8 results on '"Lissitzky, Jean-Claude"'
Search Results
2. Supplementary Figure 1 from Cyclic AMP Signaling as a Mediator of Vasculogenic Mimicry in Aggressive Human Melanoma Cells In vitro
- Author
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Lissitzky, Jean-Claude, primary, Parriaux, Danielle, primary, Ristorcelli, Elodie, primary, Vérine, Alain, primary, Lombardo, Dominique, primary, and Verrando, Patrick, primary
- Published
- 2023
- Full Text
- View/download PDF
3. Supplementary Figure Legend from Cyclic AMP Signaling as a Mediator of Vasculogenic Mimicry in Aggressive Human Melanoma Cells In vitro
- Author
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Lissitzky, Jean-Claude, primary, Parriaux, Danielle, primary, Ristorcelli, Elodie, primary, Vérine, Alain, primary, Lombardo, Dominique, primary, and Verrando, Patrick, primary
- Published
- 2023
- Full Text
- View/download PDF
4. GRASP55 Is Dispensable for Normal Hematopoiesis but Necessary for Myc-Dependent Leukemic Growth
- Author
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Bailly, Anne-Laure, primary, Grenier, Julien M. P., additional, Cartier-Michaud, Amandine, additional, Bardin, Florence, additional, Balzano, Marielle, additional, Goubard, Armelle, additional, Lissitzky, Jean-Claude, additional, De Grandis, Maria, additional, Mancini, Stéphane J. C., additional, Serge, Arnauld, additional, and Aurrand-Lions, Michel, additional
- Published
- 2020
- Full Text
- View/download PDF
5. Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis
- Author
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Cartier-Michaud, Amandine, Bailly, Anne-Laure, Betzi, Stéphane, Shi, Xiaoli, Lissitzky, Jean-Claude, Zarubica, Ana, Sergé, Arnauld, ROCHE, Philippe, Lugari, Adrien, HAMON, Véronique, Bardin, Florence, Derviaux, Carine, Lembo, Frédérique, Audebert, Stéphane, Marchetto, Sylvie, Durand, Bénédicte, Borg, Jean-Paul, Shi, Ning, Morelli, Xavier, Aurrand-Lions, Michel, Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC), Centre de Recherche en Cancérologie de Marseille (CRCM), Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), ANR-11-IDEX-0001,Amidex,INITIATIVE D'EXCELLENCE AIX MARSEILLE UNIVERSITE(2011), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
- Subjects
Male ,Physiology ,[SDV]Life Sciences [q-bio] ,Golgi Apparatus ,Mice ,Animal Cells ,Reproductive Physiology ,Spermatocytes ,Medicine and Health Sciences ,Cell Cycle and Cell Division ,Testes ,Cells, Cultured ,Staining ,Chromosome Biology ,Intracellular Signaling Peptides and Proteins ,Specimen preparation and treatment ,Spermatids ,humanities ,Protein Transport ,Meiosis ,Seminiferous tubules ,Cell Processes ,cardiovascular system ,Cellular Types ,Anatomy ,Cellular Structures and Organelles ,Genital Anatomy ,Protein Binding ,Research Article ,endocrine system ,lcsh:QH426-470 ,education ,Immunoglobulins ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,Germ cells ,Acrosomes ,Animals ,Spermatogenesis ,Binding Sites ,fungi ,Reproductive System ,DAPI staining ,Membrane Proteins ,Biology and Life Sciences ,Cell Biology ,Spermatogonia ,Sperm ,Mice, Inbred C57BL ,Research and analysis methods ,lcsh:Genetics ,Nuclear staining ,Carrier Proteins ,Cell Adhesion Molecules - Abstract
Spermatogenesis is a dynamic process that is regulated by adhesive interactions between germ and Sertoli cells. Germ cells express the Junctional Adhesion Molecule-C (JAM-C, encoded by Jam3), which localizes to germ/Sertoli cell contacts. JAM-C is involved in germ cell polarity and acrosome formation. Using a proteomic approach, we demonstrated that JAM-C interacted with the Golgi reassembly stacking protein of 55 kDa (GRASP55, encoded by Gorasp2) in developing germ cells. Generation and study of Gorasp2-/- mice revealed that knock-out mice suffered from spermatogenesis defects. Acrosome formation and polarized localization of JAM-C in spermatids were altered in Gorasp2-/- mice. In addition, Golgi morphology of spermatocytes was disturbed in Gorasp2-/- mice. Crystal structures of GRASP55 in complex with JAM-C or JAM-B revealed that GRASP55 interacted via PDZ-mediated interactions with JAMs and induced a conformational change in GRASP55 with respect of its free conformation. An in silico pharmacophore approach identified a chemical compound called Graspin that inhibited PDZ-mediated interactions of GRASP55 with JAMs. Treatment of mice with Graspin hampered the polarized localization of JAM-C in spermatids, induced the premature release of spermatids and affected the Golgi morphology of meiotic spermatocytes., Author summary Spermatogenesis defects are a common cause of male sterility. Spermatogenesis occurs in the seminiferous tubules of the testes and involves adhesive interactions between developing germ cells and Sertoli cells. Knock-out mouse models identified several adhesion molecules that are critically involved in spermatogenesis. We previously demonstrated that the Junctional Adhesion Molecule-C (JAM-C) plays a crucial role in establishing spermatids polarity. The latter involves rearrangements of the Golgi apparatus in spermatids which contribute to acrosome formation. The present study demonstrated that the C-terminal cytosolic region of JAM-C interacted with the Golgi reassembly stacking protein of 55 kDa (GRASP55) encoded by Gorasp2 and that spermatogenesis was impaired in Gorasp2-deficient mice. We developed an inhibitor of GRASP55 interaction with JAM-C and demonstrated that treatment of wild-type mice with the inhibitory compound induced germ cell loss. Therefore, the male infertility-associated pathway identified in this study is important not only from a genetic point of view, but also as a potential target for male contraception.
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- 2017
6. Protein-Protein Interaction Inhibition (2P21)-Oriented Chemical Library Accelerates Hit Discovery
- Author
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Milhas, Sabine, Raux, Brigitt, Betzi, Stephane, Derviaux, Carine, Roche, Philippe, Restouin, Audrey, Basse, Marie-Jeanne, Rebuffet, Etienne, Lugari, Adrien, Badol, Marion, Kashyap, Rudra, Lissitzky, Jean-Claude, Eydoux, Cecilia, Hamon, Veronique, Gourde, Marie -Edith, Combes, Sebastien, Zimmermann, Pascale, Aurrand-Lions, Michel, Roux, Thomas, Rogers, Catherine, Muller, Susanne, Knapp, Stefan, Trinquet, Eric, Collette, Yves, Guillemot, Jean-Claude, Morelli, Xavier, Architecture et fonction des macromolécules biologiques (AFMB), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM] ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience; no abstract
- Published
- 2016
7. Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis.
- Author
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Cartier-Michaud A, Bailly AL, Betzi S, Shi X, Lissitzky JC, Zarubica A, Sergé A, Roche P, Lugari A, Hamon V, Bardin F, Derviaux C, Lembo F, Audebert S, Marchetto S, Durand B, Borg JP, Shi N, Morelli X, and Aurrand-Lions M
- Subjects
- Animals, Binding Sites, Carrier Proteins chemistry, Carrier Proteins genetics, Cells, Cultured, Golgi Apparatus ultrastructure, Intracellular Signaling Peptides and Proteins, Male, Membrane Proteins chemistry, Membrane Proteins genetics, Mice, Mice, Inbred C57BL, Protein Binding, Protein Transport, Spermatogonia cytology, Carrier Proteins metabolism, Cell Adhesion Molecules metabolism, Golgi Apparatus metabolism, Immunoglobulins metabolism, Membrane Proteins metabolism, Spermatogenesis, Spermatogonia metabolism
- Abstract
Spermatogenesis is a dynamic process that is regulated by adhesive interactions between germ and Sertoli cells. Germ cells express the Junctional Adhesion Molecule-C (JAM-C, encoded by Jam3), which localizes to germ/Sertoli cell contacts. JAM-C is involved in germ cell polarity and acrosome formation. Using a proteomic approach, we demonstrated that JAM-C interacted with the Golgi reassembly stacking protein of 55 kDa (GRASP55, encoded by Gorasp2) in developing germ cells. Generation and study of Gorasp2-/- mice revealed that knock-out mice suffered from spermatogenesis defects. Acrosome formation and polarized localization of JAM-C in spermatids were altered in Gorasp2-/- mice. In addition, Golgi morphology of spermatocytes was disturbed in Gorasp2-/- mice. Crystal structures of GRASP55 in complex with JAM-C or JAM-B revealed that GRASP55 interacted via PDZ-mediated interactions with JAMs and induced a conformational change in GRASP55 with respect of its free conformation. An in silico pharmacophore approach identified a chemical compound called Graspin that inhibited PDZ-mediated interactions of GRASP55 with JAMs. Treatment of mice with Graspin hampered the polarized localization of JAM-C in spermatids, induced the premature release of spermatids and affected the Golgi morphology of meiotic spermatocytes.
- Published
- 2017
- Full Text
- View/download PDF
8. Protein-Protein Interaction Inhibition (2P2I)-Oriented Chemical Library Accelerates Hit Discovery.
- Author
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Milhas S, Raux B, Betzi S, Derviaux C, Roche P, Restouin A, Basse MJ, Rebuffet E, Lugari A, Badol M, Kashyap R, Lissitzky JC, Eydoux C, Hamon V, Gourdel ME, Combes S, Zimmermann P, Aurrand-Lions M, Roux T, Rogers C, Müller S, Knapp S, Trinquet E, Collette Y, Guillemot JC, and Morelli X
- Subjects
- Crystallography, X-Ray, Protein Interaction Mapping, Drug Discovery, Proteins chemistry, Small Molecule Libraries
- Abstract
Protein-protein interactions (PPIs) represent an enormous source of opportunity for therapeutic intervention. We and others have recently pinpointed key rules that will help in identifying the next generation of innovative drugs to tackle this challenging class of targets within the next decade. We used these rules to design an oriented chemical library corresponding to a set of diverse "PPI-like" modulators with cores identified as privileged structures in therapeutics. In this work, we purchased the resulting 1664 structurally diverse compounds and evaluated them on a series of representative protein-protein interfaces with distinct "druggability" potential using homogeneous time-resolved fluorescence (HTRF) technology. For certain PPI classes, analysis of the hit rates revealed up to 100 enrichment factors compared with nonoriented chemical libraries. This observation correlates with the predicted "druggability" of the targets. A specific focus on selectivity profiles, the three-dimensional (3D) molecular modes of action resolved by X-ray crystallography, and the biological activities of identified hits targeting the well-defined "druggable" bromodomains of the bromo and extraterminal (BET) family are presented as a proof-of-concept. Overall, our present study illustrates the potency of machine learning-based oriented chemical libraries to accelerate the identification of hits targeting PPIs. A generalization of this method to a larger set of compounds will accelerate the discovery of original and potent probes for this challenging class of targets.
- Published
- 2016
- Full Text
- View/download PDF
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