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I2CT
Immunologie, Immunopathologie et Chimie Thérapeutique
Publications
2011
Murphy Fiona A, Poland Craig A, Duffin Rodger, Al-Jamal Khuloud T, Ali-Boucetta Hanene, Nunes Antonio, Byrne Fiona, Prina-Mello Adriele, Volkov Yuri, Li Shouping, Mather Stephen J, Bianco Alberto, Prato Maurizio, Macnee William, Wallace William A, Kostarelos Kostas, Donaldson Ken
Length-dependent retention of carbon nanotubes in the pleural space of mice initiates sustained inflammation and progressive fibrosis on the parietal pleura Article de journal
Dans: The American Journal of Pathology, vol. 178, non 6, p. 2587–2600, 2011, ISSN: 1525-2191.
Résumé | Liens | BibTeX | Étiquettes: Animals, carbon, Cell Proliferation, Disease Progression, Emission-Computed, Epithelium, Fibrosis, I2CT, inflammation, Lymph Nodes, Mediastinum, Mice, Nanotubes, Nanowires, Particle Size, Pleura, Pleural Cavity, Single-Photon, Team-Bianco, Time Factors, Tomography, X-Ray Computed
@article{murphy_length-dependent_2011,
title = {Length-dependent retention of carbon nanotubes in the pleural space of mice initiates sustained inflammation and progressive fibrosis on the parietal pleura},
author = {Fiona A Murphy and Craig A Poland and Rodger Duffin and Khuloud T Al-Jamal and Hanene Ali-Boucetta and Antonio Nunes and Fiona Byrne and Adriele Prina-Mello and Yuri Volkov and Shouping Li and Stephen J Mather and Alberto Bianco and Maurizio Prato and William Macnee and William A Wallace and Kostas Kostarelos and Ken Donaldson},
doi = {10.1016/j.ajpath.2011.02.040},
issn = {1525-2191},
year = {2011},
date = {2011-06-01},
journal = {The American Journal of Pathology},
volume = {178},
number = {6},
pages = {2587--2600},
abstract = {The fibrous shape of carbon nanotubes (CNTs) raises concern that they may pose an asbestos-like inhalation hazard, leading to the development of diseases, especially mesothelioma. Direct instillation of long and short CNTs into the pleural cavity, the site of mesothelioma development, produced asbestos-like length-dependent responses. The response to long CNTs and long asbestos was characterized by acute inflammation, leading to progressive fibrosis on the parietal pleura, where stomata of strictly defined size limit the egress of long, but not short, fibers. This was confirmed by demonstrating clearance of short, but not long, CNT and nickel nanowires and by visualizing the migration of short CNTs from the pleural space by single-photon emission computed tomographic imaging. Our data confirm the hypothesis that, although a proportion of all deposited particles passes through the pleura, the pathogenicity of long CNTs and other fibers arises as a result of length-dependent retention at the stomata on the parietal pleura.},
keywords = {Animals, carbon, Cell Proliferation, Disease Progression, Emission-Computed, Epithelium, Fibrosis, I2CT, inflammation, Lymph Nodes, Mediastinum, Mice, Nanotubes, Nanowires, Particle Size, Pleura, Pleural Cavity, Single-Photon, Team-Bianco, Time Factors, Tomography, X-Ray Computed},
pubstate = {published},
tppubtype = {article}
}
The fibrous shape of carbon nanotubes (CNTs) raises concern that they may pose an asbestos-like inhalation hazard, leading to the development of diseases, especially mesothelioma. Direct instillation of long and short CNTs into the pleural cavity, the site of mesothelioma development, produced asbestos-like length-dependent responses. The response to long CNTs and long asbestos was characterized by acute inflammation, leading to progressive fibrosis on the parietal pleura, where stomata of strictly defined size limit the egress of long, but not short, fibers. This was confirmed by demonstrating clearance of short, but not long, CNT and nickel nanowires and by visualizing the migration of short CNTs from the pleural space by single-photon emission computed tomographic imaging. Our data confirm the hypothesis that, although a proportion of all deposited particles passes through the pleura, the pathogenicity of long CNTs and other fibers arises as a result of length-dependent retention at the stomata on the parietal pleura.
2008
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 Article de journal
Dans: Cell Death and Differentiation, vol. 15, non 4, p. 793–804, 2008, ISSN: 1350-9047.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
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.
2005
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 Article de journal
Dans: Nature Chemical Biology, vol. 1, non 7, p. 377–382, 2005, ISSN: 1552-4450.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
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.
Weber Alexander N R, Moncrieffe Martin C, Gangloff Monique, Imler Jean-Luc, Gay Nicholas J
Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway Article de journal
Dans: The Journal of Biological Chemistry, vol. 280, non 24, p. 22793–22799, 2005, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation
@article{weber_ligand-receptor_2005,
title = {Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway},
author = {Alexander N R Weber and Martin C Moncrieffe and Monique Gangloff and Jean-Luc Imler and Nicholas J Gay},
doi = {10.1074/jbc.M502074200},
issn = {0021-9258},
year = {2005},
date = {2005-01-01},
journal = {The Journal of Biological Chemistry},
volume = {280},
number = {24},
pages = {22793--22799},
abstract = {In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions.},
keywords = {Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation},
pubstate = {published},
tppubtype = {article}
}
In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions.
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 Article de journal
Dans: Nature Chemical Biology, vol. 1, non 7, p. 377–382, 2005, ISSN: 1552-4450.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
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.
2003
Goto Akira, Blandin Stéphanie A, Royet Julien, Reichhart Jean-Marc, Levashina Elena A
Silencing of Toll pathway components by direct injection of double-stranded RNA into Drosophila adult flies Article de journal
Dans: Nucleic Acids Res., vol. 31, non 22, p. 6619–6623, 2003, ISSN: 1362-4962.
Résumé | BibTeX | Étiquettes: Animals, blandin, Cell Surface, Double-Stranded, Epistasis, Female, Genetic, Green Fluorescent Proteins, Homeodomain Proteins, Luminescent Proteins, M3i, Phenotype, Receptors, reichhart, RNA, RNA Interference, Serpins, Signal Transduction, Time Factors, Toll-Like Receptors, Transcription Factors
@article{goto_silencing_2003,
title = {Silencing of Toll pathway components by direct injection of double-stranded RNA into Drosophila adult flies},
author = {Akira Goto and Stéphanie A Blandin and Julien Royet and Jean-Marc Reichhart and Elena A Levashina},
issn = {1362-4962},
year = {2003},
date = {2003-11-01},
journal = {Nucleic Acids Res.},
volume = {31},
number = {22},
pages = {6619--6623},
abstract = {Double-stranded RNA (dsRNA) gene interference is an efficient method to silence gene expression in a sequence-specific manner. Here we show that the direct injection of dsRNA can be used in adult Drosophila flies to disrupt function of endogenous genes in vivo. As a proof of principle, we have used this method to silence components of a major signaling cascade, the Toll pathway, which controls fruit fly resistance to fungal and Gram-positive bacterial infections. We demonstrate that the knockout is efficient only if dsRNA is injected in 4- or more day-old flies and that it lasts for at least 1 week. Furthermore, we report dsRNA-based epistatic gene analysis via injection of a mixture of two dsRNAs and propose that injection of dsRNA represents a powerful method for rapid functional analysis of genes in Drosophila melanogaster adults, particularly of those whose mutations are lethal during development.},
keywords = {Animals, blandin, Cell Surface, Double-Stranded, Epistasis, Female, Genetic, Green Fluorescent Proteins, Homeodomain Proteins, Luminescent Proteins, M3i, Phenotype, Receptors, reichhart, RNA, RNA Interference, Serpins, Signal Transduction, Time Factors, Toll-Like Receptors, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Double-stranded RNA (dsRNA) gene interference is an efficient method to silence gene expression in a sequence-specific manner. Here we show that the direct injection of dsRNA can be used in adult Drosophila flies to disrupt function of endogenous genes in vivo. As a proof of principle, we have used this method to silence components of a major signaling cascade, the Toll pathway, which controls fruit fly resistance to fungal and Gram-positive bacterial infections. We demonstrate that the knockout is efficient only if dsRNA is injected in 4- or more day-old flies and that it lasts for at least 1 week. Furthermore, we report dsRNA-based epistatic gene analysis via injection of a mixture of two dsRNAs and propose that injection of dsRNA represents a powerful method for rapid functional analysis of genes in Drosophila melanogaster adults, particularly of those whose mutations are lethal during development.
1998
Uttenweiler-Joseph S, Moniatte M, Lagueux Marie, Dorsselaer Van A, Hoffmann Jules A, Bulet Philippe
Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 95, non 19, p. 11342–11347, 1998, ISSN: 0027-8424.
Résumé | BibTeX | Étiquettes: Animals, bacteria, Chromatography, Cloning, Hemolymph, High Pressure Liquid, hoffmann, Immunity, Insect Proteins, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, messenger, Molecular, Peptides, Protein Precursors, RNA, Sequence Analysis, Spectrometry, Time Factors
@article{uttenweiler-joseph_differential_1998,
title = {Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study},
author = {S Uttenweiler-Joseph and M Moniatte and Marie Lagueux and Van A Dorsselaer and Jules A Hoffmann and Philippe Bulet},
issn = {0027-8424},
year = {1998},
date = {1998-09-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {95},
number = {19},
pages = {11342--11347},
abstract = {We have developed an approach based on a differential mass spectrometric analysis to detect molecules induced during the immune response of Drosophila, regardless of their biological activities. For this, we have applied directly matrix-assisted laser desorption/ionization MS to hemolymph samples from individual flies before and after an immune challenge. This method provided precise information on the molecular masses of immune-induced molecules and allowed the detection, in the molecular range of 1.5-11 kDa, of 24 Drosophila immune-induced molecules (DIMs). These molecules are all peptides, and four correspond to already characterized antimicrobial peptides. We have further analyzed the induction of the various peptides by immune challenge in wild-type flies and in mutants with a compromised antimicrobial response. We also describe a methodology combining matrix-assisted laser desorption ionization time-of-flight MS, HPLC, and Edman degradation, which yielded the peptide sequence of three of the DIMs. Finally, molecular cloning and Northern blot analyses revealed that one of the DIMs is produced as a prepropeptide and is inducible on a bacterial challenge.},
keywords = {Animals, bacteria, Chromatography, Cloning, Hemolymph, High Pressure Liquid, hoffmann, Immunity, Insect Proteins, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, messenger, Molecular, Peptides, Protein Precursors, RNA, Sequence Analysis, Spectrometry, Time Factors},
pubstate = {published},
tppubtype = {article}
}
We have developed an approach based on a differential mass spectrometric analysis to detect molecules induced during the immune response of Drosophila, regardless of their biological activities. For this, we have applied directly matrix-assisted laser desorption/ionization MS to hemolymph samples from individual flies before and after an immune challenge. This method provided precise information on the molecular masses of immune-induced molecules and allowed the detection, in the molecular range of 1.5-11 kDa, of 24 Drosophila immune-induced molecules (DIMs). These molecules are all peptides, and four correspond to already characterized antimicrobial peptides. We have further analyzed the induction of the various peptides by immune challenge in wild-type flies and in mutants with a compromised antimicrobial response. We also describe a methodology combining matrix-assisted laser desorption ionization time-of-flight MS, HPLC, and Edman degradation, which yielded the peptide sequence of three of the DIMs. Finally, molecular cloning and Northern blot analyses revealed that one of the DIMs is produced as a prepropeptide and is inducible on a bacterial challenge.
1975
Feyereisen R, Lagueux Marie, Hoffmann Jules A
The hemolymphatic transport of molting hormone during the development of Locusta migratoria L Article de journal
Dans: C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat., vol. 280, non 14, p. 1709–1712, 1975.
Résumé | BibTeX | Étiquettes: Age Factors, Animals, Carrier Proteins, Chromatography, Ecdysone, Ecdysterone, Gel, Grasshoppers, Hematopoietic System, hoffmann, Larva, M3i, Neurosecretory Systems, Protein Binding, Time Factors
@article{feyereisen_hemolymphatic_1975,
title = {The hemolymphatic transport of molting hormone during the development of Locusta migratoria L},
author = {R Feyereisen and Marie Lagueux and Jules A Hoffmann},
year = {1975},
date = {1975-04-01},
journal = {C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat.},
volume = {280},
number = {14},
pages = {1709--1712},
abstract = {Shortly after injection of radio-labelled ecdysone into fifth instar larvae of Locusta migratoria, 20-hydroxy-ecdysone (ecdysterone) is the main hormone found in the blood. Some 10% of the circulating hormone are bound to hemolymph macromolecules. The ratio of bound to free hormone is stage-dependent; it decreases considerably after previous injections of non-labelled ecdysone, but increases in insects in which ecdysone biosynthesis has been blocked by extirpation of the prothoracic glands or selective X-ray treatment of the hemocytopoietic tissue.},
keywords = {Age Factors, Animals, Carrier Proteins, Chromatography, Ecdysone, Ecdysterone, Gel, Grasshoppers, Hematopoietic System, hoffmann, Larva, M3i, Neurosecretory Systems, Protein Binding, Time Factors},
pubstate = {published},
tppubtype = {article}
}
Shortly after injection of radio-labelled ecdysone into fifth instar larvae of Locusta migratoria, 20-hydroxy-ecdysone (ecdysterone) is the main hormone found in the blood. Some 10% of the circulating hormone are bound to hemolymph macromolecules. The ratio of bound to free hormone is stage-dependent; it decreases considerably after previous injections of non-labelled ecdysone, but increases in insects in which ecdysone biosynthesis has been blocked by extirpation of the prothoracic glands or selective X-ray treatment of the hemocytopoietic tissue.
1974
Hoffmann Jules A, Koolman J, Karlson P, Joly P
Molting hormone titer and metabolic fate of injected ecdysone during the fifth larval instar and in adults of Locusta migratoria (Orthoptera) Article de journal
Dans: Gen. Comp. Endocrinol., vol. 22, non 1, p. 90–97, 1974, ISSN: 0016-6480.
BibTeX | Étiquettes: Age Factors, Animals, Chromatography, Ecdysone, Feces, Grasshoppers, hoffmann, Hydroxylation, Invertebrate Hormones, Larva, M3i, Thin Layer, Time Factors, Tritium
@article{hoffmann_molting_1974,
title = {Molting hormone titer and metabolic fate of injected ecdysone during the fifth larval instar and in adults of Locusta migratoria (Orthoptera)},
author = {Jules A Hoffmann and J Koolman and P Karlson and P Joly},
issn = {0016-6480},
year = {1974},
date = {1974-01-01},
journal = {Gen. Comp. Endocrinol.},
volume = {22},
number = {1},
pages = {90--97},
keywords = {Age Factors, Animals, Chromatography, Ecdysone, Feces, Grasshoppers, hoffmann, Hydroxylation, Invertebrate Hormones, Larva, M3i, Thin Layer, Time Factors, Tritium},
pubstate = {published},
tppubtype = {article}
}
1973
Koolman J, Hoffmann Jules A, Karlson P
Sulphage esters as inactivation products of ecdysone in Locusta migratoria Article de journal
Dans: Hoppe-Seyler's Z. Physiol. Chem., vol. 354, non 9, p. 1043–1048, 1973, ISSN: 0018-4888.
BibTeX | Étiquettes: Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium
@article{koolman_sulphage_1973,
title = {Sulphage esters as inactivation products of ecdysone in Locusta migratoria},
author = {J Koolman and Jules A Hoffmann and P Karlson},
issn = {0018-4888},
year = {1973},
date = {1973-09-01},
journal = {Hoppe-Seyler's Z. Physiol. Chem.},
volume = {354},
number = {9},
pages = {1043--1048},
keywords = {Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium},
pubstate = {published},
tppubtype = {article}
}