Publications
2005
Reichhart Jean-Marc
Tip of another iceberg: Drosophila serpins Article de journal
Dans: Trends Cell Biol., vol. 15, no. 12, p. 659–665, 2005, ISSN: 0962-8924.
Résumé | Liens | BibTeX | Étiquettes: Animals, Immunity, M3i, Protein Conformation, reichhart, Serine Proteinase Inhibitors, Serpins
@article{reichhart_tip_2005,
title = {Tip of another iceberg: Drosophila serpins},
author = {Jean-Marc Reichhart},
doi = {10.1016/j.tcb.2005.10.001},
issn = {0962-8924},
year = {2005},
date = {2005-12-01},
journal = {Trends Cell Biol.},
volume = {15},
number = {12},
pages = {659--665},
abstract = {Serpins are serine protease inhibitors with a conserved structure that have been identified in nearly all species and act as suicide substrates by binding covalently to their target proteases. Serpins regulate various physiological processes and defence mechanisms. In humans, several serpin mutations are linked to diseases. The genome of Drosophila melanogaster encodes 29 serpins and even more serine proteases. To date, three serpins have been investigated in detail. Spn27A controls the Toll pathway during early development and is involved in defence reactions in adult flies. SPN42DaA is an inhibitor of furin, a subtilisin-like convertase that is required for pro-protein maturation. Spn43Ac controls the Toll pathway during the immune response. In each case, Drosophila genetics has shed new light on the function of these serine protease inhibitors.},
keywords = {Animals, Immunity, M3i, Protein Conformation, reichhart, Serine Proteinase Inhibitors, Serpins},
pubstate = {published},
tppubtype = {article}
}
2003
Ligoxygakis Petros, Roth Siegfried, Reichhart Jean-Marc
A serpin regulates dorsal-ventral axis formation in the Drosophila embryo Article de journal
Dans: Curr. Biol., vol. 13, no. 23, p. 2097–2102, 2003, ISSN: 0960-9822.
Résumé | BibTeX | Étiquettes: Animals, Body Patterning, Cell Surface, Crosses, Female, Genetic, Immunohistochemistry, M3i, Microinjections, Receptors, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors
@article{ligoxygakis_serpin_2003,
title = {A serpin regulates dorsal-ventral axis formation in the Drosophila embryo},
author = {Petros Ligoxygakis and Siegfried Roth and Jean-Marc Reichhart},
issn = {0960-9822},
year = {2003},
date = {2003-12-01},
journal = {Curr. Biol.},
volume = {13},
number = {23},
pages = {2097--2102},
abstract = {Extracellular serine protease cascades have evolved in vertebrates and invertebrates to mediate rapid, local reactions to physiological or pathological cues. The serine protease cascade that triggers the Toll signaling pathway in Drosophila embryogenesis shares several organizational characteristics with those involved in mammalian complement and blood clotting. One of the hallmarks of such cascades is their regulation by serine protease inhibitors (serpins). Serpins act as suicide substrates and are cleaved by their target protease, forming an essentially irreversible 1:1 complex. The biological importance of serpins is highlighted by serpin dysfunction diseases, such as thrombosis caused by a deficiency in antithrombin. Here, we describe how a serpin controls the serine protease cascade, leading to Toll pathway activation. Female flies deficient in Serpin-27A produce embryos that lack dorsal-ventral polarity and show uniform high levels of Toll signaling. Since this serpin has been recently shown to restrain an immune reaction in the blood of Drosophila, it demonstrates that proteolysis can be regulated by the same serpin in different biological contexts.},
keywords = {Animals, Body Patterning, Cell Surface, Crosses, Female, Genetic, Immunohistochemistry, M3i, Microinjections, Receptors, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
1999
Levashina Elena A, Langley E, Green C, Gubb David, Ashburner M, Hoffmann Jules A, Reichhart Jean-Marc
Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila Article de journal
Dans: Science, vol. 285, no. 5435, p. 1917–1919, 1999, ISSN: 0036-8075.
Résumé | BibTeX | Étiquettes: Animals, Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, hoffmann, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation
@article{levashina_constitutive_1999,
title = {Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila},
author = {Elena A Levashina and E Langley and C Green and David Gubb and M Ashburner and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0036-8075},
year = {1999},
date = {1999-09-01},
journal = {Science},
volume = {285},
number = {5435},
pages = {1917--1919},
abstract = {The antifungal defense of Drosophila is controlled by the spaetzle/Toll/cactus gene cassette. Here, a loss-of-function mutation in the gene encoding a blood serine protease inhibitor, Spn43Ac, was shown to lead to constitutive expression of the antifungal peptide drosomycin, and this effect was mediated by the spaetzle and Toll gene products. Spaetzle was cleaved by proteolytic enzymes to its active ligand form shortly after immune challenge, and cleaved Spaetzle was constitutively present in Spn43Ac-deficient flies. Hence, Spn43Ac negatively regulates the Toll signaling pathway, and Toll does not function as a pattern recognition receptor in the Drosophila host defense.},
keywords = {Animals, Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, hoffmann, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation},
pubstate = {published},
tppubtype = {article}
}