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93 results on '"Zamzami, Naoufal"'

52. Condensed matter in cell death

Author

Zamzami, Naoufal and Kroemer, Guido

Subjects
Cell death -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Apoptosis is identified by changes including nuclear chromatin condensation and nuclear fragmentation, but the molecular basis of these events is still largely unclear. A nuclear factor essential for apoptotic chromatin, but not DNA fragmentation, has been identified. The new factor, named Acinus, is shown to be present mainly in the nucleus and is activated through cleavage by caspases during apoptosis. Acinus may be a useful tool in dissecting changes occurring in the nucleus during apoptosis.

Published
1999

54. Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein R and Bcl-2

Author

Jacotot, Etienne, Ferri, Karine K.F., El Hamel, Chahrazed, Brenner, Catherine, Druillennec, Sabine, Hoebeke, Johan, Rustin, Pierre, Métivier, Didier, Lenoir, Christine, Geuskens, Maurice, Vieira, Helena H.L.A., Loeffler, Markus, Belzacq, Anne-Sophie, Briand, Jean-Paul, Zamzami, Naoufal, Edelman, Lena, Xie, Zhi Hua, Reed, John J.C., Roques, Bernard B.P., Kroemer, Guido, Jacotot, Etienne, Ferri, Karine K.F., El Hamel, Chahrazed, Brenner, Catherine, Druillennec, Sabine, Hoebeke, Johan, Rustin, Pierre, Métivier, Didier, Lenoir, Christine, Geuskens, Maurice, Vieira, Helena H.L.A., Loeffler, Markus, Belzacq, Anne-Sophie, Briand, Jean-Paul, Zamzami, Naoufal, Edelman, Lena, Xie, Zhi Hua, Reed, John J.C., Roques, Bernard B.P., and Kroemer, Guido

Abstract

Viral protein R (Vpr), an apoptogenic accessory protein encoded by HIV-1, induces mitochondrial membrane permeabilization (MMP) via a specific interaction with the permeability transition pore complex, which comprises the voltage-dependent anion channel (VDAC) in the outer membrane (OM) and the adenine nucleotide translocator (ANT) in the inner membrane. Here, we demonstrate that a synthetic Vpr-derived peptide (Vpr52-96) specifically binds to the intermembrane face of the ANT with an affinity in the nanomolar range. Taking advantage of this specific interaction, we determined the role of ANT in the control of MMP. In planar lipid bilayers, Vpr52-96 and purified ANT cooperatively form large conductance channels. This cooperative channel formation relies on a direct protein-protein interaction since it is abolished by the addition of a peptide corresponding to the Vpr binding site of ANT. When added to isolated mitochondria, Vpr52-96 uncouples the respiratory chain and induces a rapid inner MMP to protons and NADH. This inner MMP precedes outer MMP to cytochrome c. Vpr52-96-induced matrix swelling and inner MMP both are prevented by preincubation of purified mitochondria with recombinant Bcl-2 protein. In contrast to König's polyanion (PA10), a specific inhibitor of the VDAC, Bcl-2 fails to prevent Vpr52-96 from crossing the mitochondrial OM. Rather, Bcl-2 reduces the ANT-Vpr interaction, as determined by affinity purification and plasmon resonance studies. Concomitantly, Bcl-2 suppresses channel formation by the ANT-Vpr complex in synthetic membranes. In conclusion, both Vpr and Bcl-2 modulate MMP through a direct interaction with ANT., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
2001

56. Plasma membrane potential in thymocyte apoptosis

Author

Dallaporta, Bruno, Marchetti, Piero, De Pablo, Manuel M.A., Maisse, Carine, Duc, Huynh-Thien, Métivier, Didier, Zamzami, Naoufal, Geuskens, Maurice, Kroemer, Guido, Dallaporta, Bruno, Marchetti, Piero, De Pablo, Manuel M.A., Maisse, Carine, Duc, Huynh-Thien, Métivier, Didier, Zamzami, Naoufal, Geuskens, Maurice, and Kroemer, Guido

Abstract

SCOPUS: ar.j, info:eu-repo/semantics/published

Published
1999

58. Possible contribution of apoptosis-inducing factor (AIF) and reactive oxygen species (ROS) to UVB-induced caspase-independent cell death in the T cell line Jurkat

Author

Murahashi, Hideaki, primary, Azuma, Hiroshi, additional, Zamzami, Naoufal, additional, Furuya, Ko-ji, additional, Ikebuchi, Kenji, additional, Yamaguchi, Miki, additional, Yamada, Yoshiko, additional, Sato, Norihiro, additional, Fujihara, Mitsuhiro, additional, Kroemer, Guido, additional, and Ikeda, Hisami, additional

Published
2003
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59. A cytofluorometric assay of nuclear apoptosis induced in a cell-free system: Application to ceramide-induced apoptosis

Author

Susin, Santos, Zamzami, Naoufal, Larochette, Nathanael, Dallaporta, Bruno, Marzo, Isabel, Brenner, Catherine, Hirsch, Tamara, Petit, Patrice P.X., Geuskens, Maurice, Kroemer, Guido, Susin, Santos, Zamzami, Naoufal, Larochette, Nathanael, Dallaporta, Bruno, Marzo, Isabel, Brenner, Catherine, Hirsch, Tamara, Petit, Patrice P.X., Geuskens, Maurice, and Kroemer, Guido

Abstract

Purified nuclei exposed to apoptogenic factors in vitro undergo morphological and biochemical changes in chromatin organization. Most cell- free models of nuclear apoptosis are based on the quantitation of endonuclease-mediated DNA fragmentation on agarose gels or on the changes of nuclear morphology revealed by the DNA-intercalating fluorochrome 4'-6- diamidino-2-phenylindole dihydrochloride. In this work we develop a cytofluorometric system for the accurate quantitation of nuclear DNA loss. This system has been used to determine the conditions of nuclear apoptosis induced by apoptosis-inducing factor (AIF) contained in the supernatant of mitochondria induced to undergo permeability transition. AIF can provoke significant nuclear DNA loss in ≤ 5 min, acts over a wide pH range (pH 6 to 9), and resists cysteine protease inhibitors such as iodoacetamide and N- ethylmaleimide. Moreover, we applied this system to the question of how the proapoptotic second messenger ceramide would induce apoptosis in vitro: via a direct effect on nuclei, a direct effect on mitochondria, or via indirect mechanisms? Our data indicate that ceramide has to activate yet unknown cytosolic effectors that, in the presence of mitochondria, can induce nuclear apoptosis in vitro., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
1997

60. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

Author

Susin, Santos, Zamzami, Naoufal, Castedo, Maria, Hirsch, Tamara, Marchetti, Piero, Macho, Antonio, Daugas, Eric, Kroemer, Guido, Geuskens, Maurice, Susin, Santos, Zamzami, Naoufal, Castedo, Maria, Hirsch, Tamara, Marchetti, Piero, Macho, Antonio, Daugas, Eric, Kroemer, Guido, and Geuskens, Maurice

Abstract

SCOPUS: ar.j, info:eu-repo/semantics/published

Published
1996

61. Mitochondrial permeability transition is a central coordinating event of apoptosis

Author

Marchetti, Piero, Castedo, Maria, Susin, Santos, Zamzami, Naoufal, Hirsch, Tamara, Macho, Antonio, Haeffner, Astrid, Hirsch, François, Geuskens, Maurice, Kroemer, Guido, Marchetti, Piero, Castedo, Maria, Susin, Santos, Zamzami, Naoufal, Hirsch, Tamara, Macho, Antonio, Haeffner, Astrid, Hirsch, François, Geuskens, Maurice, and Kroemer, Guido

Abstract

SCOPUS: ar.j, info:eu-repo/semantics/published

Published
1996

62. Methods to Measure Membrane Potential and Permeability Transition in the Mitochondria During Apoptosis.

Author

Walker, John M., Brady, Hugh J. M., Zamzami, Naoufal, and Kroemer, Guido

Abstract

Mitochondrial membrane permeabilization (MMP) constitutes an early event of the apoptotic process. MMP affects both mitochondrial membranes. Inner MMP leads to the dissipation of the inner transmembrane potential and outer MMP culminates in the efflux of apoptogenic factors. The exact molecular mechanisms of MMP are still controversial. A growing body of data suggests that the cell death regulatory activity of Bcl-2 family members depends, at least in some instances, on their ability to modulate the opening of the mitochondrial permeability transition pore complex. Here, we will detail some experimental protocols designed to measure mitochondrial membrane potential and permeability transition, either in intact cells or in isolated mitochondria. [ABSTRACT FROM AUTHOR]

Published
2004
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63. Heat-shock protein 70 antagonizes apoptosis-inducing factor

Author

Ravagnan, Luigi, primary, Gurbuxani, Sandeep, additional, Susin, Santos A., additional, Maisse, Carine, additional, Daugas, Eric, additional, Zamzami, Naoufal, additional, Mak, Tak, additional, Jäättelä, Marja, additional, Penninger, Josef M., additional, Garrido, Carmen, additional, and Kroemer, Guido, additional

Published
2001
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65. Control of Mitochondrial Membrane Permeabilization by Adenine Nucleotide Translocator Interacting with HIV-1 Viral Protein R and Bcl-2

Author

Jacotot, Etienne, primary, Ferri, Karine F., additional, El Hamel, Chahrazed, additional, Brenner, Catherine, additional, Druillennec, Sabine, additional, Hoebeke, Johan, additional, Rustin, Pierre, additional, Métivier, Didier, additional, Lenoir, Christine, additional, Geuskens, Maurice, additional, Vieira, Helena L.A., additional, Loeffler, Markus, additional, Belzacq, Anne-Sophie, additional, Briand, Jean-Paul, additional, Zamzami, Naoufal, additional, Edelman, Lena, additional, Xie, Zhi Hua, additional, Reed, John C., additional, Roques, Bernard P., additional, and Kroemer, Guido, additional

Published
2001
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68. Plasma Membrane Potential in Thymocyte Apoptosis

Author

Dallaporta, Bruno, primary, Marchetti, Philippe, additional, de Pablo, Manuel A., additional, Maisse, Carine, additional, Duc, Huynh-Thien, additional, Métivier, Didier, additional, Zamzami, Naoufal, additional, Geuskens, Maurice, additional, and Kroemer, Guido, additional

Published
1999
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87. OPINION: The mitochondrion in apoptosis: how Pandora's box opens.

Author

Zamzami, Naoufal and Kroemer, Guido

Subjects
*MITOCHONDRIA, *ORGANELLES, *APOPTOSIS, *MITOCHONDRIAL membranes, *CELL membranes, *PROTEINS
Abstract

There is widespread agreement that mitochondria have a function in apoptosis, but the mechanisms behind their involvement remain controversial. Here we suggest that opening of a multiprotein complex called the mitochondrial permeability transition pore complex is sufficient (and, usually, necessary) for triggering apoptosis. [ABSTRACT FROM AUTHOR]

Published
2001
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88. Implication of mitochondria in apoptosis.

Author

Petit, Patrice, Zamzami, Naoufal, Vayssière, Jean-Luc, Mignotte, Bernard, Kroemer, Guido, and Castedo, Maria

Abstract

The induction phase of programmed cell death (PCD) or apoptosis is characterized by an extreme heterogeneity of potential PCD-triggering signal transduction pathways. During the subsequent effector phase, the numerous PCD-inducing stimuli converge into a few stereotypical pathways and cells pass a 'point of no return', thus becoming irreversibly committed to death. Evidence is accumulating that cytoplasmic structures, including mitochondria, participate in the critical effector stage and that alterations usually considered to define apoptosis, as nuclear chromatolysis and cytolysis, have to be ascribed to the late degradation phase. We and others have recently shown that nuclear features of apoptosis are preceded by alterations in mitochondrial function and structure. The importance of these alterations for the apoptotic process and also the possible link between, these observations, the permeability transition pore and the programmed cell death, are dicussed. (Mol Cell Biochem 174: 185–188, 1997) [ABSTRACT FROM AUTHOR]

Published
1997
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92. Pro-autophagic polyphenols reduce the acetylation of cytoplasmic proteins

Author

Erika Vacchelli, Federico Pietrocola, Mireia Niso-Santano, Maria Chiara Maiuri, Naoufal Zamzami, Guido Kroemer, Delphine Lissa, Shoaib Ahmad Malik, Lorenzo Galluzzi, Guillermo Mariño, Pietrocola, Federico, Mariño, Guillermo, Lissa, Delphine, Vacchelli, Erika, Malik, Shoaib Ahmad, Niso Santano, Mireia, Zamzami, Naoufal, Galluzzi, Lorenzo, Maiuri, MARIA CHIARA, and Kroemer, Guido

Subjects
Polyphenol, Cytoplasm, Population, Gene Expression, Biology, Resveratrol, chemistry.chemical_compound, Cell Cycle News & Views, Sirtuin 1, Report, Cell Line, Tumor, Stilbenes, Autophagy, French paradox, Humans, education, Molecular Biology, Piceatannol, education.field_of_study, food and beverages, Polyphenols, Acetylation, Cell Biology, Beclin 1, Enzyme Activation, Biochemistry, chemistry, Microscopy, Fluorescence, biology.protein, Myricetin, Developmental Biology, Protein deacetylation
Abstract

Resveratrol is a polyphenol contained in red wine that has been amply investigated for its beneficial effects on organismal metabolism, in particular in the context of the so-called "French paradox," i.e., the relatively low incidence of coronary heart disease exhibited by a population with a high dietary intake of cholesterol and saturated fats. At least part of the beneficial effect of resveratrol on human health stems from its capacity to promote autophagy by activating the NAD-dependent deacetylase sirtuin 1. However, the concentration of resveratrol found in red wine is excessively low to account alone for the French paradox. Here, we investigated the possibility that other mono- and polyphenols contained in red wine might induce autophagy while affecting the acetylation levels of cellular proteins. Phenolic compounds found in red wine, including anthocyanins (oenin), stilbenoids (piceatannol), monophenols (caffeic acid, gallic acid) glucosides (delphinidin, kuronamin, peonidin) and flavonoids (catechin, epicatechin, quercetin, myricetin), were all capable of stimulating autophagy, although with dissimilar potencies. Importantly, a robust negative correlation could be established between autophagy induction and the acetylation levels of cytoplasmic proteins, as determined by a novel immunofluorescence staining protocol that allows for the exclusion of nuclear components from the analysis. Inhibition of sirtuin 1 by both pharmacological and genetic means abolished protein deacetylation and autophagy as stimulated by resveratrol, but not by piceatannol, indicating that these compounds act through distinct molecular pathways. In support of this notion, resveratrol and piceatannol synergized in inducing autophagy as well as in promoting cytoplasmic protein deacetylation. Our results highlight a cause-effect relationship between the deacetylation of cytoplasmic proteins and autophagy induction by red wine components.

Published
2012

93. Methods to measure membrane potential and permeability transition in the mitochondria during apoptosis.

Author

Zamzami N and Kroemer G

Subjects
Animals, Cells, Cultured, Hepatocytes cytology, Mice, Permeability, Proto-Oncogene Proteins c-bcl-2 metabolism, Rats, Apoptosis physiology, Membrane Potentials, Mitochondria metabolism
Abstract

Mitochondrial membrane permeabilization (MMP) constitutes an early event of the apoptotic process. MMP affects both mitochondrial membranes. Inner MMP leads to the dissipation of the inner transmembrane potential and outer MMP culminates in the efflux of apoptogenic factors. The exact molecular mechanisms of MMP are still controversial. A growing body of data suggests that the cell death regulatory activity of Bcl-2 family members depends, at least in some instances, on their ability to modulate the opening of the mitochondrial permeability transition pore complex. Here, we will detail some experimental protocols designed to measure mitochondrial membrane potential and permeability transition, either in intact cells or in isolated mitochondria.

Published
2004
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