Ca2+-induced Increased Lipid Packing And Domain Formation In Submitochondrial Particles. A Possible Early Step In The Mechanism Of Ca2+- Stimulated Generation Of Reactive Oxygen Species By The Respiratory Chain

dc.creatorGrijalba M.T.
dc.creatorVercesi A.E.
dc.creatorSchreier S.
dc.date1999
dc.date2015-06-30T15:20:06Z
dc.date2015-11-26T15:25:59Z
dc.date2015-06-30T15:20:06Z
dc.date2015-11-26T15:25:59Z
dc.date.accessioned2018-03-28T22:34:44Z
dc.date.available2018-03-28T22:34:44Z
dc.identifier
dc.identifierBiochemistry. , v. 38, n. 40, p. 13279 - 13287, 1999.
dc.identifier62960
dc.identifier10.1021/bi9828674
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0032589515&partnerID=40&md5=9907f7fad4c945776d4bccec5dfa2aa8
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/100974
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/100974
dc.identifier2-s2.0-0032589515
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1261029
dc.descriptionCa2+ and P(i) accumulation by mitochondria triggers a number of alterations leading to nonspecific increase in inner membrane permeability [Kowaltowski, A. J., et al. (1996) J. Biol. Chem. 271, 29292934]. The molecular nature of the membrane perturbation that precedes oxidative damage is still unknown. EPR spectra of spin probes incorporated in submitochondrial particles (SMP) and in model membranes suggest that Ca2+-cardiolipin (CL) complexation plays an important role. Ca2+-induced lipid domain formation was detected in SMP but not in mitoplasts, in SMP extracted lipids, or in CL- containing liposomes. The results were interpreted in terms of Ca2+ sequestration of CL tightly bound to membrane proteins, in particular the ADP-ATP carrier, and formation of CL-enriched strongly immobilized clusters in lipid shells next to boundary lipid. The in-plane lipid and protein rearrangement is suggested to cause increased reactive oxygen species production in succinate-supplemented, antimycin A-poisoned SMP, favoring the formation of carbon-centered radicals, detected by EPR spin trapping. Removal of tightly bound CL is also proposed to cause protein aggregation, facilitating intermolecular thiol oxidation. Lipid peroxidation was also monitored by the disappearance of the nitroxide EPR spectrum. The decay was faster for nitroxides in a more hydrophobic environment, and was inhibited by butylated hydroxytoluene, by EGTA, or by substituting Mg2+ for Ca2+. In addition, Ca2+ caused an increase in permeability, evidenced by the release of carboxyfluorescein from respiring SMP. The results strongly support Ca2+ binding to CL as one of the early steps in the molecular mechanism of Ca2+- induced nonspecific inner mitochondrial membrane permeabilization.
dc.description38
dc.description40
dc.description13279
dc.description13287
dc.descriptionZoratti, M., Szabò, I., (1995) Biochim. Biophys. Acta, 1241, pp. 139-176
dc.descriptionFagian, M.M., Pereira-Da-Silva, L., Martins, I.S., Vercesi, A.E., (1990) J. Biol. Chem., 265, pp. 19955-19960
dc.descriptionKowaltowski, A.J., Castilho, R.F., Grijalba, M.T., Bechara, E.J.H., Vercesi, A.E., (1996) J. Biol. Chem., 271, pp. 2929-2934
dc.descriptionHalestrap, A.P., Woodfield, K.-Y., Connern, C.P., (1997) J. Biol. Chem., 272, pp. 3346-3354
dc.descriptionVercesi, A.E., Kowaltowski, A.J., Grijalba, M.T., Meinicke, A.R., Castilho, R.F., (1997) Biosci. Rep., 17, pp. 43-52
dc.descriptionKowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1995) Am. J. Physiol., pp. C141-C147
dc.descriptionKowaltowski, A.J., Netto, L.E.S., Vercesi, A.E., (1998) J. Biol. Chem., 273, pp. 12766-12769
dc.descriptionNovgorodov, S.A., Gudz, T.I., Brierley, G.P., Pfeiffer, D.R., (1989) Arch. Biochem. Biophys., 311, pp. 219-228
dc.descriptionAmbrosio, G., Zweier, J.L., Duilio, C., Kuppusamy, P., Santoro, G., Elia, P.P., Trito, I., Flaherty, J.T., (1993) J. Biol. Chem., 268, pp. 18532-18541
dc.descriptionGreene, E.L., Paller, M.S., (1994) Am. J. Physiol., 266, pp. F13-F20
dc.descriptionHarb, J.S., Comte, J., Gautheron, D.C., (1980) Arch. Biochem. Biophys., 208, pp. 305-318
dc.descriptionHoch, F.L., (1992) Biochim. Biophys. Acta, 1113, pp. 71-133
dc.descriptionPowell, G.L., Knowles, P.F., Marsh, D., (1987) Biochemistry, 26, pp. 8138-8145
dc.descriptionBeyer, K., Klingenberg, M., (1985) Biochemistry, 24, pp. 3826-3831
dc.descriptionDe Kruijff, B., Verkleij, A.J., Leunissen-Bijvelt, J., Van Echteld, C.J.A., Hille, J., Rijnbout, H., (1982) Biochim. Biophys. Acta, 693, pp. 1-12
dc.descriptionOhnishi, S., Ito, T., (1974) Biochemistry, 13, pp. 881-887
dc.descriptionHaverstick, D.M., Glaser, M., (1987) Proc. Natl. Acad. Sci. U.S.A., 84, pp. 4475-4479
dc.descriptionLieser, G., Mittler-Nehar, S., Spinke, J., Knoll, W., (1994) Biochim. Biophys. Acta 1192, pp. 14-20
dc.descriptionEdidin, M., (1997) Curr. Opin. Struct. Biol., pp. 582-1532
dc.descriptionBrustovetsky, N., Klingenberg, M., (1996) Biochemistry, 35, pp. 8483-8488
dc.descriptionVercesi, A.E., Reynafarje, B., Lehninger, A.L., (1978) J. Biol. Chem., 253, pp. 6379-6385
dc.descriptionBeltran, C., Gomez-Puyou, M.T., Darzon, A., Gomez-Puyou, A., (1986) Eur. J. Biochem., 160, pp. 163-168
dc.descriptionRouser, G., Fleischer, S., Yamamoto, A., (1970) Lipids, 5, pp. 494-496
dc.descriptionLowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.S., (1951) J. Biol. Chem., 193, pp. 265-275
dc.descriptionFolch, J., Lees, M., Sloane-Stanley, G.H., (1957) J. Biol. Chem., 226, pp. 497-501
dc.descriptionHubbell, W.L., McConnell, H.M., (1971) J. Am. Chem. Soc., 93, pp. 314-326
dc.descriptionSchreier, S., Polnaszek, C.F., Smith, I.C.P., (1978) Biochim. Biophys. Acta, 515, pp. 375-436
dc.descriptionFrezzatti W.A., Jr., Toselli, W.R., Schreier, S., (1986) Biochim. Biophys. Acta, 860, pp. 531-538
dc.descriptionGrijalba, M.T., Andrade, B.A., Meinicke, A.R., Castilho, R.F., Vercesi, A.E., Schreier, S., (1998) Free Radical Res., 28, pp. 301-318
dc.descriptionSchreier, S., Marsh, D., Smith, I.C.P., (1976) Arch. Biochem. Biophys., 172, pp. 1-11
dc.descriptionJost, P.C., Griffith, O.H., Capaldi, R.A., Vanderkooi, G., (1973) Proc. Natl. Acad. Sci. U.S.A., 70, pp. 480-484
dc.descriptionKoltover, V.K., Reichman, L.M., Yasaitis, A.A., Blumenfeld, L.A., (1971) Biochim. Biophys. Acta, 234, pp. 306-310
dc.descriptionCadenas, E.A., Boveris, A., Ragan, C.I., Stoppani, A.O.M., (1977) Arch. Biochem. Biophys., 180, pp. 248-257
dc.descriptionGiulivi, C., Boveris, A., Cadenas, E., (1995) Arch. Biochem. Biophys., 316, pp. 909-916
dc.descriptionBoveris, A., Cadenas, E.A., Stoppani, A.O.M., (1976) Biochem. J., 156, pp. 435-444
dc.descriptionRadi, R., Sims, S., Cassina, A., Turrens, J.F., (1993) Free Radical Biol. Med., 15, pp. 653-659
dc.descriptionArroyo, C.M., Kramer, J.H., Dickens, B.F., Weglicki, W.B., (1987) FEBS Lett., 221, pp. 101-104
dc.descriptionMakino, K., Imaishi, H., Morinishi, S., Takeuchi, T., Fujita, Y., (1986) Biochem. Biophys. Res. Commun., 141, pp. 381-386
dc.descriptionKillian, J.A., Koorengevel, M.C., Bouwstra, J.A., Gooris, G., Dowhan, W., De Kruijff, B., (1994) Biochim. Biophys. Acta, 1189, pp. 225-232
dc.descriptionMittler-Neher, S., Knoll, W., (1993) Biochim. Biophys. Acta, 1152, pp. 259-269
dc.descriptionCable, M.B., Powell, G.L., (1980) Biochemistry, 19, pp. 5679-5686
dc.descriptionSmaal, E.S., Schreuder, C., Van Baal, J.B., Tijburg, P.N.M., Mandersloot, J.G., De Kruijff, B.A., De Gier, J., (1987) Biochim. Biophys. Acta, 897, pp. 191-196
dc.descriptionDe Kruijff, B., Nayar, R., Cullis, P.R., (1982) Biochim. Biophys. Acta, 684, pp. 47-52
dc.descriptionTaraschi, T.F., De Kruijff, B.A., Verkleij, A.J., (1983) Eur. J. Biochem., 129, pp. 621-625
dc.descriptionKnowles, P., Watts, A., Marsh, D., (1979) Biochemistry, 18, pp. 4480-4487
dc.descriptionMarsh, D., Watts, A., Maschke, W., Knowles, P., (1978) Biochem. Biophys. Res. Commun., 81, pp. 397-402
dc.descriptionKleinschmidt, J., Powell, G.L., Marsh, D., (1998) Biochemistry, 37, pp. 11579-11585
dc.descriptionMahaney, J.E., Kleinschmidt, J., Marsh, D., Thomas, D.D., (1992) Biophys. J., 63, pp. 1513-1522
dc.descriptionTrumpower, B.L., (1990) J. Biol. Chem., 265, pp. 11409-11412
dc.descriptionTurrens, J.F., Alexander, A., Lehninger, A.L., (1986) Arch. Biochem. Biophys., 237, pp. 408-414
dc.descriptionSkulachev, V.P., (1996) FEBS Lett., 397, pp. 7-10
dc.descriptionZhang, L., Yu, L., Yu, C.-A., (1998) J. Biol. Chem., 273, pp. 33972-33976
dc.descriptionNohl, H., Jordan, W., (1986) Biochem. Biophys. Res. Commun., 138, pp. 533-539
dc.descriptionVerstraeten, S.V., Nogueira, L.V., Schreier, S., Oteiza, P.I., (1997) Arch. Biochem. Biophys., 338, pp. 121-127
dc.languageen
dc.publisher
dc.relationBiochemistry
dc.rightsfechado
dc.sourceScopus
dc.titleCa2+-induced Increased Lipid Packing And Domain Formation In Submitochondrial Particles. A Possible Early Step In The Mechanism Of Ca2+- Stimulated Generation Of Reactive Oxygen Species By The Respiratory Chain
dc.typeArtículos de revistas


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