805 research outputs found
Scintillating-fibre calorimetry
No full textLavoro di rassegna sulla calorimetria a fibre scintillant
Mitochondrial Permeability Transition And Oxidative Stress
No full textMitochondrial permeability transition (MPT) is a non-selective inner membrane permeabilization that may precede necrotic and apoptotic cell death. Although this process has a specific inhibitor, cyclosporin A, little is known about the nature of the proteinaceous pore that results in MPT. Here, we review data indicating that MPT is not a consequence of the opening of a pre-formed pore, but the consequence of oxidative damage to pre-existing membrane proteins. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.4951-21215Liu, X., Kim, C.N., Yang, J., Jemmerson, R., Wang, X., (1996) Cell, 86, pp. 147-157Susin, S.A., Zamzami, N., Castedo, M., Hirsch, T., Marchetti, P., Macho, A., Daugas, E., Kroemer, G., (1996) J. Exp. Med., 184, pp. 1331-1341Green, D.R., Reed, J.C., (1998) Science, 281, pp. 1309-1312Skulachev, V.P., (1998) FEBS Lett., 423, pp. 275-280Kroemer, G., (1999) Biochem. Soc. Symp., 66, pp. 1-15Zoratti, M., Szabò, I., (1995) Biochim. Biophys. Acta, 1241, pp. 139-176Kowaltowski, A.J., Vercesi, A.E., (1999) Free Radic. Biol. Med., 26, pp. 463-471Castilho, R.F., Kowaltowski, A.J., Vercesi, A.E., (1996) J. Bioenerg. Biomembr., 28, pp. 523-529Fagian, M.M., Pereira-da-Silva, L., Martins, I.S., Vercesi, A.E., (1990) J. Biol. Chem., 265, pp. 19955-19960Vercesi, A.E., (1984) Biochem. Biophys. Res. Commun., 119, pp. 305-310Brustovetsky, N., Klingenberg, M., (1996) Biochemistry, 35, pp. 8483-8488Brdiczka, D., Beutner, G., Ruck, A., Dolder, M., Wallimann, T., (1998) Biofactors, 8, pp. 235-242Halestrap, A.P., (1999) Biochem. Soc. Symp., 66, pp. 181-203Lehninger, A.L., Vercesi, A.E., Bababunmi, E.A., (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 1690-1694Hunter, D.R., Haworth, R.A., (1979) Arch. Biochem. Biophys., 195, pp. 453-459Lotscher, H.R., Winterhalter, K.H., Carafoli, E., Richter, C., (1980) J. Biol. Chem., 255, pp. 9325-9330Jurkowitz, M.S., Geisbuhler, T., Jung, D.W., Brierley, G.P., (1983) Arch. Biochem. Biophys., 223, pp. 120-128Vercesi, A.E., (1987) Arch. Biochem. Biophys., 252, pp. 171-178Byrne, A.M., Lemasters, J.J., Nieminen, A.L., (1999) Hepatology, 29, pp. 1523-1531Zago, E.B., Castilho, R.F., Vercesi, A.E., (2000) FEBS Lett., 478, pp. 29-33Bernardes, C.F., Meyer-Fernandes, J.R., Basseres, D.S., Castilho, R.F., Vercesi, A.E., (1994) Biochim. Biophys. Acta, 1188, pp. 93-100Hoek, J.B., Rydstrom, J., (1988) Biochem. J., 254, pp. 1-10Kowaltowski, A.J., Vercesi, A.E., (2000) Mitochondria in Pathogenesis, , (Lemasters, J.J. and Nieminen A.-L., Eds.), Plenum, New York, in pressGardner, P.R., Fridovich, I., (1991) J. Biol. Chem., 266, pp. 19328-19333Skulachev, V.P., (1997) Biosci. Rep., 17, pp. 347-366Peng, C.F., Straub, K.D., Kane, J.J., Murphy, M.L., Wadkins, C.L., (1977) Biochim. Biophys. Acta, 462, pp. 403-413Bernardi, P., Azzone, G.F., (1983) Eur. J. Biochem., 134, pp. 377-383Catisti, R., Vercesi, A.E., (1999) FEBS Lett., 464, pp. 97-101Kowaltowski, A.J., Vercesi, A.E., Fiskum, G., (2000) Cell Death Differ., 7, pp. 903-910Korshunov, S.S., Skulachev, V.P., Starkov, A.A., (1997) FEBS Lett., 416, pp. 15-18Skulachev, V.P., (1998) Biochim. Biophys. Acta, 1363, pp. 100-124Le Quoc, D., Le Quoc, K., Gaudemer, Y., (1976) Biochem. Biophys. Res. Commun., 68, pp. 106-113Harris, E.J., Baum, H., (1980) Biochem. J., 186, pp. 725-732Vercesi, A.E., Ferraz, V.L., Macedo, D.V., Fiskum, G., (1988) Biochem. Biophys. Res. Commun., 154, pp. 934-941Valle, V.G., Fagian, M.M., Parentoni, L.S., Meinicke, A.R., Vercesi, A.E., (1993) Arch. Biochem. Biophys., 307, pp. 1-7Siliprandi, D., Scutari, G., Zoccarato, F., Siliprandi, N., (1974) FEBS Lett., 42, pp. 197-199Lenartowicz, E., Bernardi, P., Azzone, G.F., (1991) J. Bioenerg. Biomembr., 23, pp. 679-688Costantini, P., Chernyak, B.V., Petronilli, V., Bernardi, P., (1996) J. Biol. Chem., 271, pp. 6746-6751Castilho, R.F., Kowaltowski, A.J., Meinicke, A.R., Bechara, E.J., Vercesi, A.E., (1995) Free Radic. Biol. Med., 18, pp. 479-486Costantini, P., Belzacq, A.S., Vieira, H.L., Larochette, N., De Pablo, M.A., Zamzami, N., Susin, S.A., Kroemer, G., (2000) Oncogene, 19, pp. 307-314Kowaltowski, A.J., Castilho, R.F., Grijalba, M.T., Bechara, E.J., Vercesi, A.E., (1996) J. Biol. Chem., 271, pp. 2929-2934Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1996) FEBS Lett., 378, pp. 150-152Kowaltowski, A.J., Netto, L.E., Vercesi, A.E., (1998) J. Biol. Chem., 273, pp. 12766-12769Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1995) Am. J. Physiol., 269, pp. C141-C147Scorrano, L., Petronilli, V., Bernardi, P., (1997) J. Biol. Chem., 272, pp. 12295-12299Kuzminova, A.E., Zhuravlyova, A.V., Vyssokikh, M.Yu., Zorova, L.D., Krasnikov, B.F., Zorov, D.B., (1998) FEBS Lett., 434, pp. 313-316Frei, B., Winterhalter, K.H., Richter, C., (1985) J. Biol. 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Neurosci., 18, pp. 205-213Fujimura, M., Morita-Fujimura, Y., Noshita, N., Sugawara, T., Kawase, M., Chan, P.H., (2000) J. Neurosci., 20, pp. 2817-2824Voehringer, D.W., Hirschberg, D.L., Xiao, J., Lu, Q., Roederer, M., Lock, C.B., Herzenberg, L.A., Herzenberg, L.A., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 2680-2685Petersen, A., Castilho, R.F., Hansson, O., Wieloch, T., Brundin, P., (2000) Brain Res., 857, pp. 20-29Nieminen, A.L., Byrne, A.M., Herman, B., Lemasters, J.J., (1997) Am. J. Physiol., 272, pp. C1286-C1294Dhanbhoora, C.M., Babson, J.R., (1992) Arch. Biochem. Biophys., 293, pp. 130-139Ghibelli, L., Coppola, S., Fanelli, C., Rotilio, G., Civitareale, P., Scovassi, A.I., Ciriolo, M.R., (1999) FASEB J., 13, pp. 2031-2036Yang, C.F., Shen, H.M., Ong, C.N., (2000) Arch. Biochem. Biophys., 380, pp. 319-330Skulachev, V.P., (1999) Mol. Asp. Med., 20, pp. 139-18
Level 1 Muon Trigger Simulation in the Barrel Region
No full textLevel 1 Muon Trigger Simulation in the Barrel Regio
The Thiol-specific Antioxidant Enzyme Prevents Mitochondrial Permeability Transition: Evidence For The Participation Of Reactive Oxygen Species In This Mechanism
No full textMitochondrial swelling and membrane protein thiol oxidation associated with mitochondrial permeability transition induced by Ca2+ and inorganic phosphate are inhibited in a dose-dependent manner either by catalase, the thiol-specific antioxidant enzyme (TSA), a protein recently demonstrated to present thiol peroxidase activity, or ebselen, a selenium-containing heterocycle which also possesses thiol peroxidase activity. This inhibition of mitochondrial permeability transition is due to the removal of mitochondrial-generated H2O2 which can easily diffuse to the extramitochondrial space. Whereas ebselen required the presence of reduced glutathione as a reductant to grant its protective effect, TSA was fully reduced by mitochondrial components. Decrease in the oxygen concentration of the reaction medium also inhibits mitochondrial permeabilization and membrane protein thiol oxidation, in a concentration-dependent manner. The results presented in this report confirm that mitochondrial permeability transition induced by Ca2+ and inorganic phosphate is reactive oxygen species- dependent. The possible importance of TSA as an intracellular antioxidant, avoiding the onset of mitochondrial permeability transition, is discussed in the text.273211276612769Gunter, T.E., Gunter, K.K., Sheu, S.-S., Gavin, C.E., (1994) Am. J. Physiol., 267, pp. C313-C339Zoratti, M., Szabó, I., (1995) Biochim. Blophys. Acta, 1241, pp. 139-176Lehninger, A.L., Vercesi, A.E., Bababunmi, E.A., (1978) Proc. Natl. Acad. Sci. U. S. A., 79, pp. 6842-6846Vercesi, A.E., Kowaltowski, A.J., Grijalba, M.T., Meinicke, A.R., Castilho, R.F., (1997) Biosci. Rep., 17, pp. 43-52Castilho, R.F., Kowaltowski, A.J., Meinicke, A.R., Vercesi, A.E., (1995) Free Radical Biol. & Med., 18, pp. 479-486Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1995) Am. J. Physiol., 269, pp. C141-C147Valle, V.G.R., Fagian, M.M., Parentoni, L.S., Meinicke, A.R., Vercesi, A.E., (1993) Arch. Biockem. Biophys., 307, pp. 1-7Kowaltowski, A.J., Castilho, R.F., Vercesi, A.E., (1996) FEBS Lett., 378, pp. 150-152Kowaltowski, A.J., Castilho, R.F., Grijalba, M.T., Bechara, E.J.H., Vercesi, A.E., (1996) J. Biol. Chem., 271, pp. 2929-2934Fagian, M.M., Pereira-da-Silva, L., Martins, I.S., Vercesi, A.E., (1990) J. Biol. Chem., 265, pp. 19955-19960Castilho, R.F., Kowaltowski, A.J., Vercesi, A.E., (1996) J. Bioenerg. Biomembr., 28, pp. 523-529Scorrano, L., Petronilli, V., Bernardi, P., (1997) J. Biol. Chem., 272, pp. 12295-12299Pastorino, J.G., Snyder, J.W., Serroni, A., Hoek, J.B., Farber, J.L., (1993) J. Biol. Chem., 268, pp. 13791-13798Griffiths, E., Halestrap, A.P., (1995) Biochem. J., 307, pp. 93-98Zamzami, N., Hirsch, T., Dallaporta, B., Petit, P.X., Kroemer, G., (1997) J. Bioenerg. Biomembr., 29, pp. 185-193Skulachev, V.P., (1996) FEBS Lett., 397, pp. 7-10Kim, K., Kim, I.H., Lee, K.-Y., Rhee, S.G., Stadtman, E.R., (1988) J. Biol. Chem., 263, pp. 4704-4711Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., Rhee, S.G., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 7017-7021Chae, H.Z., Chung, S.J., Rhee, S.G., (1994) J. Biol. Chem., 269, pp. 27670-27678Netto, L.E.S., Chae, H.Z., Kang, S.-W., Rhee, S.G., Stadtman, E.R., (1996) J. Biol. Chem., 271, pp. 15315-15321Nogoceke, E., Gommel, D.U., Kieb, M., Kalisz, H.M., Flohé, L., (1997) Biol. Chem., 378, pp. 827-836Kim, I.H., Kim, K., Rhee, S.G., (1989) Proc. Natl. Acad. Sci. U. S. A., 86, pp. 6018-6022Watabe, S., Kohno, H., Kouyama, H., Hiroi, T., Yago, N., Nakazawa, T., (1994) J. Biochem. (Tokyo), 115, pp. 648-654Ishii, T., Kawane, T., Taketani, S., Bannai, S., (1995) Biochem. Biophys. Res. Commun., 216, pp. 970-975Sies, H., (1993) Free Radical Biol. & Med., 14, pp. 313-323Kowaltowski, A.J., Vercesi, A.E., Castilho, R.F., (1997) Biochim. Biophys. Acta, 1318, pp. 385-402Boveris, A., Martino, E., Stoppani, A.O.M., (1977) Anal. Biochem., 80, pp. 145-158Chae, H.Z., Uhm, T.B., Rhee, S.G., (1994) Proc. Natl. Acad. Sci. U. S. A., 91, pp. 7022-7026Tsuji, K., Copeland, N.G., Jenkins, N.A., Obinata, M., (1995) Biochem. J., 307, pp. 377-381Zhang, P., Liu, B., Kang, S.W., Seo, M.S., Rhee, S.G., Obeid, L.M., (1997) J. Biol. Chem., 272, pp. 30615-3061
Note illustrative della Carta geologica delle Prealpi bresciane tra la V. Vrenda e il M. Pizzocolo. Explanation notes of the geological map of the Brescian Prealps between Val Vrenda and M. Pizzocolo.
No full textThe geological map of the V. Vrenda-M. Pizzocolo
area (1:25.000) is the partial result of studies carried out
for several years and that are still in progress in the
Brescian Prealps.
The explanatory text briefly describes the different
rock formations as well as Quaternary informal units
and it is completed by a long bibliographical list which
can supply further information to enhance the geological
knowledge and the regional description of this area.
Several variations have modified the previous cartography
and the new data introduce elements to reinterpret
the paleogeographic evolution of the area.
New data allows an updating of the tectonic evolution
of the Prealps; the Quaternary deposits have been distinguished
into several informal stratigraphic units. Geomorphological
symbols complete the map: karst features,
fluvial erosional cliffs, moraine ridges and other
glacial and fluvioglacial features have been mapped, as
well as gravel and limestone quarries
Polarization-Independent All-Optical Regenerator for DPSK Data
No full textWe demonstrate polarization-independent simultaneous all-optical phase-preserving amplitude regeneration and wavelength conversion of NRZ differential phase shift keying (DPSK) data by four-wave mixing (FWM) in a semiconductor optical amplifier (SOA). The dependence upon polarization state of the signals is eliminated by using a co-polarized dual-pump architecture. Investigation on the regenerative capability vs. pumps detuning shows significant BER threshold margin improvement over 6 nm conversion range
Chiral resolution, configurational study and pharmacological profile of 2-phenoxypropionic acids
No full textThe Role Of Reactive Oxygen Species In Mitochondrial Permeability Transition
No full textWe have provided evidence that mitochondrial membrane permeability transition induced by inorganic phosphate, uncouplers or prooxidants such as t-butyl hydroperoxide and diamide is caused by a Ca 2+-stimulated production of reactive oxygen species (ROS) by the respiratory chain, at the level of the coenzyme Q. The ROS attack to membrane protein thiols produces cross-linkage reactions, that may open membrane pores upon Ca 2+ binding. Studies with submitochondrial particles have demonstrated that the binding of Ca 2+ to these particles (possibly to cardiolipin) induces lipid lateral phase separation detected by electron paramagnetic resonance experiments exploying stearic acids spin labels. This condition leads to a disorganization of respiratory chain components, favoring ROS production and consequent protein and lipid oxidation.1714352Nicholls, D.G., Åkerman, K.E.O., (1982) Biochim. Biophys. Acta., 683, pp. 57-88Gunter, T.E., Pfeiffer, D.R., (1990) Am. J. 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On the enantiomers of 2-dimethylamino-3pentanone, key intermediate in the syntesis of analgesic alkylaminoalkylnaphthalenes
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