Onder Lucas, Mörbe Urs, Pikor Natalia, Novkovic Mario, Cheng Hung-Wei, Hehlgans Thomas, Pfeffer Klaus, Becher Burkhard, Waisman Ari, Rülicke Thomas, Gommerman Jennifer, Mueller Christopher G, Sawa Shinichiro, Scandella Elke, Ludewig Burkhard
Lymphatic Endothelial Cells Control Initiation of Lymph Node Organogenesis Article de journal
Dans: Immunity, vol. 47, no. 1, p. 80–92.e4, 2017, ISSN: 1097-4180.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cell Differentiation, Cells, Choristoma, Cultured, Embryo, Endothelial Cells, fibroblastic reticular cells, Inbred C57BL, lymph node organogenesis, Lymph Nodes, lymphatic and blood endothelial cells, lymphoid stromal cells, lymphoid tissue organizer cells, Lymphotoxin beta Receptor, Lysosphingolipid, Mammalian, Mesenchymal Stem Cells, mesenchymal stromal cells, Mice, NF-kappa B, Organogenesis, Receptor Activator of Nuclear Factor-kappa B, Receptors, Signal Transduction, Team-Mueller, transgenic
@article{onder_lymphatic_2017,
title = {Lymphatic Endothelial Cells Control Initiation of Lymph Node Organogenesis},
author = {Lucas Onder and Urs Mörbe and Natalia Pikor and Mario Novkovic and Hung-Wei Cheng and Thomas Hehlgans and Klaus Pfeffer and Burkhard Becher and Ari Waisman and Thomas Rülicke and Jennifer Gommerman and Christopher G Mueller and Shinichiro Sawa and Elke Scandella and Burkhard Ludewig},
doi = {10.1016/j.immuni.2017.05.008},
issn = {1097-4180},
year = {2017},
date = {2017-07-01},
journal = {Immunity},
volume = {47},
number = {1},
pages = {80--92.e4},
abstract = {Lymph nodes (LNs) are strategically situated throughout the body at junctures of the blood vascular and lymphatic systems to direct immune responses against antigens draining from peripheral tissues. The current paradigm describes LN development as a programmed process that is governed through the interaction between mesenchymal lymphoid tissue organizer (LTo) cells and hematopoietic lymphoid tissue inducer (LTi) cells. Using cell-type-specific ablation of key molecules involved in lymphoid organogenesis, we found that initiation of LN development is dependent on LTi-cell-mediated activation of lymphatic endothelial cells (LECs) and that engagement of mesenchymal stromal cells is a succeeding event. LEC activation was mediated mainly by signaling through receptor activator of NF-κB (RANK) and the non-canonical NF-κB pathway and was steered by sphingosine-1-phosphate-receptor-dependent retention of LTi cells in the LN anlage. Finally, the finding that pharmacologically enforced interaction between LTi cells and LECs promotes ectopic LN formation underscores the central LTo function of LECs.},
keywords = {Animals, Cell Differentiation, Cells, Choristoma, Cultured, Embryo, Endothelial Cells, fibroblastic reticular cells, Inbred C57BL, lymph node organogenesis, Lymph Nodes, lymphatic and blood endothelial cells, lymphoid stromal cells, lymphoid tissue organizer cells, Lymphotoxin beta Receptor, Lysosphingolipid, Mammalian, Mesenchymal Stem Cells, mesenchymal stromal cells, Mice, NF-kappa B, Organogenesis, Receptor Activator of Nuclear Factor-kappa B, Receptors, Signal Transduction, Team-Mueller, transgenic},
pubstate = {published},
tppubtype = {article}
}
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 Article de journal
Dans: Immunol.Lett., vol. 171, no. 1879-0542 (Electronic), p. 5–14, 2016.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
Bonnay François, Nguyen Xuan-Hung, Cohen-Berros Eva, Troxler Laurent, Batsche Eric, Camonis Jacques, Takeuchi Osamu, Reichhart Jean-Marc, Matt Nicolas
Akirin specifies NF-κB selectivity of Drosophila innate immune response via chromatin remodeling Article de journal
Dans: EMBO J., vol. 33, no. 20, p. 2349–2362, 2014, ISSN: 1460-2075.
Résumé | Liens | BibTeX | Étiquettes: Animals, bioinformatic, Cell Cycle Proteins, Chromatin Assembly and Disassembly, chromatin remodeling, DNA-Binding Proteins, Female, Genetic, Immunity, Innate, Innate immune response, M3i, Male, matt, Mutation, NF-kappa B, NF‐κB, Promoter Regions, proteomics, reichhart, Trans-Activators, Transcription Factors, Transcriptional Activation, Two-Hybrid System Techniques
@article{bonnay_akirin_2014,
title = {Akirin specifies NF-κB selectivity of Drosophila innate immune response via chromatin remodeling},
author = {François Bonnay and Xuan-Hung Nguyen and Eva Cohen-Berros and Laurent Troxler and Eric Batsche and Jacques Camonis and Osamu Takeuchi and Jean-Marc Reichhart and Nicolas Matt},
doi = {10.15252/embj.201488456},
issn = {1460-2075},
year = {2014},
date = {2014-10-01},
journal = {EMBO J.},
volume = {33},
number = {20},
pages = {2349--2362},
abstract = {The network of NF-κB-dependent transcription that activates both pro- and anti-inflammatory genes in mammals is still unclear. As NF-κB factors are evolutionarily conserved, we used Drosophila to understand this network. The NF-κB transcription factor Relish activates effector gene expression following Gram-negative bacterial immune challenge. Here, we show, using a genome-wide approach, that the conserved nuclear protein Akirin is a NF-κB co-factor required for the activation of a subset of Relish-dependent genes correlating with the presence of H3K4ac epigenetic marks. A large-scale unbiased proteomic analysis revealed that Akirin orchestrates NF-κB transcriptional selectivity through the recruitment of the Osa-containing-SWI/SNF-like Brahma complex (BAP). Immune challenge in Drosophila shows that Akirin is required for the transcription of a subset of effector genes, but dispensable for the transcription of genes that are negative regulators of the innate immune response. Therefore, Akirins act as molecular selectors specifying the choice between subsets of NF-κB target genes. The discovery of this mechanism, conserved in mammals, paves the way for the establishment of more specific and less toxic anti-inflammatory drugs targeting pro-inflammatory genes.},
keywords = {Animals, bioinformatic, Cell Cycle Proteins, Chromatin Assembly and Disassembly, chromatin remodeling, DNA-Binding Proteins, Female, Genetic, Immunity, Innate, Innate immune response, M3i, Male, matt, Mutation, NF-kappa B, NF‐κB, Promoter Regions, proteomics, reichhart, Trans-Activators, Transcription Factors, Transcriptional Activation, Two-Hybrid System Techniques},
pubstate = {published},
tppubtype = {article}
}
Goto Akira, Fukuyama Hidehiro, Imler Jean-Luc, Hoffmann Jules A
The chromatin regulator DMAP1 modulates activity of the nuclear factor B (NF-B) transcription factor Relish in the Drosophila innate immune response Article de journal
Dans: The Journal of Biological Chemistry, vol. 289, no. 30, p. 20470–20476, 2014, ISSN: 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cell Line, Chromatin Assembly and Disassembly, Epistasis, Escherichia coli, Escherichia coli Infections, Genetic, hoffmann, imler, Immunity, Innate, M3i, NF-kappa B, Repressor Proteins, Signal Transduction, Transcription Factors
@article{goto_chromatin_2014,
title = {The chromatin regulator DMAP1 modulates activity of the nuclear factor B (NF-B) transcription factor Relish in the Drosophila innate immune response},
author = {Akira Goto and Hidehiro Fukuyama and Jean-Luc Imler and Jules A Hoffmann},
doi = {10.1074/jbc.C114.553719},
issn = {1083-351X},
year = {2014},
date = {2014-07-01},
journal = {The Journal of Biological Chemistry},
volume = {289},
number = {30},
pages = {20470--20476},
abstract = {The host defense of the model organism Drosophila is under the control of two major signaling cascades controlling transcription factors of the NF-B family, the Toll and the immune deficiency (IMD) pathways. The latter shares extensive similarities with the mammalian TNF-R pathway and was initially discovered for its role in anti-Gram-negative bacterial reactions. A previous interactome study from this laboratory reported that an unexpectedly large number of proteins are binding to the canonical components of the IMD pathway. Here, we focus on DNA methyltransferase-associated protein 1 (DMAP1), which this study identified as an interactant of Relish, a Drosophila transcription factor reminiscent of the mammalian p105 NF-B protein. We show that silencing of DMAP1 expression both in S2 cells and in flies results in a significant reduction of Escherichia coli-induced expression of antimicrobial peptides. Epistatic analysis indicates that DMAP1 acts in parallel or downstream of Relish. Co-immunoprecipitation experiments further reveal that, in addition to Relish, DMAP1 also interacts with Akirin and the Brahma-associated protein 55 kDa (BAP55). Taken together, these results reveal that DMAP1 is a novel nuclear modulator of the IMD pathway, possibly acting at the level of chromatin remodeling.},
keywords = {Animals, Cell Line, Chromatin Assembly and Disassembly, Epistasis, Escherichia coli, Escherichia coli Infections, Genetic, hoffmann, imler, Immunity, Innate, M3i, NF-kappa B, Repressor Proteins, Signal Transduction, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Duheron V, Hess E, Duval M, Decossas M, Castaneda B, Klopper J E, Amoasii L, Barbaroux J B, Williams I R, Yagita H, Penninger J, Choi Y, Lezot F, Groves R, Paus R, Mueller C G
Receptor activator of NF-kappaB (RANK) stimulates the proliferation of epithelial cells of the epidermo-pilosebaceous unit Article de journal
Dans: Proc.Natl.Acad.Sci.U.S.A, vol. 108, no. 1091-6490 (Electronic), p. 5342–5347, 2011.
Résumé | Liens | BibTeX | Étiquettes: Activation, Animals, Cell Proliferation, Chemistry, cytology, Epidermis, Epithelial Cells, function, Genetics, Growth, Hair, hair follicle, Homeostasis, Immunology, Inbred C57BL, ligand, metabolism, Mice, NF-kappa B, NF-kappaB, Nude, Osteoprotegerin, physiology, Proliferation, rank, RANK ligand, Receptor, Receptor Activator of Nuclear Factor-kappa B, signaling, Skin, Skin Transplantation, stem, Stem Cells, Team-Mueller, transgenic, TRANSGENIC MICE, TRANSPLANTATION
@article{duheron_receptor_2011,
title = {Receptor activator of NF-kappaB (RANK) stimulates the proliferation of epithelial cells of the epidermo-pilosebaceous unit},
author = {V Duheron and E Hess and M Duval and M Decossas and B Castaneda and J E Klopper and L Amoasii and J B Barbaroux and I R Williams and H Yagita and J Penninger and Y Choi and F Lezot and R Groves and R Paus and C G Mueller},
doi = {10.1073/pnas.1013054108},
year = {2011},
date = {2011-03-01},
journal = {Proc.Natl.Acad.Sci.U.S.A},
volume = {108},
number = {1091-6490 (Electronic)},
pages = {5342--5347},
abstract = {Receptor activator of NF-kappaB (RANK), known for controlling bone mass, has been recognized for its role in epithelial cell activation of the mammary gland. Because bone and the epidermo-pilosebaceous unit of the skin share a lifelong renewal activity where similar molecular players operate, and because mammary glands and hair follicles are both skin appendages, we have addressed the function of RANK in the hair follicle and the epidermis. Here, we show that mice deficient in RANK ligand (RANKL) are unable to initiate a new growth phase of the hair cycle and display arrested epidermal homeostasis. However, transgenic mice overexpressing RANK in the hair follicle or administration of recombinant RANKL both activate the hair cycle and epidermal growth. RANK is expressed by the hair follicle germ and bulge stem cells and the epidermal basal cells, cell types implicated in the renewal of the epidermo-pilosebaceous unit. RANK signaling is dispensable for the formation of the stem cell compartment and the inductive hair follicle mesenchyme, and the hair cycle can be rescued by Rankl knockout skin transplantation onto nude mice. RANKL is actively transcribed by the hair follicle at initiation of its growth phase, providing a mechanism for stem cell RANK engagement and hair-cycle entry. Thus, RANK-RANKL regulates hair renewal and epidermal homeostasis and provides a link between these two activities},
keywords = {Activation, Animals, Cell Proliferation, Chemistry, cytology, Epidermis, Epithelial Cells, function, Genetics, Growth, Hair, hair follicle, Homeostasis, Immunology, Inbred C57BL, ligand, metabolism, Mice, NF-kappa B, NF-kappaB, Nude, Osteoprotegerin, physiology, Proliferation, rank, RANK ligand, Receptor, Receptor Activator of Nuclear Factor-kappa B, signaling, Skin, Skin Transplantation, stem, Stem Cells, Team-Mueller, transgenic, TRANSGENIC MICE, TRANSPLANTATION},
pubstate = {published},
tppubtype = {article}
}
Lee Kwang-Zin, Ferrandon Dominique
Negative regulation of immune responses on the fly Article de journal
Dans: EMBO J., vol. 30, no. 6, p. 988–990, 2011, ISSN: 1460-2075.
Liens | BibTeX | Étiquettes: *Gene Expression Regulation, *Homeostasis, Animals, bacteria, Bacteria/*immunology, Biological, Drosophila melanogaster/*immunology, Drosophila Proteins/biosynthesis/metabolism, ferrandon, Gene Expression Regulation, Homeostasis, M3i, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinases/metabolism, Models, NF-kappa B, NF-kappa B/metabolism, ras Proteins, ras Proteins/metabolism, Receptor Protein-Tyrosine Kinases, Receptor Protein-Tyrosine Kinases/metabolism
@article{lee_negative_2011b,
title = {Negative regulation of immune responses on the fly},
author = {Kwang-Zin Lee and Dominique Ferrandon},
doi = {10.1038/emboj.2011.47},
issn = {1460-2075},
year = {2011},
date = {2011-01-01},
journal = {EMBO J.},
volume = {30},
number = {6},
pages = {988--990},
keywords = {*Gene Expression Regulation, *Homeostasis, Animals, bacteria, Bacteria/*immunology, Biological, Drosophila melanogaster/*immunology, Drosophila Proteins/biosynthesis/metabolism, ferrandon, Gene Expression Regulation, Homeostasis, M3i, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinases/metabolism, Models, NF-kappa B, NF-kappa B/metabolism, ras Proteins, ras Proteins/metabolism, Receptor Protein-Tyrosine Kinases, Receptor Protein-Tyrosine Kinases/metabolism},
pubstate = {published},
tppubtype = {article}
}
Paquette Nicholas, Broemer Meike, Aggarwal Kamna, Chen Li, Husson Marie, Ertürk-Hasdemir Deniz, Reichhart Jean-Marc, Meier Pascal, Silverman Neal
Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling Article de journal
Dans: Mol. Cell, vol. 37, no. 2, p. 172–182, 2010, ISSN: 1097-4164.
Résumé | Liens | BibTeX | Étiquettes: Alleles, Amino Acid Motifs, Animals, Biological, Caspases, Inhibitor of Apoptosis Proteins, M3i, MAP Kinase Kinase Kinases, Models, NF-kappa B, reichhart, Sequence Alignment, Signal Transduction, Ubiquitin-Protein Ligases, Ubiquitination
@article{paquette_caspase-mediated_2010,
title = {Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling},
author = {Nicholas Paquette and Meike Broemer and Kamna Aggarwal and Li Chen and Marie Husson and Deniz Ertürk-Hasdemir and Jean-Marc Reichhart and Pascal Meier and Neal Silverman},
doi = {10.1016/j.molcel.2009.12.036},
issn = {1097-4164},
year = {2010},
date = {2010-01-01},
journal = {Mol. Cell},
volume = {37},
number = {2},
pages = {172--182},
abstract = {Innate immune responses are critical for the immediate protection against microbial infection. In Drosophila, infection leads to the rapid and robust production of antimicrobial peptides through two NF-kappaB signaling pathways-IMD and Toll. The IMD pathway is triggered by DAP-type peptidoglycan, common to most Gram-negative bacteria. Signaling downstream from the peptidoglycan receptors is thought to involve K63 ubiquitination and caspase-mediated cleavage, but the molecular mechanisms remain obscure. We now show that PGN stimulation causes caspase-mediated cleavage of the imd protein, exposing a highly conserved IAP-binding motif (IBM) at its neo-N terminus. A functional IBM is required for the association of cleaved IMD with the ubiquitin E3-ligase DIAP2. Through its association with DIAP2, IMD is rapidly conjugated with K63-linked polyubiquitin chains. These results mechanistically connect caspase-mediated cleavage and K63 ubiquitination in immune-induced NF-kappaB signaling.},
keywords = {Alleles, Amino Acid Motifs, Animals, Biological, Caspases, Inhibitor of Apoptosis Proteins, M3i, MAP Kinase Kinase Kinases, Models, NF-kappa B, reichhart, Sequence Alignment, Signal Transduction, Ubiquitin-Protein Ligases, Ubiquitination},
pubstate = {published},
tppubtype = {article}
}
Hetru Charles, Hoffmann Jules A
NF-kappaB in the immune response of Drosophila Article de journal
Dans: Cold Spring Harb Perspect Biol, vol. 1, no. 6, p. a000232, 2009, ISSN: 1943-0264.
Résumé | Liens | BibTeX | Étiquettes: Animals, bacteria, Fungi, Gene Expression Regulation, hoffmann, M3i, NF-kappa B
@article{hetru_nf-kappab_2009,
title = {NF-kappaB in the immune response of Drosophila},
author = {Charles Hetru and Jules A Hoffmann},
doi = {10.1101/cshperspect.a000232},
issn = {1943-0264},
year = {2009},
date = {2009-12-01},
journal = {Cold Spring Harb Perspect Biol},
volume = {1},
number = {6},
pages = {a000232},
abstract = {The nuclear factor kappaB (NF-kappaB) pathways play a major role in Drosophila host defense. Two recognition and signaling cascades control this immune response. The Toll pathway is activated by Gram-positive bacteria and by fungi, whereas the immune deficiency (Imd) pathway responds to Gram-negative bacterial infection. The basic mechanisms of recognition of these various types of microbial infections by the adult fly are now globally understood. Even though some elements are missing in the intracellular pathways, numerous proteins and interactions have been identified. In this article, we present a general picture of the immune functions of NF-kappaB in Drosophila with all the partners involved in recognition and in the signaling cascades.},
keywords = {Animals, bacteria, Fungi, Gene Expression Regulation, hoffmann, M3i, NF-kappa B},
pubstate = {published},
tppubtype = {article}
}
Goto Akira, Matsushita Kazufumi, Gesellchen Viola, Chamy Laure El, Kuttenkeuler David, Takeuchi Osamu, Hoffmann Jules A, Akira Shizuo, Boutros Michael, Reichhart Jean-Marc
Akirins are highly conserved nuclear proteins required for NF-kappaB-dependent gene expression in drosophila and mice Article de journal
Dans: Nat. Immunol., vol. 9, no. 1, p. 97–104, 2008, ISSN: 1529-2916.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cell Line, Embryo, Fibroblasts, hoffmann, Humans, Immunity, Innate, Interleukin-1beta, M3i, Mammalian, Mice, NF-kappa B, Nuclear Proteins, Proteins, reichhart, Signal Transduction, Toll-Like Receptors, transgenic, Tumor Necrosis Factor-alpha
@article{goto_akirins_2008,
title = {Akirins are highly conserved nuclear proteins required for NF-kappaB-dependent gene expression in drosophila and mice},
author = {Akira Goto and Kazufumi Matsushita and Viola Gesellchen and Laure El Chamy and David Kuttenkeuler and Osamu Takeuchi and Jules A Hoffmann and Shizuo Akira and Michael Boutros and Jean-Marc Reichhart},
doi = {10.1038/ni1543},
issn = {1529-2916},
year = {2008},
date = {2008-01-01},
journal = {Nat. Immunol.},
volume = {9},
number = {1},
pages = {97--104},
abstract = {During a genome-wide screen with RNA-mediated interference, we isolated CG8580 as a gene involved in the innate immune response of Drosophila melanogaster. CG8580, which we called Akirin, encoded a protein that acted in parallel with the NF-kappaB transcription factor downstream of the Imd pathway and was required for defense against Gram-negative bacteria. Akirin is highly conserved, and the human genome contains two homologs, one of which was able to rescue the loss-of-function phenotype in drosophila cells. Akirins were strictly localized to the nucleus. Knockout of both Akirin homologs in mice showed that one had an essential function downstream of the Toll-like receptor, tumor necrosis factor and interleukin (IL)-1beta signaling pathways leading to the production of IL-6. Thus, Akirin is a conserved nuclear factor required for innate immune responses.},
keywords = {Animals, Cell Line, Embryo, Fibroblasts, hoffmann, Humans, Immunity, Innate, Interleukin-1beta, M3i, Mammalian, Mice, NF-kappa B, Nuclear Proteins, Proteins, reichhart, Signal Transduction, Toll-Like Receptors, transgenic, Tumor Necrosis Factor-alpha},
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 Article de journal
Dans: Journal of Immunology, vol. 181, no. 1550-6606 (Electronic), p. 1103–1108, 2008.
Résumé | BibTeX | Étiquettes: 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}
}
Frolet Cécile, Thoma Martine, Blandin Stéphanie A, Hoffmann Jules A, Levashina Elena A
Boosting NF-kappaB-dependent basal immunity of Anopheles gambiae aborts development of Plasmodium berghei Article de journal
Dans: Immunity, vol. 25, no. 4, p. 677–685, 2006, ISSN: 1074-7613.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anopheles gambiae, blandin, Gene Expression, Gene Expression Regulation, Genes, hoffmann, Immunity, Insect, M3i, NF-kappa B, Plasmodium berghei, telomerase
@article{frolet_boosting_2006,
title = {Boosting NF-kappaB-dependent basal immunity of Anopheles gambiae aborts development of Plasmodium berghei},
author = {Cécile Frolet and Martine Thoma and Stéphanie A Blandin and Jules A Hoffmann and Elena A Levashina},
url = {http://www.ncbi.nlm.nih.gov/pubmed/17045818},
doi = {10.1016/j.immuni.2006.08.019},
issn = {1074-7613},
year = {2006},
date = {2006-10-01},
journal = {Immunity},
volume = {25},
number = {4},
pages = {677--685},
abstract = {Anopheles gambiae, the major vector for the protozoan malaria parasite Plasmodium falciparum, mounts powerful antiparasitic responses that cause marked parasite loss during midgut invasion. Here, we showed that these antiparasitic defenses were composed of pre- and postinvasion phases and that the preinvasion phase was predominantly regulated by Rel1 and Rel2 members of the NF-kappaB transcription factors. Concurrent silencing of Rel1 and Rel2 decreased the basal expression of the major antiparasitic genes TEP1 and LRIM1 and abolished resistance of Anopheles to the rodent malaria parasite P. berghei. Conversely, depletion of a negative regulator of Rel1, Cactus, prior to infection, enhanced the basal expression of TEP1 and of other immune factors and completely prevented parasite development. Our findings uncover the crucial role of the preinvasion defense in the elimination of parasites, which is at least in part based on circulating blood molecules.},
keywords = {Animals, Anopheles gambiae, blandin, Gene Expression, Gene Expression Regulation, Genes, hoffmann, Immunity, Insect, M3i, NF-kappa B, Plasmodium berghei, telomerase},
pubstate = {published},
tppubtype = {article}
}
Imler Jean-Luc, Hoffmann Jules A
Toll and Toll-like proteins: an ancient family of receptors signaling infection Article de journal
Dans: Reviews in Immunogenetics, vol. 2, no. 3, p. 294–304, 2000, ISSN: 1398-1714.
Résumé | BibTeX | Étiquettes: Adaptor Proteins, Animals, Antigens, Autoantigens, CD14, Cell Adhesion Molecules, Cell Surface, Differentiation, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, I-kappa B Proteins, imler, Immunity, Immunologic, infection, Innate, Insect Proteins, Interleukin-1 Receptor-Associated Kinases, Knockout, Larva, Lipopolysaccharides, M3i, Mammals, MAP Kinase Signaling System, Membrane Glycoproteins, Membrane Proteins, Mice, Multigene Family, Myeloid Differentiation Factor 88, NF-kappa B, peptidoglycan, Phosphorylation, Post-Translational, Protein Kinases, Protein Processing, Protein Structure, Receptors, Recombinant Fusion Proteins, Signal Transducing, Signal Transduction, Teichoic Acids, Tertiary, Toll-Like Receptor 4, Toll-Like Receptor 5, Toll-Like Receptor 6, Toll-Like Receptor 9, Toll-Like Receptors, Ubiquitins
@article{imler_toll_2000,
title = {Toll and Toll-like proteins: an ancient family of receptors signaling infection},
author = {Jean-Luc Imler and Jules A Hoffmann},
issn = {1398-1714},
year = {2000},
date = {2000-01-01},
journal = {Reviews in Immunogenetics},
volume = {2},
number = {3},
pages = {294--304},
abstract = {Innate immunity is the first-line host defense of multicellular organisms that rapidly operates to limit infection upon exposure to microbes. It involves intracellular signaling pathways in the fruit-fly Drosophila and in mammals that show striking similarities. Recent genetic and biochemical data have revealed, in particular, that proteins of the Toll family play a critical role in the immediate response to infection. We review here the recent developments on the structural and functional characterization of this evolutionary ancient and important family of proteins, which can function as cytokine receptors (Toll in Drosophila) or pattern recognition receptors (TLR4 in mammals) and activate similar, albeit non identical signal transduction pathways, in flies and mammals.},
keywords = {Adaptor Proteins, Animals, Antigens, Autoantigens, CD14, Cell Adhesion Molecules, Cell Surface, Differentiation, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, I-kappa B Proteins, imler, Immunity, Immunologic, infection, Innate, Insect Proteins, Interleukin-1 Receptor-Associated Kinases, Knockout, Larva, Lipopolysaccharides, M3i, Mammals, MAP Kinase Signaling System, Membrane Glycoproteins, Membrane Proteins, Mice, Multigene Family, Myeloid Differentiation Factor 88, NF-kappa B, peptidoglycan, Phosphorylation, Post-Translational, Protein Kinases, Protein Processing, Protein Structure, Receptors, Recombinant Fusion Proteins, Signal Transducing, Signal Transduction, Teichoic Acids, Tertiary, Toll-Like Receptor 4, Toll-Like Receptor 5, Toll-Like Receptor 6, Toll-Like Receptor 9, Toll-Like Receptors, Ubiquitins},
pubstate = {published},
tppubtype = {article}
}
Barillas-Mury Carolina, Charlesworth A, Gross I, Richman A, Hoffmann Jules A, Kafatos Fotis C
Immune factor Gambif1, a new rel family member from the human malaria vector, Anopheles gambiae Article de journal
Dans: EMBO J., vol. 15, no. 17, p. 4691–4701, 1996, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Anopheles, Base Sequence, Biological Transport, Cell Nucleus, Cells, Complementary, Cultured, DNA, DNA-Binding Proteins, hoffmann, Insect Proteins, Insect Vectors, M3i, NF-kappa B, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-rel, Sequence Homology, Trans-Activators, Transcriptional Activation
@article{barillas-mury_immune_1996,
title = {Immune factor Gambif1, a new rel family member from the human malaria vector, Anopheles gambiae},
author = {Carolina Barillas-Mury and A Charlesworth and I Gross and A Richman and Jules A Hoffmann and Fotis C Kafatos},
issn = {0261-4189},
year = {1996},
date = {1996-09-01},
journal = {EMBO J.},
volume = {15},
number = {17},
pages = {4691--4701},
abstract = {A novel rel family member, Gambif1 (gambiae immune factor 1), has been cloned from the human malaria vector, Anopheles gambiae, and shown to be most similar to Drosophila Dorsal and Dif. Gambif1 protein is translocated to the nucleus in fat body cells in response to bacterial challenge, although the mRNA is present at low levels at all developmental stages and is not induced by infection. DNA binding activity to the kappaB-like sites in the A.gambiae Defensin and the Drosophila Diptericin and Cecropin promoters is also induced in larval nuclear extracts following infection. Gambif1 has the ability to bind to kappaB-like sites in vitro. Co-transfection assays in Drosophila mbn-2 cells show that Gambif1 can activate transcription by interacting with the Drosophila Diptericin regulatory elements, but is not functionally equivalent to Dorsal in this assay. Gambif1 protein translocation to the nucleus and the appearance of kappaB-like DNA binding activity can serve as molecular markers of activation of the immune system and open up the possibility of studying the role of defence reactions in determining mosquito susceptibility/refractoriness to malaria infection.},
keywords = {Amino Acid, Animals, Anopheles, Base Sequence, Biological Transport, Cell Nucleus, Cells, Complementary, Cultured, DNA, DNA-Binding Proteins, hoffmann, Insect Proteins, Insect Vectors, M3i, NF-kappa B, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-rel, Sequence Homology, Trans-Activators, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
Gross I, Georgel Philippe, Kappler Christine, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin Article de journal
Dans: Nucleic Acids Res., vol. 24, no. 7, p. 1238–1245, 1996, ISSN: 0305-1048.
Résumé | BibTeX | Étiquettes: Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation
@article{gross_drosophila_1996,
title = {Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin},
author = {I Gross and Philippe Georgel and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1996},
date = {1996-04-01},
journal = {Nucleic Acids Res.},
volume = {24},
number = {7},
pages = {1238--1245},
abstract = {In Drosophila, bacterial challenge induces the rapid transcription of several genes encoding potent antibacterial peptides. The upstream sequences of the diptericin and cecropin Al genes, which have been investigated in detail, contain two, respectively one sequence element homologous to the binding site of the mammalian nuclear factor kappaB. These elements have been shown to be mandatory for immune-induced transcription of both genes. Functional studies have shown that these kappaB-related elements can be the target for the Drosophila Rel proteins dorsal and Dif. Here we present a comparative analysis of the transactivating capacities of these proteins on reporter genes fused to either the diptericin or the cecropin kappaB-related motifs. We conclude from our results: (i) the kappaB motifs of the diptericin and cecropin genes are not functionally equivalent; (ii) the dorsal and Dif proteins have distinct DNA-binding characteristics; (iii) dorsal and Dif can heterodimerize in vitro; (iv) mutants containing no copies of dorsal and a single copy of Dif retain their full capacity to express the diptericin and cecropin genes in response to challenge.},
keywords = {Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Nicolas E, Michaut Lydia, Reichhart Jean-Marc, Hoffmann Jules A
The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults Article de journal
Dans: Cell, vol. 86, no. 6, p. 973–983, 1996, ISSN: 0092-8674.
Résumé | BibTeX | Étiquettes: Animals, Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors
@article{lemaitre_dorsoventral_1996,
title = {The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults},
author = {Bruno Lemaitre and E Nicolas and Lydia Michaut and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0092-8674},
year = {1996},
date = {1996-01-01},
journal = {Cell},
volume = {86},
number = {6},
pages = {973--983},
abstract = {The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways.},
keywords = {Animals, Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Kappler Christine, Langley E, Gross I, Nicolas E, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter Article de journal
Dans: Nucleic Acids Res., vol. 23, no. 7, p. 1140–1145, 1995, ISSN: 0305-1048.
Résumé | BibTeX | Étiquettes: Animals, Base Sequence, CCAAT-Enhancer-Binding Proteins, DNA, DNA-Binding Proteins, Genes, Genetic, hoffmann, Immunity, Insect, Insect Hormones, Insect Proteins, interferons, Lipopolysaccharides, M3i, NF-kappa B, Nuclear Proteins, Plasmids, Promoter Regions, reichhart, Up-Regulation
@article{georgel_drosophila_1995,
title = {Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter},
author = {Philippe Georgel and Christine Kappler and E Langley and I Gross and E Nicolas and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1995},
date = {1995-04-01},
journal = {Nucleic Acids Res.},
volume = {23},
number = {7},
pages = {1140--1145},
abstract = {Bacterial challenge of larvae or adults of Drosophila induces the rapid transcription of several genes encoding antibacterial peptides with a large spectrum of activity. One of these peptides, the 82-residue anti-gram negative diptericin, is encoded by a single intronless gene and we are investigating the control of expression of this gene. Previous studies using both transgenic experiments and footprint analysis have highlighted the role in the induction of this gene of a 30 nucleotide region which contains three partially overlapping motifs with sequence homology to mammalian NF-kappa B and NF-IL6 response elements and to the GAAANN sequence present in the interferon consensus response elements of some mammalian interferon-induced genes. We now show that the latter sequence binds in immune responsive tissues (fat body, blood cells) of Drosophila a approximately 45 kDa polypeptide which cross-reacts with a polyserum directed against mammalian interferon Regulatory Factor-I. Using a transfection assay of Drosophila tumorous blood cells, we show that the GAAANN sequence positively regulates the activity of the diptericin promoter. We propose that this motif cooperatively interacts with the other response elements in the regulation of the diptericin gene expression.},
keywords = {Animals, Base Sequence, CCAAT-Enhancer-Binding Proteins, DNA, DNA-Binding Proteins, Genes, Genetic, hoffmann, Immunity, Insect, Insect Hormones, Insect Proteins, interferons, Lipopolysaccharides, M3i, NF-kappa B, Nuclear Proteins, Plasmids, Promoter Regions, reichhart, Up-Regulation},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Meister Marie, Kappler Christine, Lemaitre Bruno, Reichhart Jean-Marc, Hoffmann Jules A
Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements Article de journal
Dans: Biochem. Biophys. Res. Commun., vol. 197, no. 2, p. 508–517, 1993, ISSN: 0006-291X.
Résumé | Liens | BibTeX | Étiquettes: Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart
@article{georgel_insect_1993,
title = {Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements},
author = {Philippe Georgel and Marie Meister and Christine Kappler and Bruno Lemaitre and Jean-Marc Reichhart and Jules A Hoffmann},
doi = {10.1006/bbrc.1993.2508},
issn = {0006-291X},
year = {1993},
date = {1993-12-01},
journal = {Biochem. Biophys. Res. Commun.},
volume = {197},
number = {2},
pages = {508--517},
abstract = {We are using the diptericin gene as a model system to study the control of expression of the genes encoding antibacterial peptides during the Drosophila immune reaction. In order to investigate the putative regulatory regions in the diptericin promoter, we performed DNaseI footprinting experiments combined with gel-shift assays in two inducible systems: the larval fat body and a tumorous Drosophila blood cell line. Our results confirm the importance of kappa B-like elements previously described in the immune response of insects and reveal for the first time the involvement of other regions containing sequences homologous to mammalian acute-phase response elements.},
keywords = {Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart},
pubstate = {published},
tppubtype = {article}
}
Kappler Christine, Meister Marie, Lagueux Marie, Gateff E, Hoffmann Jules A, Reichhart Jean-Marc
Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila Article de journal
Dans: EMBO J., vol. 12, no. 4, p. 1561–1568, 1993, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection
@article{kappler_insect_1993,
title = {Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila},
author = {Christine Kappler and Marie Meister and Marie Lagueux and E Gateff and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {1993},
date = {1993-04-01},
journal = {EMBO J.},
volume = {12},
number = {4},
pages = {1561--1568},
abstract = {The Drosophila diptericin gene codes for a 9 kDa antibacterial peptide and is rapidly and transiently expressed in larvae and adults after bacterial challenge. It is also induced in a tumorous Drosophila blood cell line by the addition of lipopolysaccharide (LPS). The promoter of this gene contains two 17 bp repeats located closely upstream of the TATA-box and harbouring a decameric kappa B-related sequence. This study reports that the replacement of the two 17 bp repeats by random sequences abolishes bacteria inducibility in transgenic fly lines. In transfected tumorous blood cells, the replacement of both or either of the 17 bp motifs reduces dramatically LPS inducibility, whereas multiple copies significantly increase the level of transcriptional activation by LPS challenge. A specific DNA-protein binding activity is evidenced in cytoplasmic and nuclear extracts of induced blood cells and fat body. It is absent in controls. It is proposed that induction of the diptericin gene mediated by the two 17 bp repeats occurs via a mechanism similar to that of mammalian NF-kappa B.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection},
pubstate = {published},
tppubtype = {article}
}
Reichhart Jean-Marc, Georgel Philippe, Meister Marie, Lemaitre Bruno, Kappler Christine, Hoffmann Jules A
Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila Article de journal
Dans: C. R. Acad. Sci. III, Sci. Vie, vol. 316, no. 10, p. 1218–1224, 1993, ISSN: 0764-4469.
Résumé | BibTeX | Étiquettes: Animals, Blotting, Cellular, Gene Expression, Genes, Genetic, hoffmann, Immunity, Insect, M3i, NF-kappa B, Northern, reichhart, translocation, Zygote
@article{reichhart_expression_1993,
title = {Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila},
author = {Jean-Marc Reichhart and Philippe Georgel and Marie Meister and Bruno Lemaitre and Christine Kappler and Jules A Hoffmann},
issn = {0764-4469},
year = {1993},
date = {1993-01-01},
journal = {C. R. Acad. Sci. III, Sci. Vie},
volume = {316},
number = {10},
pages = {1218--1224},
abstract = {The rel/NF-kappa B-related morphogen dorsal is a maternally expressed gene which is involved in the control of the dorso-ventral axis during early embryogenesis of Drosophila. We show that this gene is also expressed in the fat body of larvae and adults of Drosophila as well as in a tumorous blood cell line: its expression is noticeably enhanced upon bacterial (or lipopolysaccharide) challenge. This challenge also induces within 15-30 min a nuclear translocation of the dorsal protein. The genes encoding inducible antibacterial peptides in Drosophila contain kappa B-related nucleotide sequences and we show that the dorsal protein can bind to such motifs and sequence-specifically transactivate a reporter gene in co-transfection experiments with a Drosophila cell line. However, in dl1 mutants, in the absence of dorsal protein, the genes encoding antibacterial peptides retain their inducibility, suggesting a multifactorial control. The results indicate that in addition to its role in embryogenesis, dorsal is involved in the immune response of Drosophila. They also strengthen the analogy between the mammalian acute phase response and the insect immune response.},
keywords = {Animals, Blotting, Cellular, Gene Expression, Genes, Genetic, hoffmann, Immunity, Insect, M3i, NF-kappa B, Northern, reichhart, translocation, Zygote},
pubstate = {published},
tppubtype = {article}
}