Relevant bibliographies by topics / Apoptosomes

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Academic literature on the topic 'Apoptosomes'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Apoptosomes"

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Chai, Jijie, and Yigong Shi. "Apoptosome and inflammasome: conserved machineries for caspase activation." National Science Review 1, no. 1 (2014): 101–18. http://dx.doi.org/10.1093/nsr/nwt025.

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Abstract Apoptosome and inflammasome are multimeric protein complexes that mediate the activation of specific caspases at the onset of apoptosis and inflammation. The central component of apoptosome or inflammasome is a tripartite scaffold protein, exemplified by Apaf-1 and NLRC4, which contains an amino-terminal homotypic interaction motif, a central nucleotide-binding oligomerization domain and a carboxyl-terminal ligand-sensing domain. In the absence of death cue or an inflammatory signal, Apaf-1 or NLRC4 exists in an auto-inhibited, monomeric state, which is stabilized by adenosine diphosphate (ADP). Binding to an apoptosis- or inflammation-inducing ligand, together with replacement of ADP by adenosine triphosphate (ATP), results in the formation of a multimeric apoptosome or inflammasome. The assembled apoptosome and inflammasome serve as dedicated machineries to facilitate the activation of specific caspases. In this review, we describe the structure and functional mechanisms of mammalian inflammasome and apoptosomes from three representative organisms. Emphasis is placed on the molecular mechanism of caspase activation and the shared features of apoptosomes and inflammasomes.
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Beem, Elaine, L. Shannon Holliday, and Mark S. Segal. "The 1.4-MDa apoptosome is a critical intermediate in apoptosome maturation." American Journal of Physiology-Cell Physiology 287, no. 3 (2004): C664—C672. http://dx.doi.org/10.1152/ajpcell.00232.2003.

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Previously, we demonstrated that both 150 mM KCl and alkaline pH inhibit cytochrome c-mediated activation of procaspase-3 in a unique manner. To determine the mechanism of inhibition, we analyzed the effect of KCl and alkaline pH on the formation of apoptosomes (a large complex consisting of cytochrome c, Apaf-1, and procaspase-9/caspase-9) in vitro. Our results suggest that an initial ∼700-kDa apoptosome matures through a 1.4-MDa intermediate before a ∼700-kDa apoptosome is reformed and procaspase-3 is activated. We further demonstrate that 150 mM KCl interferes with the conversion of the initial ∼700-kDa apoptosome to the 1.4-MDa intermediate, while alkaline pH “traps” the apoptosome in the 1.4-MDa intermediate. Analysis of the cleaved state of procaspase-9 and procaspase-3 suggests that the 1.4-MDa intermediate may be required for cleavage of procaspase-9. Consistent with these results, in vivo data suggest that blocking acidification during the induction of apoptosis inhibits activation of procaspase-3. On the basis of these results, we propose a model of apoptosome maturation.
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Murphy, Brona M., Amanda J. O'Neill, Colin Adrain, R. William G. Watson, and Seamus J. Martin. "The Apoptosome Pathway to Caspase Activation in Primary Human Neutrophils Exhibits Dramatically Reduced Requirements for Cytochrome c." Journal of Experimental Medicine 197, no. 5 (2003): 625–32. http://dx.doi.org/10.1084/jem.20021862.

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Caspase activation is a central event in numerous forms of apoptosis and results in the proteolytic degradation of multiple substrate proteins that contribute to the apoptotic phenotype. An important route to caspase activation proceeds via assembly of the “apoptosome” as a result of the cell stress–associated release of mitochondrial cytochrome c. Previous studies have shown that primary neutrophils are largely incapable of mitochondrial respiration, suggesting that these cells either lack functional mitochondria or possess a defective respiratory chain. This prompted us to examine whether neutrophils retain an intact cytochrome c/apoptotic protease-activating factor 1 (Apaf-1) pathway to caspase activation and apoptosis. We show that primary human neutrophils contain barely detectable levels of cytochrome c as well as other mitochondrial proteins. Surprisingly, neutrophil cell–free extracts readily supported Apaf-1–dependent caspase activation, suggesting that these cells may assemble cytochrome c–independent apoptosomes. However, further analysis revealed that the trace amount of cytochrome c present in neutrophils is both necessary and sufficient for Apaf-1–dependent caspase activation in these cells. Thus, neutrophils have a lowered threshold requirement for cytochrome c in the Apaf-1–dependent cell death pathway. These observations suggest that neutrophils retain cytochrome c for the purpose of assembling functional apoptosomes rather than for oxidative phosphorylation.
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Wang, Li, Qi Qiao, and Hao Wu. "Understanding CARD Tricks in Apoptosomes." Structure 25, no. 4 (2017): 575–77. http://dx.doi.org/10.1016/j.str.2017.03.013.

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Adams, Jerry M., and Suzanne Cory. "Apoptosomes: engines for caspase activation." Current Opinion in Cell Biology 14, no. 6 (2002): 715–20. http://dx.doi.org/10.1016/s0955-0674(02)00381-2.

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Adrain, Colin, Gabriela Brumatti, and Seamus J. Martin. "Apoptosomes: protease activation platforms to die from." Trends in Biochemical Sciences 31, no. 5 (2006): 243–47. http://dx.doi.org/10.1016/j.tibs.2006.03.004.

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Chen, Min, Alan D. Guerrero, Li Huang, et al. "Caspase-9-induced Mitochondrial Disruption through Cleavage of Anti-apoptotic BCL-2 Family Members." Journal of Biological Chemistry 282, no. 46 (2007): 33888–95. http://dx.doi.org/10.1074/jbc.m702969200.

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Mitochondrial disruption during apoptosis results in the release of cytochrome c that forms apoptosomes with Apaf-1 and caspase-9. Activation of caspase-9 by dimerization in apoptosomes then triggers a caspase signaling cascade. In addition, other apoptosis signaling molecules released from the mitochondrion, such as apoptosis-inducing factor and endonuclease G, may induce caspase-9-independent apoptosis. To determine the signaling events induced by caspase-9, we used chemically induced dimerization for specific activation of caspase-9. We observed that caspase-9 dimerization resulted in the loss of mitochondrial membrane potential and the cleavage of anti-apoptotic Bcl-2, Bcl-xL, and Mcl-1. Moreover, cleavage-resistant Bcl-2, Bcl-xL, or Mcl-1 potently inhibited caspase-9-dependent loss of mitochondrial membrane potential and the release of cytochrome c. Our data suggest that a caspase-9 signaling cascade induces feedback disruption of the mitochondrion through cleavage of anti-apoptotic Bcl-2, Bcl-xL, and Mcl-1.
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Suto, Daisuke, Kazuaki Sato, Yoshihiro Ohba, Tetsuhiko Yoshimura, and Junichi Fujii. "Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism." Biochemical Journal 392, no. 2 (2005): 399–406. http://dx.doi.org/10.1042/bj20050580.

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Stimuli for apoptotic signalling typically induce release of cyt c (cytochrome c) from mitochondria. Cyt c then initiates the formation of the apoptosome, comprising Apaf-1 (apoptotic protease-activating factor 1), caspase-9 and other cofactors. The issue of whether the redox state of the haem in cyt c affects the initiation of the apoptotic pathway is currently a subject of debate. In a cell-free reconstitution system, we found that only oxidized cyt c was capable of activating the caspase cascade. Oxidized cyt c was reduced by the physiological reductants cysteine and glutathione, after which it was unable to activate the caspase cascade. It is thus likely that cyt c with oxidized haem is in a conformation capable of interaction with Apaf-1 and forming apoptosomes. When either oxidized or reduced cyt c was treated with submillimolar concentrations of endoperoxide, which affected less than 3% of the redox state of haem, the ability of the oxidized cyt c to activate the caspase cascade was abolished. Higher amounts of singlet oxygen were required to affect the optical spectral change of haem, suggesting that the suppressed pro-apoptotic function of oxidized cyt c is a mechanism that is separate from the redox state of haem. Oxidative protein modification of cyt c by singlet oxygen was evident, on the basis of elevated contents of carbonyl compounds. Our data suggest that singlet oxygen eliminates the pro-apoptotic ability of oxidized cyt c not via the reduction of haem, but via the modification of amino acid residues that are required for apoptosome formation.
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Prudnikov,, I. M., V. M. Tsyvkin, A. M. Smirnov, and I. V. Pristash. "HUMAN HEMATOPOIETIC STEM CELLS GENERATE EXOSOMES CONTAINING ACTIVE PROTEASOMES BUT NOT CASPASES." Fiziolohichnyĭ zhurnal 66, no. 6 (2020): 13–20. http://dx.doi.org/10.15407/fz66.06.013.

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Activities of two classes of neutral proteases were studied: caspases and proteasomes, which are contained in extracellular vesicles generated by mesenchymal and hematopoietic human stem cells (MSCs and HSCs, respectively). The formation of apoptosomes induced by the cytochrome C and dATP did not occurred in these cells. The presence of TNFa in the culture medium of HSCs causes the appearance of caspase-3 intracellular activity. Herewith caspase activity was detected in exosomes also. This activity was completely inhibited by a non-substrate caspase inhibitor, emricasane, and it was not sensitive to proteasome inhibitors. It is assumed that the caspases’ activity from the cultural medium is the sum of membrane (outer side of exosome membrane), intracellular and extracellular activities. Apparently, this activity refers to apoptosomes as it was revealed by gel filtration of cultural medium with TNFa free from exosomes. Thus, TNFa induces the appearance of neutrophils in the culture of HSCs or the generation of other differentiated cells that are capable of apoptosis, in contrast to HSCs or MSCs. Proteasomal activity increased noticeably in exosomes from HSCs after the addition of TNFa. In contrast to exosomes from MSCs, all activity of proteasomes in HSCs-produced exosomes had a membrane localization.
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Tsujimoto, Yoshihide. "Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?" Genes to Cells 3, no. 11 (1998): 697–707. http://dx.doi.org/10.1046/j.1365-2443.1998.00223.x.

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Dissertations / Theses on the topic "Apoptosomes"

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Twiddy, Davina Deborah. "Molecular and proteomic characterisation of the ~700 kDa apoptosome." Thesis, University of Leicester, 2005. http://hdl.handle.net/2381/30776.

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The apoptosome is a caspase-activating complex consisting of Apaf-1, caspase-9 and cytochrome c, which is essential for the induction of stress-mediated apoptosis. This complex ranges in size from ~ 700 kDa to ~ 1.4 MDa, possibly due to the stable association of modulatory proteins. In the current study I employed two strategies to isolate and characterise the active ~ 700 kDa apoptosome in vitro. Firstly, I used GST-Casp91-130, which binds to the CARD domain of Apaf-1 in a dATP and cytochrome c-dependent manner, to affinity-purify an apoptosome containing only Apaf-1XL and cytochrome c. This result was confirmed by the second approach, which used an antibody to the caspase-9 to immunoprecipitate of the native apoptosome, which contained Apaf-1 and caspase-9 (p34/p35). However, in the absence of SMAC and Omi, the native apoptosome also contained caspase-3 and XIAP, both of which associated via the catalytic domains of caspase-9. When isolating the apoptosome from apoptotic cells using TAP-tagged caspase-9 variants, I discovered that the location of the TAP-tag can affect the ability of caspase-9 to interact with known binding partners and consequently can influence the induction of cell death. I have also studied the role of the apoptosome in the caspase-3 null cell line, MCF-7, and have demonstrated that an active ~ 700 kDa apoptosome complex is formed in both dATP-activated cell lysates and an apoptotic MCF-7 cells. Furthermore, the active apoptosome can directly process and activate caspase-7.
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Langlais, Claudia. "Characterisation of the ~700kDa apoptosome complex from THP.1 cells." Thesis, University of Leicester, 2002. http://hdl.handle.net/2381/30765.

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Apoptosis or programmed cell death is a process involving the regulated self-destruction of a cell. Execution of the apoptotic programme requires the hierarchical activation of a family of proteases, the caspases. Here, I describe the characterisation and purification of the apoptosome, a ~700kDa caspase activating complex. Gel filtration of dATP-activated THP.1 cell lysates showed that effector caspase activity is assessed with a large complex, the apoptosome, which contains Apaf-1 and active caspases-9, -3 and -7. Further analysis revealed two large complexes, a biologically inactive ~1.4MDa and a biologically active ~700kDa complex to be formed very rapidly. Experiments involving the use of the caspase inhibitor z-VAD.FMK demonstrated that complex formation is caspase-independent, however, release of processed caspase-9 from the complex and the recruitment of other procaspases to the complex, is caspase activity-dependent. In apoptotic cells, the ~700kDa apoptosome complex predominates and is therefore suggested to be the biologically relevant complex. Normal intracellular K+ concentrations inhibited formation of the ~700kDa apoptosome complex in lysates and in a reconstituted system. Increasing concentrations of cytochrome c partially reversed inhibition. A mechanism is proposed for the inhibitory effect of K+ during dATP-dependent caspase activation in cellular lysates. The ~700kDa apoptosome complex was purified using multi-step purification procedures. Several proteins were identified in the purified apoptosome fraction and these included Apaf-1 and capase-9 as well as XIAP, b-actin, CAP-1, CAZ1/CAZ2 and possibly Hsc70 are all involved with the cytoskeleton and are capable of binding actin, whereas rabaptin-5 and IKKg (NEMO) are known to be involved in endosomal transport and the NFkB pathway, respectively. The possible involvement of these proteins in apoptosome assembly and function is discussed.
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Malet, Engra Gema. "Identificación de moduladores del apoptosoma mediante química combinatoria." Doctoral thesis, Universitat de València, 2005. http://hdl.handle.net/10803/9529.

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La apoptosis es un proceso importante en una amplia variedad sistemas biológicos, incluyendo el recambio celular normal, el sistema inmunológico y el desarrollo embrionario. La apoptosis inadecuada está implicada en muchas enfermedades incluyendo enfermedades neurodegenerativas tales como las enfermedades de Alzheimer y Huntington, isquemia, desórdenes autoinmunes y varias formas de cáncer. La familia de proteínas Bcl-2 abarca una clase de estructuras homólogas que sirven para inhibir o para activar la apoptosis en un proceso intrincado y a su vez, bien orquestado. Los estímulos apoptósicos inducen la translocación de miembros pro-apoptósicos de la familia de Bcl-2 a la membrana mitochondrial externa donde forman canales iónicos que pueden contribuir a disipar el potencial transmembrana de la mitocondria y favorecer la liberación de citocromo c. En el citosol, esta proteína se une al factor activador de apoptosis (Apaf-1) para formar el complejo denominado apoptosoma que activa una familia de proteasas denominada caspasas. Las caspasas hidrolizan una serie de proteínas clave para la supervivencia celular y la célula muere de forma no necrótica. Estas moléculas moduladoras podrían ser consideradas como agentes "cabeza de serie" para el desarrollo de compuestos que puedan inhibir el crecimiento de células tumorales y/o paliar o aminorar los daños celulares asociados a las enfermedades neurodegenerativas En la tesis doctoral se utiliza la Química Combinatoria para la identificación de moléculas de interés biomédico moduladoras del apoptosoma. Para ello, en primer lugar es necesario poner a punto un ensayo de alto rendimiento que permita utilizar la diana terapéutica, el apoptosoma, y que permita el cribado funcional de un elevado número de moléculas con el objetivo de identificar efectores artificiales del sistema Apaf-1-caspasas. El trabajo presentado en esta tesis incorpora como novedad la utilización de los componentes básicos recombinantes purificados del apoptosoma y la reconstitución de su actividad in vitro para el cribado. Con este ensayo y formato de cribado, lo que se consigue una mejor definición de la diana molecular de búsqueda de moléculas moduladoras. Por otro lado, la posibilidad de manipulación de los distintos componentes del apoptosoma en las reacciones de reconstitución permite llevar a cabo la caracterización del mecanismo de acción de los compuestos actuvos identificados y su sitio de unión. Finalmente se llevo a cabo unestudio in vivo de los compuestos identificados como moduladores.<br>Protein-protein interactions represent points of chemical intervention for therapeutic gain in the biological processes associated with disease. Apoptosis is an interesting biological process because its importance in a wide variety of biological systems. Inappropriate apoptosis is involved in many human pathologies, including neurodegenerative diseases such as Alzheimer's and Huntington's, ischaemia, autoimmune disorders and several forms of cancer. Diverse apoptotic stimuli, including activation of cell surface death receptors, anticancer agents, irradiation, lack of survival factors, and ischemia induce signaling cascades that all activate a family of cysteine aspartyl proteases called caspases. It is these proteases that execute the apoptotic process. Effector caspases are responsible for the disassembly of cellular components while initiator caspases are responsible for activation of the effector caspases. Because of the critical consequences of apoptosis malfunctioning, the activation of caspases is scrupulously controlled. Some apoptotic signals activate the mitochondria-mediated or intrinsic pathway that utilizes caspase-9 as its initiator. Caspase-9 activation is triggered by the release to the cytosol of proapoptotic proteins from the mitochondrial inter-membrane space, in particular cytochrome c. The formation of the macromolecular complex named apoptosome is a key event in this pathway. The apoptosome is a holoenzyme multiprotein complex formed by cytochrome c-activated Apaf-1 (apoptotic protease-activating factor), dATP and procaspase-9. In this macromolecular complex apoptosome-associated caspase-9 is activated and then, in turn, activate effector caspases. To identify molecules that could ameliorate disease-associated apoptosis, drug discovery efforts have initially targeted caspase activity rather than activation. Nevertheless, protein-protein interactions upstream of caspase activation can be also relevant points of intervention for the development of modulators of apoptosis pathways. In particular, recent data propose the formation of the apoptosome as an interesting target for the development of apoptotic modulators. In the absence of detailed structural information, the conventional methods used for the identification of modulators of the apoptosome have been based in indirect measurements of the cytochrome c- and dATP-induced activation of caspase-3-like activity on defined cytosolic extracts. Using this methodology Lademann et al. have identified inhibitors of the apoptosome through the screening of small molecules using cytosolic extracts of selected cells.We have carried out a discovery program employing an in vitro reconstituted active apoptosome assembled from its recombinant constituent proteins. Here we describe the identification of compounds that inhibit the apoptosome-mediated activation of procaspase-9 from the screening of a diversity-oriented chemical library of N-alkylglycines. The active compounds rescued from the library were chemically optimized to obtain molecules that bind to both recombinant and human endogenous Apaf-1 and decrease the apoptotic phenotype in mitochondrial-mediated models of cellular apoptosis.
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Henty, Kristen M. "A role for neuroglobin in the inhibition of cytochrome c-mediated apoptosome formation." Thesis, University of Auckland, 2011. http://hdl.handle.net/2292/8268.

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The mitochondrial pathway of apoptosis is an important mediator of cell death in many human diseases. A key event in this pathway is permeabilisation of the outer mitochondrial membrane and subsequent release of the heme-protein cytochrome c from mitochondria into the cytosol. Thereafter, cytosolic cytochrome c mediates the formation of the apoptosome complex, which cleaves the initiator caspase 9, thereby activating the caspase signalling cascade. Apoptosome formation is thought to require cytochrome c which has its heme iron in the ferric form. Neuroglobin, a recently discovered globin, protects various cell lines and tissues from apoptosis. Previously, neuroglobin has been shown to efficiently reduce the heme iron of cytochrome c in vitro. We hypothesise that neuroglobin prevents apoptosome assembly by reducing cytochrome c. The work carried out in this thesis aimed to investigate the properties of the neuroglobin-cytochrome c complex and identify its role in the regulation of apoptosome formation. Surface Plasmon Resonance experiments have been used to explore the nature of the complex and have revealed that neuroglobin binds to cytochrome c with weak affinity (KD = 27-56 μM), forming a transient protein complex that is mediated largely by electrostatic interactions. A putative specific complex structure has been predicted by computer modelling. The interacting residues on the neuroglobin interface in the putative complex have been mutated and changes in binding affinity were measured with SPR. The results from these studies are consistent with the neuroglobin-cytochrome c interaction occurring via an encounter complex mechanism. Furthermore, cell-free in vitro assay systems have been developed to measure caspase activation and apoptosome formation induced by exogenous cytochrome c. In keeping with previous studies, ferric cytochrome c efficiently initiated apoptosome formation, while ferrous cytochrome c exhibited very little of this activity. Ferrous neuroglobin was capable of efficiently inhibiting apoptosome formation initiated by ferric cytochrome c, whereas ferric neuroglobin was significantly less effective. Taken together, these experiments suggest a role for ferrous neuroglobin in the prevention of apoptosome formation.
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Cagnol, Sébastien. "Contrôle de la mort cellulaire par la voie des MAPK1/3 (ERK2/1)." Phd thesis, Université de Nice Sophia-Antipolis, 2005. http://tel.archives-ouvertes.fr/tel-00104792.

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La mort cellulaire programmée ou apoptose est un mécanisme conservé chez les eucaryotes multicellulaires qui contribue au développement embryonnaire et à l'homéostasie cellulaire des organismes. Dans les cellules vivantes, l'activité des protéases qui exécutent le programme de mort cellulaire, les caspases, est contrôlée par des signaux de survie provenant de l'environnement cellulaire. Les caspases initiatrices de l'apoptose régulée par l'environnement, la caspase 9 et la caspase 8 sont activées respectivement par l'apoptosome et par les récepteurs de mort. Les signaux environnementaux, parmi lesquels le contact avec la matrice extracellulaire ou la présence de facteurs de croissance, activent des voies de signalisation contrôlant la machinerie de mort cellulaire. La voie des MAPK1/3 est une voie de signalisation contrôlée par le proto-oncogènes Ras et comportant les kinases Raf, MEK1/2 et MAPK1/3 (ERK2/1 ou p42/p44). La voie des MAPK1/3, qui est impliquée dans la prolifération et la différentiation cellulaire, joue un rôle essentiel dans la survie cellulaire. L'objectif de cette thèse a été de caractériser les mécanismes moléculaires impliqués dans le contrôle de la mort cellulaire par la voie des MAPK1/3. Ce travail est basé sur l'utilisation d'une forme active et inductible de la kinase Raf-1 (DRaf-1:ER) dont l'activation forte et prolongée correspond à une induction pathologique de la voie des MAPK1/3. Nous avons montré que, selon le type cellulaire, l'activation de deltaRaf-1:ER favorise la survie ou la mort cellulaire. Dans les cellules fibroblastiques CCL39, l'activation de deltaRaf-1:ER protège de la mort cellulaire mitochondriale induite par la privation en sérum du milieu de culture. Dans ces conditions, nous avons montré que la stimulation de Raf-1 :ER bloque l'activation de la caspase-9 mais n'empêche pas la délocalisation du cytochrome c, la multimérisation d'APAF1 ni le recrutement de la procaspase 9 dans l'apoptosome. Ce mécanisme post mitochondrial de protection contre la mort cellulaire dépend de la néo-synthèse des protéines et nécessite une activité continue de la kinase MEK. A l'inverse, dans les cellules HEK 293 issues de rein embryonnaire et présentant des caractéristiques neuronales, nous avons montré que l'activation soutenue de la voie des MAPK1/3 par DRaf1-ER induit une mort cellulaire massive. Celle-ci est caractérisée par l'activation des caspases et la fragmentation de l'ADN. La mort cellulaire est détectée plus de 24 heures après l'activation de Raf1-ER, elle est maximale à 48h. L'induction de la mort cellulaire ne requière la synthèse protéique que durant la phase précoce d'activation mais nécessite l'activité continue du module MEK/MAPK. La mort cellulaire résulte de l'activation de la caspase 8 et n'implique pas la voie mitochondriale, elle est caractérisée par une vacuolisation importante du cytoplasme des cellules qui l'apparente à une forme particulière d'apoptose. L'inactivation des fonctions du récepteur fas et de son adaptateur FADD indique que le processus d'activation de la caspase 8 est indépendant de la voie des récepteurs de mort. L'ensemble de ces travaux apporte des connaissances nouvelles sur le contrôle de la mort cellulaire par la voie Raf/MAPK1/3. Nous avons montré que la voie de signalisation peut, selon le contexte cellulaire, favoriser la survie cellulaire ou induire la mort. Dans les deux cas, le contrôle de la mort cellulaire dépend à la fois de la synthèse protéique et de mécanismes post-traductionnels. Les mécanismes moléculaires affectés par l'activation prolongée des MAPK1/3 seraient impliqués aussi bien dans la résistance des cellules tumorales aux traitements proapoptotiques que dans le développement des maladies neurodégénératives.
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Marina, García Noemí. "Complexos reguladors amb participació de proteïnes de la família NOD: estudis sobre la interacció entre Citocrom c i Apaf-1 a l'apoptosoma." Doctoral thesis, Universitat de Barcelona, 2007. http://hdl.handle.net/10803/1001.

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L'apoptosi o mort cel.lular programada és un procés central al desenvolupament, homeòstasi cel.lular, la resposta a l'estrés, l'envelliment i diferents malalties, als organismes eucariotes pluricel.lulars. Una de les vies que regula l'activació de l'apoptosi és la via intrinseca mitocondrial, a la que el citocrom c (Cit c), alliberat des de la mitocòndria en reposta a un estímul proapoptòtic, en presència de dATP indueix l'oligomerizació d'Apaf-1 (Apoptotic protease activating factor-1) i posterior reclutament de la caspasa-9, conduint a la formació del complex macromolecular activador de l'apoptosi anomenat apoptosoma. Citocroms de diferents vertebrats són equivalents en quant a la seva capacitat d'induir apoptosi a sistemes in vitro, mentre que el de llevat (YCit c) no presenta aquesta activitat. En concret s'ha determinat a partir d'estudis amb mutants derivats de HHCit c (citocrom c de cor de cavall) i YCit c, que els residus de Lys 7, 25, 39 i 72, així com els residus 62-65 dels citocroms de mamífer participen a la interacció amb Apaf-1. En base a aquests antecedents, i dins de la línia de treball iniciada al nostre laboratori encaminada al descobriment de molècules d'interès terapèutic relacionades amb l'apoptosi, es va plantejar com objetiu d'aquesta tesi l'estudi de la interacció entre Cit c i Apaf-1, com un pas preliminar per a l'obtenció de compostos orgànics capaços de modular aquesta interacció. En base als antecedents citats, es va proposar la generació de mutants de YCit c que incorporessin modificacions a la seva regió N-terminal que aproximessin la seva seqüència a la de HHCit c, per dotar-los d'activitat apoptòtica, així com pèptids derivats dels mateixos que mantinguessin unit el grup prostètic hemo. Les mutacions plantejades comprenien la delecció de la cua de cinc residus de l'extrem N-terminal de la seqüència de YCit c (Delta), i la substitució dels residus Ala 7 i Pro 25 d'aquest, per dos residus de Lys (A7K, P25K). Addicionalment es va introduir una Met a la possició 27 (K27M), que permetria generar els hemopèptids derivats dels mutants anteriors per degradació química amb BrCN. Per a la realització dels estudis de funcionalitat d'aquests derivats de YCit c, que comprenien assaigs in vitro d'activació de la caspasa -9 i -3, així com estudis de polarització de la fluorescència, es requeria disposar de la proteïna Apaf-1 en quantitat suficient, pel que es plantejà l'obtenció de dues construccions derivades d'Apaf-1-XL que poguessin expresar-se a E.coli, corresponents als dominis N-terminals CARD- NOD, constitutivament actius, i al C-terminal WDR, responsable de la interacció amb Cit c. Així, es van generar i caracteritzar mitjançant diferents tècniques espectroscòpiques, els mutants derivats de YCit c, YCit c (Delta/A7K/K27M), YCit c (Delta/P25K/K27M) i YCit c (Delta/A7K/P25K/K27M), així com l'hemopèptid derivat d'aquest, HP 7K25K 1-27. Igualment es van obtenir construccions derivades d'Apaf-1-XL que comprenien els residus 1-570 i 1-572, corresponents als dominis N-terminals, així com les que comprenien els residus 570-1248 i 583-1248, corresponents al domini C-terminal. Els estudis d'activació de caspases en cap cas van posar de manifest una capacitat proapoptòtica dels mutants generats. El mateix resultat negatiu es va obtenir per a l'hemopèptid anterior i pèptids sintètics derivats de la seqüència de HHCit c, sintetitzats al laboratori del grup col.laborador del Dr. E. Pérez- Payá (Centro de investigación Príncipe Felipe, València). No obstant, els estudis de polarització de la fluorescència van posar de manifest la capacitat del mutant YCit c (Delta/A7K/P25K/K27M) d'interaccionar amb Apaf-1. El conjunt d'aquests resultats indicava que les mutacions introduïdes a la seqüència de YCit c eren suficients per induir en aquest la capacitat per interaccionar amb Apaf-1, però no suficients per induir la formació de l'apoptosoma actiu. Per a l'hemopèptid es va determinar una potencial capacitat inhibidora de la formació de l'apoptosoma, que quedava emmascarada per l'efecte oxidatiu del grup prostètic hemo. Aquests mateixos assaigs van permetre establir la funcionalitat per a totes les proteïnes recombinants derivades d'Apaf-1-XL. Amb motiu d'una estada al laboratori del Profesor G. Núñez (University of Michigan, Ann Arbor, EUA) es plantejà un objetiu addicional que va consistir en la determinació dels components del complex de reconeixement del component bacterià muramil dipèptid (MDP), responsable de l'activació de la resposta inflamatòria mediada per Nod2, proteïna de la família NOD, a la que pertany igualment Apaf-1. Així, assaigs d'immunoprecipitació amb derivats del MDP, van indicar una interacció no directa entre aquest i Nod2. Mitjançant cromatografia d'afinitat i posterior anàlisi per espectrometria de masses s'han determinat potencials components del complex de reconeixement del MDP. Addicionalment, estudis preliminars de localizació cel.lular del MDP ha indicat que aquest seria incorporat per les cèl.lules de macròfag per la via endocítica.
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Kamber, Kaya Hatem E. "Regulation of the Drosophila Initiator Caspase Dronc through Ubiquitylation." eScholarship@UMMS, 2001. http://escholarship.umassmed.edu/gsbs_diss/885.

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Apoptosis is a programmed cell death mechanism that is evolutionary conserved from worms to humans. Apoptosis is mediated by initiator and effector caspases. The initiator caspases carry long pro-domains for their interaction with scaffolding proteins to form a cell-death platform, which is essential for their activation. Activated initiator caspases then cleave effector caspases that execute cell death through cleaving downstream targets. In addition to their apoptotic function, caspases also participate in events where caspase activity is not required for cell killing, but for regulating other functions, so-called non-apoptotic functions of caspases. The Drosophila initiator caspase Dronc, the ortholog of mammalian caspase-2 and caspase-9 has a CARD domain that is essential for its interaction with the scaffolding protein Dark to form the apoptosome. Apoptosome formation is crucial for activation of Dronc. Activity of both initiator and effector caspases are further kept in control by the ubiquitin system to avoid inappropriate caspase activity. However, mechanistic details of how the ubiquitin system regulates activation of Dronc are not clear. Therefore, I investigated the ubiquitylation status of Dronc and its function in Drosophila. I found that Dronc is mono-ubiquitylated at Lys78 (K78) in its CARD domain, which blocks its interaction with Dark and formation of the apoptosome. Furthermore, I demonstrated that K78 mono-ubiquitylation plays an inhibitory role in Dronc’s non-apoptotic functions, which may not require its catalytic activity but may be important for the survival of the fly. This thesis study unveils the link between the ubiquitin system and caspases through a regulatory mechanism where a single mono-ubiquitylation event could inhibit both apoptotic and non-apoptotic functions of a caspase.
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Kamber, Kaya Hatem E. "Regulation of the Drosophila Initiator Caspase Dronc through Ubiquitylation." eScholarship@UMMS, 2017. https://escholarship.umassmed.edu/gsbs_diss/885.

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Apoptosis is a programmed cell death mechanism that is evolutionary conserved from worms to humans. Apoptosis is mediated by initiator and effector caspases. The initiator caspases carry long pro-domains for their interaction with scaffolding proteins to form a cell-death platform, which is essential for their activation. Activated initiator caspases then cleave effector caspases that execute cell death through cleaving downstream targets. In addition to their apoptotic function, caspases also participate in events where caspase activity is not required for cell killing, but for regulating other functions, so-called non-apoptotic functions of caspases. The Drosophila initiator caspase Dronc, the ortholog of mammalian caspase-2 and caspase-9 has a CARD domain that is essential for its interaction with the scaffolding protein Dark to form the apoptosome. Apoptosome formation is crucial for activation of Dronc. Activity of both initiator and effector caspases are further kept in control by the ubiquitin system to avoid inappropriate caspase activity. However, mechanistic details of how the ubiquitin system regulates activation of Dronc are not clear. Therefore, I investigated the ubiquitylation status of Dronc and its function in Drosophila. I found that Dronc is mono-ubiquitylated at Lys78 (K78) in its CARD domain, which blocks its interaction with Dark and formation of the apoptosome. Furthermore, I demonstrated that K78 mono-ubiquitylation plays an inhibitory role in Dronc’s non-apoptotic functions, which may not require its catalytic activity but may be important for the survival of the fly. This thesis study unveils the link between the ubiquitin system and caspases through a regulatory mechanism where a single mono-ubiquitylation event could inhibit both apoptotic and non-apoptotic functions of a caspase.
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Kiechle, Tamara. "Apoptose als möglicher Pathomechanismus der Nervenzelldegeneration beim M. Huntington immunhistochemische und Western-Blot-Untersuchung menschlichen und transgenen murinen Post-mortem-Gehirngewebes zur Stadien-abhängigen Bildung der Komponenten des Apoptosom-Komplexes /." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=974902020.

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Kim, Hyun-Eui. "Biochemical analysis of apoptosome formation." 2006. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=215.

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Books on the topic "Apoptosomes"

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Cecconi, Francesco, and Marcello D'Amelio. Apoptosome: An up-and-coming therapeutical tool. Springer, 2010.

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Cecconi, Francesco, and Marcello D'Amelio, eds. Apoptosome. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-3415-1.

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Cecconi, Francesco, and Marcello D'Amelio. Apoptosome: An up-and-coming therapeutical tool. Springer, 2014.

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Cecconi, Francesco, and Marcello D'Amelio. Apoptosome: An up-and-coming therapeutical tool. Springer, 2010.

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Book chapters on the topic "Apoptosomes"

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Böning, Dieter, Michael I. Lindinger, Damian M. Bailey, et al. "Apoptosome." In Encyclopedia of Exercise Medicine in Health and Disease. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2113.

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Scherrmann, Jean-Michel, Kim Wolff, Christine A. Franco, et al. "Apoptosome." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1069.

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Cavallucci, Virve, and Marcello D’Amelio. "Physiological and Pathological Role of Apoptosis." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_1.

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Kuwano, Yuki, Imed-Eddine Gallouzi, and Myriam Gorospe. "Role of the RNA-Binding Protein HuR in Apoptosis and Apoptosome Function." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_10.

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Park, Sang Eun, and Young Hyun Yoo. "Acetylcholinesterase as a Pharmacological Target in Cancer Research." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_11.

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Rigou, Patricia, Audrey Faye, and Jean-Luc Poyet. "Putative Role of HCA66, A New Apaf-1 Interacting Protein, in the Physiopathology of NF1 Microdeletion Syndrome Patients." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_12.

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Scorrano, Luca. "Cristae Remodeling and Mitochondrial Fragmentation: A Checkpoint for Cytochrome c Release and Apoptosis?" In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_13.

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D’Amelio, Marcello, and Francesco Cecconi. "Apoptosome Pharmacological Manipulation: From Current Developments in the Laboratory to Clinical Implications." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_14.

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Kingston, Ross. "The Therapeutic Role of Taurine in Ischaemia-Reperfusion Injury." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_15.

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Tsuruma, Tetsuhiro, Hidekaz Kameshima, Yuji Iwayama, et al. "Targeting Survivin in Cancer Therapy: Clinical Considerations." In Apoptosome. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_16.

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Conference papers on the topic "Apoptosomes"

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Prudnikov, Igor, Anton Smirnov, and Volodymyr Tsyvkin. "Apoptosomes and proteasomes from exosomes generated by human hematopoietic stem cells." In Cell-to-Cell Metabolic Cross-Talk in Physiology and Pathology. MDPI, 2020. http://dx.doi.org/10.3390/cells2020-08924.

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Amer, Amal O., Anwari Akhter, Mikhail Gavrilin, et al. "The Role Of The Inflammasome And The Apoptosome In The Control Of Pulmonary Pathogens." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5643.

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Prabhu, Varun V., Michael Amadori, Honghao Zhang, Jason Pitaressi, Neelu Yadav, and Dhyan Chandra. "Abstract LB-47: Resveratrol induces Apaf-1 dependent but apoptosome-independent apoptosis in cancer cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-47.

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Prudnikov, Igor, Anton Smirnov, and Volodymyr Tsyvkin. "The actin cytoskeleton is a key element of the apoptosome assembly in the developing brain." In Cell-to-Cell Metabolic Cross-Talk in Physiology and Pathology. MDPI, 2020. http://dx.doi.org/10.3390/cells2020-08923.

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Fook Alves, Veruska Lia, Daniela B. Zanatta, mariana bleker oliveira, et al. "Abstract 1017: Silencing of apoptosome regulating genes, HSP70 and TRIAP1, induces apoptosis in MM cell lines." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1017.

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Reports on the topic "Apoptosomes"

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Kornbluth, Sally. Killing Breast Cancer Cells through Activation of the Apoptosome. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada499570.

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Kornbluth, Sally. Killing Breast Cancer Cells Through Activation of the Apoptosome. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada516650.

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