1,521 research outputs found
Mitochondrial Permeability Transition And Oxidative Stress
Mitochondrial 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. 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Dr. Shanesha R.F. Brooks-Tatum, RWWL AUC, July 2011
This video is a conversation with Dr. Shanesha R.F. Brooks-Tatum. Dr. Brooks-Tatum talks about her book, "The Encyclopedia of Hip Hop Literature." Daniel Le, AUC Woodruff Library, is the interviewer
The Role Of Reactive Oxygen Species In Mitochondrial Permeability Transition
We 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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Letter: R.F. Pettigrew to H.L. Loucks, May 30, 1916
R.F. Pettigrew articulates to H.L. Loucks his distaste for the book that Loucks recommended to him. Pettigrew also mentions that he would prefer to remain distanced from any conference with the author of the book. Pettigrew expresses great admiration and interest in Loucks' manuscript and desire to read it further
3,5,3'-triiodothyronine Induces Mitochondrial Permeability Transition Mediated By Reactive Oxygen Species And Membrane Protein Thiol Oxidation
Ca2+-loaded rat liver mitochondria treated with 3,5,3'- triiodothyronine (T3) undergo nonspecific inner membrane permeabilization, as evidenced by mitochondrial swelling, a decrease in membrane potential (ΔΨ), and an increase in the rate of oxygen uptake. T3 analogues thyroxine (T4), 3',5'-diiodothyronine (T2), and 3,5',3'-triiodothyronine (reverse T3), in decreasing order of potency, resulted in a similar but less extensive effect. Permeabilization induced by T3 is dependent on Ca2+ (1 μM) and T3 (0.5-25 μM) concentrations and is inhibited by cyclosporin A, a known inhibitor of mitochondrial permeability transition. Catalase or dithiothreitol also prevents membrane permeabilization, suggesting the participation of membrane protein thiol group oxidation induced by reactive oxygen species. The determination of the mitochondrial membrane protein thiol group content after treatment with Ca2+ and T3 shows a significant decrease, due to thiol oxidation. When mitochondria are incubated in the presence of inorganic phosphate and the protonophore carbonyl cyanide p- trifluoromethoxyphenylhydrazone, mitochondrial swelling still occurs after treatment with T3 and high Ca2+ concentrations, suggesting that mitochondrial permeabilization is not dependent on T3-induced ΔΨ or matrix pH alterations. Under these experimental conditions, when no oxygen is present in the incubation medium, no permeabilization occurs, suggesting that the permeabilization is dependent on mitochondrial-generated reactive oxygen species. Confirming this hypothesis, superoxide generation in a suspension of submitochondrial particles is increased when T3 is present. Our results lead to the conclusion that T3 induces a situation of oxidative stress in isolated liver mitochondria, with Ca2+-mediated membrane protein thiol oxidation and nonspecific inner membrane permeabilization.3541151157Soboll, S., (1993) Biochim. Biophys. 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The evolution of fat grafting : from soft tissue augmentation to regenerative medicine
The Author traces the evolution of fat grafting over the years from the first publication in 1893, to the systematization of the technique thanks to the contribution of Sydney Coleman. In recent years studies on the nature of adipose tissue have shown that besides multiple resident cells, fat tissue contains stem cells (ADSCs) capable of differentiating in multiple lineages, such as bone, cartilage, muscle, nerve, etc. Thus, in addition to the traditional notion that fat is a high energy reservoir, it becomes apparent that fat is a repair organ providing the basis for soft tissue regeneration. Manipulation of ADSCs promises to affect different fields of medicine and provide the physician with a variety of regenerative medical therapies
Low-frequency model-order reduction of electromagnetic fields without matrix factorization
Electrical Engineering, Mathematics and Computer Scienc
High Susceptibility Of Activated Lymphocytes To Oxidative Stress-induced Cell Death
The present study provides evidence that activated spleen lymphocytes from Walker 256 tumor bearing rats are more susceptible than controls to iert-butyl hydroperoxide (t-BOOH)-induced necrotic cell death in vitro. The iron chelator and antioxidant deferoxamine, the intracellular Ca2+ chelator BAPTA, the L-type Ca2+ channel antagonist nifedipine or the mitochondrial permeability transition inhibitor cyclosporin A, but not the calcineurin inhibitor FK-506, render control and activated lymphocytes equally resistant to the toxic effects of t-BOOH. Incubation of activated lymphocytes in the presence of t-BOOH resulted in a cyclosporin A-sensitive decrease in mitochondrial membrane potential. These results indicate that the higher cytosolic Ca 2+ level in activated lymphocytes increases their susceptibility to oxidative stress-induced cell death in a mechanism involving the participation of mitochondrial permeability transition.801137148ABE, K., SAITO, H., Characterization of t-butyl hydroperoxide toxicity in cultured rat cortical neurones and astrocytes (1998) Pharmacol Toxicol, 83, pp. 40-46ARNOLD, R., BRENNER, D., BECKER, M., FREY, C.R., KRAMMER, P.H., How T lymphocytes switch between life and death (2006) Eur J Immunol, 36, pp. 1654-1658BARTESAGHI, S., TRUJILLO, M., DENICOLA, A., FOLKES, L., WARDMAN, P., RADI, R., Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals (2004) Free Radic Biol Med, 36, pp. 471-483BARTOLI, G.M., PICCIONI, E., AGOSTARA, G., CALVIELLO, G., PALOZZA, P., Different mechanisms of tert-butyl hydroperoxide-induced lethal injury in normal and tumor thymocytes (1994) Arch Biochem Biophys, 312, pp. 81-87BERNARDES, C.F., PEREIRA, DA SILVA, L., VERCESI, A.E., t-Butylhydroperoxide-induced Ca2+ efflux from liver mitochondria in the presence of physiological concentrations of Mg2+ and ATP (1986) Biochim Biophys Acta, 850, pp. 41-48BOYUM, A., Isolation of lymphocytes, granulocytes and macrophages (1976) Scand J Immunol, (SUPPL. 5), pp. 9-15BRUMATTI, G., WEINLICH, R., CHEHAB, C.F., YON, M., AMARANTE-MENDES, G.P., Comparison of the anti-apoptotic effects of Bcr-Abl, Bcl-2 and Bcl-x(L) following diverse apoptogenic stimuli (2003) FEBS Lett, 541, pp. 57-63BUTTKE, T.M., SANDSTROM, P.A., Redox regulation of programmed cell death in lymphocytes (1995) Free Radic Res, 22, pp. 389-397CAMPOS, C.B., DEGASPERI, G.R., PACIFICO, D.S., ALBERICI, L.C., CARREIRA, R.S., GUIMARÃES, F., CASTILHO, R.F., VERCESI, A.E., Ibuprofen-induced Walker 256 tumor cell death: Cytochrome c release from functional mitochondria and enhancement by calcineurin inhibition (2004) Biochem Pharmacol, 68, pp. 2197-2206CASTILHO, R.F., KOWALTOWSKI, A.J., MEINICKE, A.R., BECHARA, E.J., VERCESI, A.E., Permeabilization of the inner mitochondrial membrane by Ca2+ ions is stimulated by t-butyl hydroperoxide and mediated by reactive oxygen species generated by mitochondria (1995) Free Radic Biol Med, 18, pp. 479-486CONKLIN, K.A., Chemotherapy-associated oxidative stress: Impact on chemotherapeutic effectiveness (2004) Integr Cancer Ther, 3, pp. 294-300CROMPTON, M., ELLINGER, H., COSTI, A., Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress (1988) Biochem J, 255, pp. 357-360CROMPTON, M., The mitochondrial permeability transition pore and its role in cell death (1999) Biochem J, 341, pp. 233-249DALY, M.J., YOUNG, R.J., BRITNELL, S.L., NAYLER, W.G., The role of calcium in the toxic effects of tert-butyl hydroperoxide on adult rat cardiac myocytes (1991) J Mol Cell Cardiol, 23, pp. 1303-1312DEGASPERI, G.R., VELHO, J.A., ZECCHIN, K.G., SOUZA, C.T., VELLOSO, L.A., BORECKÝ, J., CASTILHO, R.F., VERCESI, A.E., Role of mitochondria in the immune response to cancer: A central role for Ca 2+ (2006) J Bioenerg Biomembr, 38, pp. 1-10DEGASPERI, G.R., ZECCHIN, K.G., BORECKY, J., CRUZ-HOFLING, M.A., CASTILHO, R.F., VELLOSO, L.A., GUIMARÃES, F., VERCESI, A.E., Verapamil-sensitive Ca2+ channel regulation of Th1-type proliferation of splenic lymphocytes induced by Walker 256 tumor development in rats (2006) Eur J Pharmacol, 549, pp. 179-184DOROSHOW, J.H., Anthracycline antibiotic-stimulated superoxide, hydrogen peroxide, and hydroxyl radical production by NADH dehydrogenase (1983) Cancer Res, 43, pp. 4543-4551FESKE, S., Calcium signalling in lymphocyte activation and disease (2007) Nat Rev Immunol, 7, pp. 690-702FRIBERG, H., FERRAND-DRAKE, M., BENGTSSON, F., HALESTRAP, A.P., WIELOCH, T., Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death (1998) JNeurosci, 18, pp. 5151-5159GALAT, A., Peptidylprolyl cis/trans isomerases (immunophilins): Biological diversity - targets - functions (2003) Curr Top Med Chem, 3, pp. 1315-1347GIARDINI, C., LA NASA, G., CONTU, L., GALIMBERTI, M., POLCHI, P., ANGELUCCI, E., BARONCIANI, D., LUCARELLI, G., Desferrioxamine therapy induces clearance of iron deposits after bone marrow transplantation for thalassemia: Case report (1993) Bone Marrow Transplant, (SUPPL. 1), pp. 108-110GOLDSTEIN, S., CZAPSKI, G., Transition metal ions and oxygen radicals (1990) Int Rev Exp Pathol, 31, pp. 133-164GREEN, D.R., KROEMER, G., The pathophysiology of mitochondrial cell death (2004) Science, 305, pp. 626-629GREEN, D.R., REED, J.C., Mitochondria and apoptosis (1998) Science, 281, pp. 1309-1312GRIFFITHS, E.J., HALESTRAP, A.P., 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 (1991) Biochem J, 274, pp. 611-614GROSSMAN, Z., MIN, B., MEIER-S, CHELLERSHEIM, M., PAUL, W.E., Concomitant regulation of T-cell activation and homeostasis (2004) Nat Rev Immunol, 4, pp. 387-395HALLIWELL, B., Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action? (1989) Free Radic Biol Med, 7, pp. 645-651HARTLEY, A., DAVIES, M., RICE- EVANS, C., Desferrioxamine as a lipid chain-breaking antioxidant in sickle erythrocyte membranes (1990) FEBS Lett, 264, pp. 145-148HERMISTON, M.L., XU, Z., MAJETI, R., WEISS, A., Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases (2002) J Clin Invest, 109, pp. 9-14HOE, S., ROWLEY, D.A., HALLIWELL, B., Reactions of ferrioxamine and desferrioxamine with the hydroxyl radical (1982) Chem Biol Interact, 41, pp. 75-81JOCELYN, P.C., DICKSON, J., Glutathione and the mitochondrial reduction of hydroperoxides (1980) BiochimBiophys Acta, 590, pp. 1-12KENNEDY, C.H., CHURCH, D.F., WINSTON, G.W., PRYOR, W.A., tert-Butyl hydroperoxide-induced radical production in rat liver mitochondria (1992) Free Radic Biol Med, 12, pp. 381-387KOWALTOWSKI, A.J., CASTILHO, R.F., VERCESI, A.E., Mitochondrial permeability transition and oxidative stress (2001) FEBS Lett, 495, pp. 12-15KRAMMER PH, ARNOLD R AND LAVRIK IN. 2007. Life and death in peripheral T cells. Nat Rev Immunol 7: 532-542LEMASTERS, J.J., ET AL., The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy (1998) Biochim Biophys Acta, 1366, pp. 177-196MACKALL, C.L., FLEISHER, T.A., BROWN, M.R., MAGRATH, I.T., SHAD, A.T., HOROWITZ, M.E., WEXLER, L.H., GRESS, R.E., Lymphocyte depletion during treatment with intensive chemotherapy for cancer (1994) Blood, 84, pp. 2221-2228MARTIN, S.J., REUTELINGSPERGER, C.P.M., MCGAHON, A.J., RADER, J., VAN SCHIE, R.C.A.A., LAFACE, D.M., GREEN, D.R., Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overex-pression of Bcl-2 and Abl (1995) J Exp Med, 182, pp. 1-12MATHER, M.W., ROTTENBERG, H., The inhibition of calcium signaling in T lymphocytes from old mice results from enhanced activation of the mitochondrial permeability transition pore (2002) Mech Ageing Dev, 123, pp. 707-724NIEMINEN, A.L., BYRNE, A.M., HERMAN, B., LEMASTERS, J.J., Mitochondrial permeability transition in hepatocytes induced by t-BuOOH: NAD(P)H and reactive oxygen species (1997) Am J Physiol, 272, pp. C1286-C1294QUINTANA, A., GRIESEMER, D., SCHWARZ, E.C., HOTH, M., Calcium-dependent activation of T-lymphocytes (2005) Pflugers Arch, 450, pp. 1-12ROTTENBERG, H., WU, S., Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells (1998) Biochim Biophys Acta, 1404, pp. 393-404ROY, C.R., Immunology: Professional secrets (2003) Nature, 425, pp. 351-352STAHNKE, K., FULDA, S., FRIESEN, C., STRAUSS, G., DEBATIN, K.M., Activation of apoptosis pathways in peripheral blood lymphocytes by in vivo chemotherapy (2001) Blood, 98, pp. 3066-3073WALLACE, K.B., Doxorubicin-induced cardiac mitochondrionopathy (2003) Pharmacol Toxicol, 93, pp. 105-115WILLIAMS, M.S., KWON, J., T cell receptor stimulation, reactive oxygen species, and cell signaling (2004) Free Radic Biol Med, 37, pp. 1144-1151ZORATTI, M., SZABO, I., The mitochondrial permeability transition (1995) Biochim Biophys Acta, 1241, pp. 139-17
Effect Of Inorganic Phosphate Concentration On The Nature Of Inner Mitochondrial Membrane Alterations Mediated By Ca2+ Ions: A Proposed Model For Phosphate-stimulated Lipid Peroxidation
Addition of high concentrations (>1 mM) of inorganic phosphate (Pi) or arsenate to Ca2+-loaded mitochondria was followed by increased rates of H2O2 production, membrane lipid peroxidation, and swelling. Mitochondrial swelling was only partially prevented either by butylhydroxytoluene, an inhibitor of lipid peroxidation, or eyclosporin A, an inhibitor of the mitochondrial permeability transition pore. This swelling was totally prevented by the simultaneous presence of these compounds. At lower Pi concentrations (1 mM), mitochondrial swelling is reversible and prevented by cyclosporin A, but not by butylhydroxytoluene. In any case (low or high phosphate concentration) exogenous catalase prevented mitochondrial swelling, suggesting that reactive oxygen species (ROS) participate in these mechanisms. Altogether, the data suggest that, at low Pi concentrations, membrane permeabilization is reversible and mediated by opening of the mitochondrial permeability transition pore, whereas at high Pi concentrations, membrane permeabilization is irreversible because lipid peroxidation also takes place. Under these conditions, lipid peroxidation is strongly inhibited by sorbate, a putative quencher of triplet carbonyl species. This suggests that high Pi or arsenate concentrations stimulate propagation of the peroxidative reactions initiated by mitochondrial-generated ROS because these anions are able to catalyze Cn-aldehyde tautomerization producing enols, which can be oxidized by hemeproteins to yield the lower Cn - 1-aldehyde in the triplet state. This proposition was also supported by experiments using a model system consisting of phosphatidylcholine/dicethylphosphate liposomes and the triplet acetone-generating system isobutanal/horseradish peroxidase, where phosphate and Ca2+ cooperate to increase the yield of thiobarbituric acid-reactive substances.271629292934Reed, D.J., (1990) Chem. Res. Toxicol., 5, pp. 495-502Orrenius, S., McConckey, D.J., Bellomo, G., Nicotera, P., (1990) Trends Pharmacol. Sci., 10, pp. 281-285McCord, J.M., (1985) N. Engl. J. Med., 312, pp. 159-163Poole-Wilson, P.A., Harding, D.P., Bourdillon, P.D., Tones, M.A., (1984) J. Mol. Cell. Cardiol., 16, pp. 175-185Halliwell, B., Gutteridge, J.M., (1985) Mol. Aspects Med., 8, pp. 89-193Kammermeier, H., Schmidt, P., Jungling, E., (1982) J. Mol. Cell. Cardiol., 14, pp. 267-277Paller, M.S., Greene, E.L., (1994) Ann. N. Y Acad. Sci., 723, pp. 59-70Lange, L.G., Hartman, M., Sobel, B.E., (1984) J. Clin. 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In memory of Paul Tessier, MD (1917-2008)
The Author traces the life and the surgical achievements of Paul Tessier, founder of craniofacial surgery
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