Chypre M, Seaman J, Cordeiro O G, Willen L, Knoop K A, Buchanan A, Sainson R C, Williams I R, Yagita H, Schneider P, Mueller C G
Characterization and application of two RANK-specific antibodies with different biological activities Journal Article
In: Immunol.Lett., vol. 171, no. 1879-0542 (Electronic), pp. 5–14, 2016.
Abstract | Links | BibTeX | Tags: Activation, Animals, ANTAGONIST, Antibodies, antibody, Antibody Affinity, Apoptosis, Assay, Cell Differentiation, Cell Surface Display Techniques, Cellular, Chemistry, comparison, Dendritic Cells, DERMAL DENDRITIC CELLS, Epithelial Cells, Epithelial microfold cell, Epitopes, Fusion, FUSION PROTEIN, HEK293 Cells, Homeostasis, Human, Humans, immune regulation, Immunization, Immunology, Immunomodulation, immunopathology, In vivo, Inbred C57BL, Intestines, Jurkat Cells, Langerhans cell, Langerhans Cells, Mice, Monoclonal, monoclonal antibody, MONOCLONAL-ANTIBODY, mouse, NF-kappa B, NF-kappaB, pathology, Protein, rank, RANK (TNFRSF11a), Receptor, Receptor Activator of Nuclear Factor-kappa B, Regulation, Secondary, Signal Transduction, signaling, Team-Mueller, therapy
@article{chypre_characterization_2016,
title = {Characterization and application of two RANK-specific antibodies with different biological activities},
author = {M Chypre and J Seaman and O G Cordeiro and L Willen and K A Knoop and A Buchanan and R C Sainson and I R Williams and H Yagita and P Schneider and C G Mueller},
doi = {10.1016/j.imlet.2016.01.003},
year = {2016},
date = {2016-03-01},
journal = {Immunol.Lett.},
volume = {171},
number = {1879-0542 (Electronic)},
pages = {5--14},
abstract = {Antibodies play an important role in therapy and investigative biomedical research. The TNF-family member Receptor Activator of NF-kappaB (RANK) is known for its role in bone homeostasis and is increasingly recognized as a central player in immune regulation and epithelial cell activation. However, the study of RANK biology has been hampered by missing or insufficient characterization of high affinity tools that recognize RANK. Here, we present a careful description and comparison of two antibodies, RANK-02 obtained by phage display (Newa, 2014 [1]) and R12-31 generated by immunization (Kamijo, 2006 [2]). We found that both antibodies recognized mouse RANK with high affinity, while RANK-02 and R12-31 recognized human RANK with high and lower affinities, respectively. Using a cell apoptosis assay based on stimulation of a RANK:Fas fusion protein, and a cellular NF-kappaB signaling assay, we showed that R12-31 was agonist for both species. R12-31 interfered little or not at all with the binding of RANKL to RANK, in contrast to RANK-02 that efficiently prevented this interaction. Depending on the assay and species, RANK-02 was either a weak agonist or a partial antagonist of RANK. Both antibodies recognized human Langerhans cells, previously shown to express RANK, while dermal dendritic cells were poorly labeled. In vivo R12-31 agonist activity was demonstrated by its ability to induce the formation of intestinal villous microfold cells in mice. This characterization of two monoclonal antibodies should now allow better evaluation of their application as therapeutic reagents and investigative tools},
keywords = {Activation, Animals, ANTAGONIST, Antibodies, antibody, Antibody Affinity, Apoptosis, Assay, Cell Differentiation, Cell Surface Display Techniques, Cellular, Chemistry, comparison, Dendritic Cells, DERMAL DENDRITIC CELLS, Epithelial Cells, Epithelial microfold cell, Epitopes, Fusion, FUSION PROTEIN, HEK293 Cells, Homeostasis, Human, Humans, immune regulation, Immunization, Immunology, Immunomodulation, immunopathology, In vivo, Inbred C57BL, Intestines, Jurkat Cells, Langerhans cell, Langerhans Cells, Mice, Monoclonal, monoclonal antibody, MONOCLONAL-ANTIBODY, mouse, NF-kappa B, NF-kappaB, pathology, Protein, rank, RANK (TNFRSF11a), Receptor, Receptor Activator of Nuclear Factor-kappa B, Regulation, Secondary, Signal Transduction, signaling, Team-Mueller, therapy},
pubstate = {published},
tppubtype = {article}
}
Al-Jamal Khuloud T, Gherardini Lisa, Bardi Giuseppe, Nunes Antonio, Guo Chang, Bussy Cyrill, Herrero Antonia M, Bianco Alberto, Prato Maurizio, Kostarelos Kostas, Pizzorusso Tommaso
Functional motor recovery from brain ischemic insult by carbon nanotube-mediated siRNA silencing Journal Article
In: Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 27, pp. 10952–10957, 2011, ISSN: 1091-6490.
Abstract | Links | BibTeX | Tags: Animals, Apoptosis, Base Sequence, Brain Ischemia, carbon, Caspase 3, Caspase Inhibitors, Cell Line, Cells, Cultured, Electron, Endothelin-1, Female, Genetic Therapy, I2CT, Inbred C57BL, Mice, Microscopy, Nanomedicine, Nanotubes, Neurons, Psychomotor Performance, Rats, RNA, RNA Interference, Small Interfering, Sprague-Dawley, Team-Bianco, Transmission
@article{al-jamal_functional_2011,
title = {Functional motor recovery from brain ischemic insult by carbon nanotube-mediated siRNA silencing},
author = {Khuloud T Al-Jamal and Lisa Gherardini and Giuseppe Bardi and Antonio Nunes and Chang Guo and Cyrill Bussy and Antonia M Herrero and Alberto Bianco and Maurizio Prato and Kostas Kostarelos and Tommaso Pizzorusso},
doi = {10.1073/pnas.1100930108},
issn = {1091-6490},
year = {2011},
date = {2011-07-01},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
volume = {108},
number = {27},
pages = {10952--10957},
abstract = {Stroke is the second cause of death worldwide with ischemic stroke accounting for 80% of all stroke insults. Caspase-3 activation contributes to brain tissue loss and downstream biochemical events that lead to programmed cell death after traumatic brain injury. Alleviation of symptoms following ischemic neuronal injury can be potentially achieved by either genetic disruption or pharmacological inhibition of caspases. Here, we studied whether silencing of Caspase-3 using carbon nanotube-mediated in vivo RNA interference (RNAi) could offer a therapeutic opportunity against stroke. Effective delivery of siRNA directly to the CNS has been shown to normalize phenotypes in animal models of several neurological diseases. It is shown here that peri-lesional stereotactic administration of a Caspase-3 siRNA (siCas 3) delivered by functionalized carbon nanotubes (f-CNT) reduced neurodegeneration and promoted functional preservation before and after focal ischemic damage of the rodent motor cortex using an endothelin-1 induced stroke model. These observations illustrate the opportunity offered by carbon nanotube-mediated siRNA delivery and gene silencing of neuronal tissue applicable to a variety of different neuropathological conditions where intervention at well localized brain foci may offer therapeutic and functional benefits.},
keywords = {Animals, Apoptosis, Base Sequence, Brain Ischemia, carbon, Caspase 3, Caspase Inhibitors, Cell Line, Cells, Cultured, Electron, Endothelin-1, Female, Genetic Therapy, I2CT, Inbred C57BL, Mice, Microscopy, Nanomedicine, Nanotubes, Neurons, Psychomotor Performance, Rats, RNA, RNA Interference, Small Interfering, Sprague-Dawley, Team-Bianco, Transmission},
pubstate = {published},
tppubtype = {article}
}
Garcia Alvaro Baeza, Pierce Raymond J, Gourbal Benjamin, Werkmeister Elisabeth, Colinet Dominique, Reichhart Jean-Marc, Dissous Colette, Coustau Christine
Involvement of the cytokine MIF in the snail host immune response to the parasite Schistosoma mansoni Journal Article
In: PLoS Pathog., vol. 6, no. 9, pp. e1001115, 2010, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Amino Acid, Animals, Apoptosis, Biomphalaria, Blotting, Cell Proliferation, Cells, Cricetinae, Cultured, Hemocytes, Host-Parasite Interactions, Humans, Liver, M3i, Macrophage Migration-Inhibitory Factors, messenger, Oocysts, Recombinant Proteins, reichhart, Reverse Transcriptase Polymerase Chain Reaction, RNA, Schistosoma mansoni, Schistosomiasis mansoni, Sequence Homology, Small Interfering, Western
@article{baeza_garcia_involvement_2010,
title = {Involvement of the cytokine MIF in the snail host immune response to the parasite Schistosoma mansoni},
author = {Alvaro Baeza Garcia and Raymond J Pierce and Benjamin Gourbal and Elisabeth Werkmeister and Dominique Colinet and Jean-Marc Reichhart and Colette Dissous and Christine Coustau},
doi = {10.1371/journal.ppat.1001115},
issn = {1553-7374},
year = {2010},
date = {2010-01-01},
journal = {PLoS Pathog.},
volume = {6},
number = {9},
pages = {e1001115},
abstract = {We have identified and characterized a Macrophage Migration Inhibitory Factor (MIF) family member in the Lophotrochozoan invertebrate, Biomphalaria glabrata, the snail intermediate host of the human blood fluke Schistosoma mansoni. In mammals, MIF is a widely expressed pleiotropic cytokine with potent pro-inflammatory properties that controls cell functions such as gene expression, proliferation or apoptosis. Here we show that the MIF protein from B. glabrata (BgMIF) is expressed in circulating immune defense cells (hemocytes) of the snail as well as in the B. glabrata embryonic (Bge) cell line that has hemocyte-like features. Recombinant BgMIF (rBgMIF) induced cell proliferation and inhibited NO-dependent p53-mediated apoptosis in Bge cells. Moreover, knock-down of BgMIF expression in Bge cells interfered with the in vitro encapsulation of S. mansoni sporocysts. Furthermore, the in vivo knock-down of BgMIF prevented the changes in circulating hemocyte populations that occur in response to an infection by S. mansoni miracidia and led to a significant increase in the parasite burden of the snails. These results provide the first functional evidence that a MIF ortholog is involved in an invertebrate immune response towards a parasitic infection and highlight the importance of cytokines in invertebrate-parasite interactions.},
keywords = {Amino Acid, Animals, Apoptosis, Biomphalaria, Blotting, Cell Proliferation, Cells, Cricetinae, Cultured, Hemocytes, Host-Parasite Interactions, Humans, Liver, M3i, Macrophage Migration-Inhibitory Factors, messenger, Oocysts, Recombinant Proteins, reichhart, Reverse Transcriptase Polymerase Chain Reaction, RNA, Schistosoma mansoni, Schistosomiasis mansoni, Sequence Homology, Small Interfering, Western},
pubstate = {published},
tppubtype = {article}
}
Podesta Jennifer E, Al-Jamal Khuloud T, Herrero Antonia M, Tian Bowen, Ali-Boucetta Hanene, Hegde Vikas, Bianco Alberto, Prato Maurizio, Kostarelos Kostas
Antitumor activity and prolonged survival by carbon-nanotube-mediated therapeutic siRNA silencing in a human lung xenograft model Journal Article
In: Small (Weinheim an Der Bergstrasse, Germany), vol. 5, no. 10, pp. 1176–1185, 2009, ISSN: 1613-6829.
Abstract | Links | BibTeX | Tags: Animals, Antineoplastic Agents, Apoptosis, carbon, Cell Line, Cell Proliferation, Electrophoresis, Gene Silencing, Humans, I2CT, Liposomes, Lung Neoplasms, Mice, Nanomedicine, Nanotubes, RNA, Small Interfering, Survival Analysis, Team-Bianco, tumor, Xenograft Model Antitumor Assays
@article{podesta_antitumor_2009,
title = {Antitumor activity and prolonged survival by carbon-nanotube-mediated therapeutic siRNA silencing in a human lung xenograft model},
author = {Jennifer E Podesta and Khuloud T Al-Jamal and Antonia M Herrero and Bowen Tian and Hanene Ali-Boucetta and Vikas Hegde and Alberto Bianco and Maurizio Prato and Kostas Kostarelos},
doi = {10.1002/smll.200801572},
issn = {1613-6829},
year = {2009},
date = {2009-05-01},
journal = {Small (Weinheim an Der Bergstrasse, Germany)},
volume = {5},
number = {10},
pages = {1176--1185},
abstract = {Carbon nanotubes are novel nanomaterials that are thought to offer potential benefits to a variety of biomedical and clinical applications. In this study, the treatment of a human lung carcinoma model in vivo using siRNA sequences leading to cytotoxicity and cell death is carried out using either cationic liposomes (DOTAP:cholesterol) or amino-functionalized multi-walled carbon nanotubes (MWNT - NH(+)(3)). Validation for the most cytotoxic siRNA sequence using a panel of human carcinoma and murine cells reveals that the proprietary siTOX sequence is human specific and can lead to significant cytotoxic activities delivered both by liposome or MWNT - NH(+)(3) in vitro. A comparative study using both types of vector indicates that only MWNT - NH(+)(3):siRNA complexes administered intratumorally can elicit delayed tumor growth and increased survival of xenograft-bearing animals. siTOX delivery via the cationic MWNT - NH(+)(3) is biologically active in vivo by triggering an apoptotic cascade, leading to extensive necrosis of the human tumor mass. This suggests that carbon-nanotube-mediated delivery of siRNA by intratumoral administration leads to successful and statistically significant suppression of tumor volume, followed by a concomitant prolongation of survival of human lung tumor-bearing animals. The direct comparison between carbon nanotubes and liposomes demonstrates the potential advantages offered by carbon nanotubes for the intracellular delivery of therapeutic agents in vivo. The present work may act as the impetus for further studies to explore the therapeutic capacity of chemically functionalized carbon nanotubes to deliver siRNA directly into the cytoplasm of target cells and achieve effective therapeutic silencing in various disease indications where local delivery is feasible or desirable.},
keywords = {Animals, Antineoplastic Agents, Apoptosis, carbon, Cell Line, Cell Proliferation, Electrophoresis, Gene Silencing, Humans, I2CT, Liposomes, Lung Neoplasms, Mice, Nanomedicine, Nanotubes, RNA, Small Interfering, Survival Analysis, Team-Bianco, tumor, Xenograft Model Antitumor Assays},
pubstate = {published},
tppubtype = {article}
}
Dieker J, Cisterna B, Monneaux F, Decossas M, van der Vlag J, Biggiogera M, Muller S
Apoptosis-linked changes in the phosphorylation status and subcellular localization of the spliceosomal autoantigen U1-70K Journal Article
In: Cell Death and Differentiation, vol. 15, no. 4, pp. 793–804, 2008, ISSN: 1350-9047.
Abstract | Links | BibTeX | Tags: Apoptosis, Autoantigens, Autoimmunity, Caspase 3, Chromatin, HeLa Cells, Humans, I2CT, Jurkat Cells, Lupus Erythematosus, Monneaux, Phosphorylation, Post-Translational, Protein Phosphatase 1, Protein Processing, Protein Transport, Recombinant Proteins, Ribonucleoprotein, RNA Splicing, Serine, Spliceosomes, Systemic, Team-Dumortier, Time Factors, U1 Small Nuclear
@article{dieker_apoptosis-linked_2008,
title = {Apoptosis-linked changes in the phosphorylation status and subcellular localization of the spliceosomal autoantigen U1-70K},
author = {J Dieker and B Cisterna and F Monneaux and M Decossas and J van der Vlag and M Biggiogera and S Muller},
doi = {10.1038/sj.cdd.4402312},
issn = {1350-9047},
year = {2008},
date = {2008-01-01},
journal = {Cell Death and Differentiation},
volume = {15},
number = {4},
pages = {793--804},
abstract = {Apoptosis consists of highly regulated pathways involving post-translational modifications and cleavage of proteins leading to sequential inactivation of the main cellular processes. Here, we focused on the apoptotic processing of one of the essential components of the mRNA splicing machinery, the U1-70K snRNP protein. We found that at an early stage of apoptosis, before the cleavage of the C-terminal part of the protein by caspase-3, the basal phosphorylation of the Ser140 residue located within the RNA recognition motif, increases very significantly. A caspase-dependent, PP1-mediated dephosphorylation of other serine residues takes place in a subset of U1-70K proteins. The U1-70K protein phosphorylated at Ser140 is clustered in heterogeneous ectopic RNP-derived structures, which are finally extruded in apoptotic bodies. The elaborate processing of the spliceosomal U1-70K protein we identified might play an important role in the regulated breakdown of the mRNA splicing machinery during early apoptosis. In addition, these specific changes in the phosphorylation/dephosphorylation balance and the subcellular localization of the U1-70K protein might explain why the region encompassing the Ser140 residue becomes a central autoantigen during the autoimmune disease systemic lupus erythematosus.},
keywords = {Apoptosis, Autoantigens, Autoimmunity, Caspase 3, Chromatin, HeLa Cells, Humans, I2CT, Jurkat Cells, Lupus Erythematosus, Monneaux, Phosphorylation, Post-Translational, Protein Phosphatase 1, Protein Processing, Protein Transport, Recombinant Proteins, Ribonucleoprotein, RNA Splicing, Serine, Spliceosomes, Systemic, Team-Dumortier, Time Factors, U1 Small Nuclear},
pubstate = {published},
tppubtype = {article}
}
Barbaroux J B, Beleut M, Brisken C, Mueller C G, Groves R W
Epidermal receptor activator of NF-kappaB ligand controls Langerhans cells numbers and proliferation Journal Article
In: Journal of Immunology, vol. 181, no. 1550-6606 (Electronic), pp. 1103–1108, 2008.
Abstract | BibTeX | Tags: APC, Apoptosis, BLOOD, Cell Count, Cell Proliferation, Cell Survival, Culture, cytology, Dendritic Cells, DERMATOLOGY, Differentiation, Epidermis, Expression, Homeostasis, Human, Humans, Immunology, IN VITRO, In vivo, KERATINOCYTES, Langerhans Cells, ligand, metabolism, Mice, NF-kappa B, NF-kappaB, OSTEOCLAST, Osteoclasts, Proliferation, Protein, rank, RANK ligand, Receptor, Receptor Activator of Nuclear Factor-kappa B, Regulation, Signal Transduction, Skin, survival, Team-Mueller, viability
@article{barbaroux_epidermal_2008,
title = {Epidermal receptor activator of NF-kappaB ligand controls Langerhans cells numbers and proliferation},
author = {J B Barbaroux and M Beleut and C Brisken and C G Mueller and R W Groves},
year = {2008},
date = {2008-01-01},
journal = {Journal of Immunology},
volume = {181},
number = {1550-6606 (Electronic)},
pages = {1103--1108},
abstract = {Langerhans cells (LC) are the dendritic APC population of the epidermis, where they reside for long periods and are self-replicating. The molecular signals underlying these characteristics are unknown. The TNF superfamily member receptor activator of NF-kappaB ligand (RANKL, TNFSF11) has been shown to sustain viability of blood dendritic cells in addition to its role in promoting proliferation and differentiation of several cell types, notably osteoclasts. In this study, we have studied expression of the RANKL system in skin and have defined a key role for this molecule in LC homeostasis. In vitro and in vivo, human KC expressed RANKL and epidermal LC expressed cell surface RANK. In vitro, RANKL sustained CD34(+) progenitor-derived LC viability following 72-h cultures in cytokine-free medium (79.5 +/- 1% vs 55.2 +/- 5.7% live cells, respectively; n = 4; p textless 0.05). In vivo, RANKL-deficient mice displayed a marked reduction in epidermal LC density (507.1 +/- 77.2 vs 873.6 +/- 41.6 LC per mm(2); n = 9; p textless 0.05) and their proliferation was impaired without a detectable effect on apoptosis. These data indicate a key role for the RANKL system in the regulation of LC survival within the skin and suggest a regulatory role for KC in the maintenance of epidermal LC homeostasis},
keywords = {APC, Apoptosis, BLOOD, Cell Count, Cell Proliferation, Cell Survival, Culture, cytology, Dendritic Cells, DERMATOLOGY, Differentiation, Epidermis, Expression, Homeostasis, Human, Humans, Immunology, IN VITRO, In vivo, KERATINOCYTES, Langerhans Cells, ligand, metabolism, Mice, NF-kappa B, NF-kappaB, OSTEOCLAST, Osteoclasts, Proliferation, Protein, rank, RANK ligand, Receptor, Receptor Activator of Nuclear Factor-kappa B, Regulation, Signal Transduction, Skin, survival, Team-Mueller, viability},
pubstate = {published},
tppubtype = {article}
}
Ferrandon Dominique
Ubiquitin-proteasome: pallbearer carries the deceased to the grave Journal Article
In: Immunity, vol. 27, no. 4, pp. 541–544, 2007, ISSN: 1074-7613.
Abstract | Links | BibTeX | Tags: *Models, Animals, Apoptosis, Apoptosis/*physiology, ferrandon, Immunological, M3i, Macrophages, Macrophages/immunology/metabolism, Models, Phagocytosis, Phagocytosis/*physiology, Proteasome Endopeptidase Complex, Proteasome Endopeptidase Complex/*metabolism, ubiquitin, Ubiquitin/*metabolism
@article{ferrandon_ubiquitin-proteasome:_2007b,
title = {Ubiquitin-proteasome: pallbearer carries the deceased to the grave},
author = {Dominique Ferrandon},
doi = {10.1016/j.immuni.2007.10.003},
issn = {1074-7613},
year = {2007},
date = {2007-10-01},
journal = {Immunity},
volume = {27},
number = {4},
pages = {541--544},
abstract = {Phagocytosis is a complex process that involves multiple cellular functions. In this issue of Immunity, Silva et al. (2007) report that a protein ubiquitylation complex and the proteasome are required for the clearance of apoptotic cells in Drosophila.},
keywords = {*Models, Animals, Apoptosis, Apoptosis/*physiology, ferrandon, Immunological, M3i, Macrophages, Macrophages/immunology/metabolism, Models, Phagocytosis, Phagocytosis/*physiology, Proteasome Endopeptidase Complex, Proteasome Endopeptidase Complex/*metabolism, ubiquitin, Ubiquitin/*metabolism},
pubstate = {published},
tppubtype = {article}
}
Bianco Alberto, Fournel Sylvie, Wieckowski Sébastien, Hoebeke Johan, Guichard Gilles
Solid-phase synthesis of CD40L mimetics Journal Article
In: Organic & Biomolecular Chemistry, vol. 4, no. 8, pp. 1461–1463, 2006, ISSN: 1477-0520.
Abstract | Links | BibTeX | Tags: Apoptosis, CD40 Ligand, Cell Line, Chromatography, Combinatorial Chemistry Techniques, High Pressure Liquid, Humans, I2CT, Molecular Mimicry, Molecular Structure, Protein Binding, Team-Bianco, tumor
@article{bianco_solid-phase_2006,
title = {Solid-phase synthesis of CD40L mimetics},
author = {Alberto Bianco and Sylvie Fournel and Sébastien Wieckowski and Johan Hoebeke and Gilles Guichard},
doi = {10.1039/b601528j},
issn = {1477-0520},
year = {2006},
date = {2006-04-01},
journal = {Organic & Biomolecular Chemistry},
volume = {4},
number = {8},
pages = {1461--1463},
abstract = {The C3-symmetric molecule has been previously shown to mimic CD40 ligand (CD40L) homotrimers and to display effector functions. This molecule consists of a cyclic hexapeptide core containing the repetition of the D-Ala-L-Lys motif. The side chains of the lysine residues have been modified by appending the CD40L-derived sequence 143Lys-Gly-Tyr-Tyr146 via a 6-aminohexanoic acid residue as a spacer. The present report describes a general solid-phase synthesis approach to and related trimeric architectures. In addition, their CD40 binding properties as well as their effector functions have been evaluated.},
keywords = {Apoptosis, CD40 Ligand, Cell Line, Chromatography, Combinatorial Chemistry Techniques, High Pressure Liquid, Humans, I2CT, Molecular Mimicry, Molecular Structure, Protein Binding, Team-Bianco, tumor},
pubstate = {published},
tppubtype = {article}
}
Fournel Sylvie, Wieckowski Sébastien, Sun Weimin, Trouche Nathalie, Dumortier Hélène, Bianco Alberto, Chaloin Olivier, Habib Mohammed, Peter Jean-Christophe, Schneider Pascal, Vray Bernard, Toes René E, Offringa Rienk, Melief Cornelis J M, Hoebeke Johan, Guichard Gilles
C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L Journal Article
In: Nature Chemical Biology, vol. 1, no. 7, pp. 377–382, 2005, ISSN: 1552-4450.
Abstract | Links | BibTeX | Tags: Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Dumortier, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Team-Dumortier, Time Factors, tumor
@article{fournel_c3-symmetric_2005,
title = {C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L},
author = {Sylvie Fournel and Sébastien Wieckowski and Weimin Sun and Nathalie Trouche and Hélène Dumortier and Alberto Bianco and Olivier Chaloin and Mohammed Habib and Jean-Christophe Peter and Pascal Schneider and Bernard Vray and René E Toes and Rienk Offringa and Cornelis J M Melief and Johan Hoebeke and Gilles Guichard},
doi = {10.1038/nchembio746},
issn = {1552-4450},
year = {2005},
date = {2005-12-01},
journal = {Nature Chemical Biology},
volume = {1},
number = {7},
pages = {377--382},
abstract = {Interaction between CD40, a member of the tumor necrosis factor receptor (TNFR) superfamily, and its ligand CD40L, a 39-kDa glycoprotein, is essential for the development of humoral and cellular immune responses. Selective blockade or activation of this pathway provides the ground for the development of new treatments against immunologically based diseases and malignancies. Like other members of the TNF superfamily, CD40L monomers self-assemble around a threefold symmetry axis to form noncovalent homotrimers that can each bind three receptor molecules. Here, we report on the structure-based design of small synthetic molecules with C3 symmetry that can mimic CD40L homotrimers. These molecules interact with CD40, compete with the binding of CD40L to CD40, and reproduce, to a certain extent, the functional properties of the much larger homotrimeric soluble CD40L. Architectures based on rigid C3-symmetric cores may thus represent a general approach to mimicking homotrimers of the TNF superfamily.},
keywords = {Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Dumortier, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Team-Dumortier, Time Factors, tumor},
pubstate = {published},
tppubtype = {article}
}
Berthier-Vergnes Odile, Bermond Fabienne, Flacher Vincent, Massacrier Catherine, Schmitt Daniel, Péguet-Navarro Josette
TNF-alpha enhances phenotypic and functional maturation of human epidermal Langerhans cells and induces IL-12 p40 and IP-10/CXCL-10 production Journal Article
In: FEBS letters, vol. 579, no. 17, pp. 3660–3668, 2005, ISSN: 0014-5793.
Abstract | Links | BibTeX | Tags: Antigens, Apoptosis, C-Type, CD, Cell Differentiation, Cells, Chemokine CXCL10, chemokines, Cultured, CXC, Epidermal Cells, HLA-DR Antigens, Humans, Hypersensitivity, Interleukin-12, Interleukin-12 Subunit p40, Langerhans Cells, Lectins, Mannose-Binding Lectins, Phenotype, Protein Subunits, Surface, T-Lymphocytes, Team-Mueller, Tumor Necrosis Factor-alpha
@article{berthier-vergnes_tnf-alpha_2005,
title = {TNF-alpha enhances phenotypic and functional maturation of human epidermal Langerhans cells and induces IL-12 p40 and IP-10/CXCL-10 production},
author = {Odile Berthier-Vergnes and Fabienne Bermond and Vincent Flacher and Catherine Massacrier and Daniel Schmitt and Josette Péguet-Navarro},
doi = {10.1016/j.febslet.2005.04.087},
issn = {0014-5793},
year = {2005},
date = {2005-07-01},
journal = {FEBS letters},
volume = {579},
number = {17},
pages = {3660--3668},
abstract = {Dendritic cells (DC) play a central role in immunity/tolerance decision, depending on their activation/maturation state. TNF-alpha is largely produced in the skin under inflammatory conditions. However, it still remains to be defined how TNF-alpha modulates the activation status of human LC, the most specialized DC controlling skin immunity. Here, we reported that fresh immature LC, highly purified from healthy human skin and exposed for two days to TNF-alpha under serum-free conditions, expressed up-regulated level of co-stimulatory molecules (CD40, CD54, CD86), maturation markers (CD83, DC-LAMP), CCR7 lymph node homing receptor, and down-regulated Langerin level, in a dose-dependent manner. This mature phenotype is closely associated with enhanced LC allostimulatory capacity. Furthermore, TNF-alpha significantly increased the number of viable LC and decreased their spontaneous apoptosis. More importantly, TNF-alpha induced LC to produce both IFN-gamma-inducible-protein IP-10/CXCL10, a Th1-attracting chemokine and IL-12 p40. Bioactive IL-12 p70 was never detected, even after additional CD40 stimulus. The results implicate LC as an effective target through which TNF-alpha may up- or down-regulate the inflammatory skin reactions.},
keywords = {Antigens, Apoptosis, C-Type, CD, Cell Differentiation, Cells, Chemokine CXCL10, chemokines, Cultured, CXC, Epidermal Cells, HLA-DR Antigens, Humans, Hypersensitivity, Interleukin-12, Interleukin-12 Subunit p40, Langerhans Cells, Lectins, Mannose-Binding Lectins, Phenotype, Protein Subunits, Surface, T-Lymphocytes, Team-Mueller, Tumor Necrosis Factor-alpha},
pubstate = {published},
tppubtype = {article}
}
Fournel Sylvie, Wieckowski Sébastien, Sun Weimin, Trouche Nathalie, Dumortier Hélène, Bianco Alberto, Chaloin Olivier, Habib Mohammed, Peter Jean-Christophe, Schneider Pascal, Vray Bernard, Toes René E, Offringa Rienk, Melief Cornelis J M, Hoebeke Johan, Guichard Gilles
C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L Journal Article
In: Nature Chemical Biology, vol. 1, no. 7, pp. 377–382, 2005, ISSN: 1552-4450.
Abstract | Links | BibTeX | Tags: Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Time Factors, tumor
@article{fournel_c3-symmetric_2005b,
title = {C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L},
author = {Sylvie Fournel and Sébastien Wieckowski and Weimin Sun and Nathalie Trouche and Hélène Dumortier and Alberto Bianco and Olivier Chaloin and Mohammed Habib and Jean-Christophe Peter and Pascal Schneider and Bernard Vray and René E Toes and Rienk Offringa and Cornelis J M Melief and Johan Hoebeke and Gilles Guichard},
doi = {10.1038/nchembio746},
issn = {1552-4450},
year = {2005},
date = {2005-01-01},
journal = {Nature Chemical Biology},
volume = {1},
number = {7},
pages = {377--382},
abstract = {Interaction between CD40, a member of the tumor necrosis factor receptor (TNFR) superfamily, and its ligand CD40L, a 39-kDa glycoprotein, is essential for the development of humoral and cellular immune responses. Selective blockade or activation of this pathway provides the ground for the development of new treatments against immunologically based diseases and malignancies. Like other members of the TNF superfamily, CD40L monomers self-assemble around a threefold symmetry axis to form noncovalent homotrimers that can each bind three receptor molecules. Here, we report on the structure-based design of small synthetic molecules with C3 symmetry that can mimic CD40L homotrimers. These molecules interact with CD40, compete with the binding of CD40L to CD40, and reproduce, to a certain extent, the functional properties of the much larger homotrimeric soluble CD40L. Architectures based on rigid C3-symmetric cores may thus represent a general approach to mimicking homotrimers of the TNF superfamily.},
keywords = {Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Time Factors, tumor},
pubstate = {published},
tppubtype = {article}
}
Royet Julien, Reichhart Jean-Marc
Detection of peptidoglycans by NOD proteins Journal Article
In: Trends Cell Biol., vol. 13, no. 12, pp. 610–614, 2003, ISSN: 0962-8924.
Abstract | BibTeX | Tags: Adaptor Proteins, Apoptosis, Carrier Proteins, Gram-Positive Bacteria, Humans, Immunity, Immunologic, Innate, M3i, Nod1 Signaling Adaptor Protein, Oligopeptides, peptidoglycan, Receptors, reichhart, Signal Transducing, Signal Transduction
@article{royet_detection_2003,
title = {Detection of peptidoglycans by NOD proteins},
author = {Julien Royet and Jean-Marc Reichhart},
issn = {0962-8924},
year = {2003},
date = {2003-12-01},
journal = {Trends Cell Biol.},
volume = {13},
number = {12},
pages = {610--614},
abstract = {Mechanisms of innate immune defense are based on the recognition of invariant microbial molecular patterns by specific receptors, followed by the activation of signaling pathways and the expression of effector molecules that will defeat the invading microorganism. Two recent reports add to the growing list of these pattern-recognition receptors by showing that the intracellular nucleotide-binding oligomerization domain 1 (NOD1) protein recognizes a diaminopimelate-containing muropeptide, a cell-wall component of Gram-negative bacteria.},
keywords = {Adaptor Proteins, Apoptosis, Carrier Proteins, Gram-Positive Bacteria, Humans, Immunity, Immunologic, Innate, M3i, Nod1 Signaling Adaptor Protein, Oligopeptides, peptidoglycan, Receptors, reichhart, Signal Transducing, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Christophides George K, Zdobnov Evgeny, Barillas-Mury Carolina, Birney Ewan, Blandin Stephanie A, Blass Claudia, Brey Paul T, Collins Frank H, Danielli Alberto, Dimopoulos George, Hetru Charles, Hoa Ngo T, Hoffmann Jules A, Kanzok Stefan M, Letunic Ivica, Levashina Elena A, Loukeris Thanasis G, Lycett Gareth, Meister Stephan, Michel Kristin, Moita Luis F, Müller Hans-Michael, Osta Mike A, Paskewitz Susan M, Reichhart Jean-Marc, Rzhetsky Andrey, Troxler Laurent, Vernick Kenneth D, Vlachou Dina, Volz Jennifer, von Mering Christian, Xu Jiannong, Zheng Liangbiao, Bork Peer, Kafatos Fotis C
Immunity-related genes and gene families in Anopheles gambiae Journal Article
In: Science, vol. 298, no. 5591, pp. 159–165, 2002, ISSN: 1095-9203.
Abstract | Links | BibTeX | Tags: Alternative Splicing, Animals, Anopheles, Apoptosis, bacteria, bioinformatic, blandin, Catechol Oxidase, Computational Biology, Enzyme Precursors, Gene Expression Regulation, Genes, Genetic, Genome, hoffmann, Immunity, Innate, Insect, Insect Proteins, M3i, Multigene Family, Peptides, Phylogeny, Plasmodium, Protein Structure, reichhart, Selection, Serine Endopeptidases, Serpins, Signal Transduction, Tertiary
@article{christophides_immunity-related_2002,
title = {Immunity-related genes and gene families in Anopheles gambiae},
author = {George K Christophides and Evgeny Zdobnov and Carolina Barillas-Mury and Ewan Birney and Stephanie A Blandin and Claudia Blass and Paul T Brey and Frank H Collins and Alberto Danielli and George Dimopoulos and Charles Hetru and Ngo T Hoa and Jules A Hoffmann and Stefan M Kanzok and Ivica Letunic and Elena A Levashina and Thanasis G Loukeris and Gareth Lycett and Stephan Meister and Kristin Michel and Luis F Moita and Hans-Michael Müller and Mike A Osta and Susan M Paskewitz and Jean-Marc Reichhart and Andrey Rzhetsky and Laurent Troxler and Kenneth D Vernick and Dina Vlachou and Jennifer Volz and Christian von Mering and Jiannong Xu and Liangbiao Zheng and Peer Bork and Fotis C Kafatos},
url = {http://www.ncbi.nlm.nih.gov/pubmed/12364793},
doi = {10.1126/science.1077136},
issn = {1095-9203},
year = {2002},
date = {2002-10-01},
journal = {Science},
volume = {298},
number = {5591},
pages = {159--165},
abstract = {We have identified 242 Anopheles gambiae genes from 18 gene families implicated in innate immunity and have detected marked diversification relative to Drosophila melanogaster. Immune-related gene families involved in recognition, signal modulation, and effector systems show a marked deficit of orthologs and excessive gene expansions, possibly reflecting selection pressures from different pathogens encountered in these insects' very different life-styles. In contrast, the multifunctional Toll signal transduction pathway is substantially conserved, presumably because of counterselection for developmental stability. Representative expression profiles confirm that sequence diversification is accompanied by specific responses to different immune challenges. Alternative RNA splicing may also contribute to expansion of the immune repertoire.},
keywords = {Alternative Splicing, Animals, Anopheles, Apoptosis, bacteria, bioinformatic, blandin, Catechol Oxidase, Computational Biology, Enzyme Precursors, Gene Expression Regulation, Genes, Genetic, Genome, hoffmann, Immunity, Innate, Insect, Insect Proteins, M3i, Multigene Family, Peptides, Phylogeny, Plasmodium, Protein Structure, reichhart, Selection, Serine Endopeptidases, Serpins, Signal Transduction, Tertiary},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Naitza S, Kappler Christine, Ferrandon Dominique, Zachary Daniel, Swimmer C, Kopczynski C, Duyk G, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis Journal Article
In: Dev. Cell, vol. 1, no. 4, pp. 503–514, 2001, ISSN: 1534-5807.
Abstract | BibTeX | Tags: Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary
@article{georgel_drosophila_2001,
title = {Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis},
author = {Philippe Georgel and S Naitza and Christine Kappler and Dominique Ferrandon and Daniel Zachary and C Swimmer and C Kopczynski and G Duyk and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {1534-5807},
year = {2001},
date = {2001-10-01},
journal = {Dev. Cell},
volume = {1},
number = {4},
pages = {503--514},
abstract = {We report the molecular characterization of the immune deficiency (imd) gene, which controls antibacterial defense in Drosophila. imd encodes a protein with a death domain similar to that of mammalian RIP (receptor interacting protein), a protein that plays a role in both NF-kappaB activation and apoptosis. We show that imd functions upstream of the DmIKK signalosome and the caspase DREDD in the control of antibacterial peptide genes. Strikingly, overexpression of imd leads to constitutive transcription of these genes and to apoptosis, and both effects are blocked by coexpression of the caspase inhibitor P35. We also show that imd is involved in the apoptotic response to UV irradiation. These data raise the possibility that antibacterial response and apoptosis share common control elements in Drosophila.},
keywords = {Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary},
pubstate = {published},
tppubtype = {article}
}