanov, Y.A. 2003. Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: Resonance energy transfer study. Biophys. Chem. 103:239-249
    • (2003) Biophys. Chem , vol.103 , pp. 239-249
    • Gorbenko, G.P.1    Domanov, Y.A.2
  • 20
    • 0035437866 scopus 로고    scopus 로고
    • Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis
    • Guégan, C., Vila, M., Rosoklija, G., Hays, A.P., Przedborski, S. 2001. Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis. J. Neurosci. 21:6569-6576
    • (2001) J. Neurosci , vol.21 , pp. 6569-6576
    • Guégan, C.1    Vila, M.2    Rosoklija, G.3    Hays, A.P.4    Przedborski, S.5
  • 22
    • 0345832111 scopus 로고    scopus 로고
    • Cardiolipin is not required for Bax-mediated cytochrome c release from yeast mitochondria
    • Iverson, S.L., Enoksson, M., Gogvadze, V., Ott, M., Orrenius, S. 2004. Cardiolipin is not required for Bax-mediated cytochrome c release from yeast mitochondria. J. Biol. Chem. 279:1100-1107
    • (2004) J. Biol. Chem , vol.279 , pp. 1100-1107
    • Iverson, S.L.1    Enoksson, M.2    Gogvadze, V.3    Ott, M.4    Orrenius, S.5
  • 23
    • 0001497483 scopus 로고
    • The reversible removal of cytochrome c from mitochondria
    • Jacobs, E.E., Sanadi, D.R. 1960. The reversible removal of cytochrome c from mitochondria. J. Biol. Chem. 235:531-534
    • (1960) J. Biol. Chem , vol.235 , pp. 531-534
    • Jacobs, E.E.1    Sanadi, D.R.2
  • 26
    • 0022382612 scopus 로고
    • Difference in some of the metabolic properties of mitochondria isolated from cerebral cortex and olfactory bulb of the rat
    • Lai, J.C.K., Rex Sheu, K.F., Carlson, K.C. Jr. 1985. Difference in some of the metabolic properties of mitochondria isolated from cerebral cortex and olfactory bulb of the rat. Brain Res. 343:52-59
    • (1985) Brain Res , vol.343 , pp. 52-59
    • Lai, J.C.K.1    Rex Sheu, K.F.2    Carlson Jr., K.C.3
  • 27
    • 0035861589 scopus 로고    scopus 로고
    • Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization
    • Lam, M., Oleinick, N.L., Nieminen, A.L. 2001. Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization. J. Biol Chem. 276:47379-47386
    • (2001) J. Biol Chem , vol.276 , pp. 47379-47386
    • Lam, M.1    Oleinick, N.L.2    Nieminen, A.L.3
  • 29
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton, S.A., Rosenberg, P.A. 1994. Excitatory amino acids as a final common pathway for neurologic disorders. N. Engl. J. Med. 330:613-622
    • (1994) N. Engl. J. Med , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 30
    • 1942536490 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios
    • Maneg, O., Malatesta, F., Ludwig, B., Drosou, V. 2004. Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios. Biochim. Biophys. Acta 1655:274-281
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 274-281
    • Maneg, O.1    Malatesta, F.2    Ludwig, B.3    Drosou, V.4
  • 31
    • 0033985059 scopus 로고    scopus 로고
    • Respiratory rate and phosphatidylserine import in brain mitochondria in vitro
    • Monni, M., Corazzi, L., Migliorati, G., Roberti, R. 2000. Respiratory rate and phosphatidylserine import in brain mitochondria in vitro. J. Membr. Biol. 173:97-105
    • (2000) J. Membr. Biol , vol.173 , pp. 97-105
    • Monni, M.1    Corazzi, L.2    Migliorati, G.3    Roberti, R.4
  • 32
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya, E.M., Bowling, A.C., Beal, M.F. 1994. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63:2179-2184
    • (1994) J. Neurochem , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 33
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls, D.G., Budd, S.L. 2000. Mitochondria and neuronal survival. Physiol. Rev. 80:315-360
    • (2000) Physiol. Rev , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 34
    • 10244257617 scopus 로고    scopus 로고
    • The integration of mitochondrial calcium transport and storage
    • Nicholls, D.G., Chalmers, S. 2004. The integration of mitochondrial calcium transport and storage. J. Bioenerg. Biomembr. 36:277-281
    • (2004) J. Bioenerg. Biomembr , vol.36 , pp. 277-281
    • Nicholls, D.G.1    Chalmers, S.2
  • 35
    • 0021994643 scopus 로고
    • Effects of Adriamycin on lipid polymorphism in cardiolipin containing model and mitochondrial membranes
    • Nicolay, K., van der Neut, R., Fok, J.J., de Kruijff, B. 1985. Effects of Adriamycin on lipid polymorphism in cardiolipin containing model and mitochondrial membranes. Biochim. Biophys. Acta 819:55-65
    • (1985) Biochim. Biophys. Acta , vol.819 , pp. 55-65
    • Nicolay, K.1    van der Neut, R.2    Fok, J.J.3    de Kruijff, B.4
  • 36
    • 0035851186 scopus 로고    scopus 로고
    • Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis
    • Ostrander, D.B., Sparagna, G.C., Amoscato, A.A., McMillin, J.B., Dowhan, W. 2001. Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis. J. Biol. Chem. 276:38061-38067
    • (2001) J. Biol. Chem , vol.276 , pp. 38061-38067
    • Ostrander, D.B.1    Sparagna, G.C.2    Amoscato, A.A.3    McMillin, J.B.4    Dowhan, W.5
  • 38
    • 1642361233 scopus 로고    scopus 로고
    • Binding and release of cytochrome c in brain mitochondria is influenced by membrane potential and hydrophobic interactions with cardiolipin
    • Piccotti, L., Buratta, M., Giannini, S., Gresele, P., Roberti, R., Corazzi, L. 2004a. Binding and release of cytochrome c in brain mitochondria is influenced by membrane potential and hydrophobic interactions with cardiolipin. J. Membr. Biol. 198:43-53
    • (2004) J. Membr. Biol , vol.198 , pp. 43-53
    • Piccotti, L.1    Buratta, M.2    Giannini, S.3    Gresele, P.4    Roberti, R.5    Corazzi, L.6
  • 39
    • 0037023702 scopus 로고    scopus 로고
    • Exogenous phospholipids specifically affect transmembrane potential of brain mitochondria and cytochrome c release
    • Piccotti, L., Marchetti, C., Migliorati, G., Roberti, R., Corazzi, L. 2002. Exogenous phospholipids specifically affect transmembrane potential of brain mitochondria and cytochrome c release. J. Biol. Chem. 277:12075-12081
    • (2002) J. Biol. Chem , vol.277 , pp. 12075-12081
    • Piccotti, L.1    Marchetti, C.2    Migliorati, G.3    Roberti, R.4    Corazzi, L.5
  • 40
    • 17144422065 scopus 로고    scopus 로고
    • NAO as a probe for cardiolipin in mitochondria: Study of changes in fluorescence emission spectra [abstract]
    • Piccotti, L., Mileykovskaya, E., Haines, T.H., Dowhan, W. 2004b. NAO as a probe for cardiolipin in mitochondria: Study of changes in fluorescence emission spectra [abstract]. Biochim. Biophys Acta 1658:(Suppl. S)261
    • (2004) Biochim. Biophys Acta , vol.1658 , Issue.SUPPL. S , pp. 261
    • Piccotti, L.1    Mileykovskaya, E.2    Haines, T.H.3    Dowhan, W.4
  • 41
    • 0035469830 scopus 로고    scopus 로고
    • Rapid extracellular release of cytochrome c is specific for apoptosis and marks cell death in vivo
    • Renz, A., Berdel, W.E., Kreuter, M., Belka, C., Schulze-Osthoff, K., Los, M. 2001. Rapid extracellular release of cytochrome c is specific for apoptosis and marks cell death in vivo. Blood 98:1542-1548
    • (2001) Blood , vol.98 , pp. 1542-1548
    • Renz, A.1    Berdel, W.E.2    Kreuter, M.3    Belka, C.4    Schulze-Osthoff, K.5    Los, M.6
  • 42
    • 0035292649 scopus 로고    scopus 로고
    • 2+ thresholds determine cytochrome c release or permeability transition pore opening in brain mitochondria
    • 2+ thresholds determine cytochrome c release or permeability transition pore opening in brain mitochondria. FASEB J. 15:565-567
    • (2001) FASEB J , vol.15 , pp. 565-567
    • Schild, L.1    Keilhoff, G.2    Augustin, W.3    Reiser, G.4    Striggow, F.5
  • 43
    • 0033539647 scopus 로고    scopus 로고
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure. Biochemistry 38:14966-14972
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlak, E.1    Robinson, N.C.2
  • 44
    • 0006847485 scopus 로고
    • Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation
    • Szoka, F., Jr., Papahadjopoulos, D. 1978. Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation. Proc. Natl. Acad. Sci. USA 75:4194-4198
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4194-4198
    • Szoka Jr., F.1    Papahadjopoulos, D.2
  • 45
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction. Evidence for the extended lipid anchorage
    • Tuominen, E.K.J., Wallace, C.J.A., Kinnunen, P.K.J. 2002. Phospholipid-cytochrome c interaction. Evidence for the extended lipid anchorage. J. Biol. Chem. 277:8822-8826
    • (2002) J. Biol. Chem , vol.277 , pp. 8822-8826
    • Tuominen, E.K.J.1    Wallace, C.J.A.2    Kinnunen, P.K.J.3
  • 46
    • 0020489067 scopus 로고
    • Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study
    • Van Venetie, R., Verkleij, A.J. 1982. Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study. Biochim. Biophys. Acta 692:397-405
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 397-405
    • Van Venetie, R.1    Verkleij, A.J.2
  • 47
    • 18144427184 scopus 로고    scopus 로고
    • 2+-induced permeabilization promotes free radicals release from rat brain mitochondria with partially inhibited complex I
    • 2+-induced permeabilization promotes free radicals release from rat brain mitochondria with partially inhibited complex I. J. Neurochem. 93:526-537
    • (2005) J. Neurochem , vol.93 , pp. 526-537
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 48
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. 2001. The expanding role of mitochondria in apoptosis. Genes Dev. 15:2922-2933
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 49
    • 0035823503 scopus 로고    scopus 로고
    • Defective cytochrome c-dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity
    • Wolf, B.B., Schuler, M., Li, W., Eggers-Sedlet, B., Lee, W., Tailor, P., Fitzgerald, P., Mills, G.B., Green, D.R. 2001. Defective cytochrome c-dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity. J. Biol. Chem. 276:34244-34251
    • (2001) J. Biol. Chem , vol.276 , pp. 34244-34251
    • Wolf, B.B.1    Schuler, M.2    Li, W.3    Eggers-Sedlet, B.4    Lee, W.5    Tailor, P.6    Fitzgerald, P.7    Mills, G.B.8    Green, D.R.9
  • 51
    • 0030830677 scopus 로고    scopus 로고
    • Cytochrome oxidase in Alzheimer's disease: Biochemical, histochemical, and immunohistochemical analyses of the visual and other systems
    • Wong-Riley, M., Antuono, P., Ho, K.C., Egan, R., Hevner, R., Liebl, W., Huang, Z., Rachel, R., Jones, J. 1997. Cytochrome oxidase in Alzheimer's disease: Biochemical, histochemical, and immunohistochemical analyses of the visual and other systems. Vision Res. 37:3593-3608
    • (1997) Vision Res , vol.37 , pp. 3593-3608
    • Wong-Riley, M.1    Antuono, P.2    Ho, K.C.3    Egan, R.4    Hevner, R.5    Liebl, W.6    Huang, Z.7    Rachel, R.8    Jones, J.9
  • 52
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • Zhang, M., Mileykovskaya, E., Dowhan, W. 2002. Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane. J. Biol. Chem. 277:43553-43556
    • (2002) J. Biol. Chem , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.