8 results on '"Gatti, Jean-Luc"'
Search Results
2. Shedding of the germinal angiotensin I-converting enzyme (gACE) involves a serine protease and is activated by epididymal fluid
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Thimon, V., Metayer, Sonia, Belghazi, M., Dacheux, Françoise, Dacheux, J.L., Gatti, Jean-Luc, Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Station de Recherches Avicoles (SRA), Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS)
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Epididymis ,Male ,Serine Proteinase Inhibitors ,Sheep ,Base Sequence ,Swine ,[SDV]Life Sciences [q-bio] ,Cell Membrane ,Molecular Sequence Data ,Serine Endopeptidases ,Extracellular Fluid ,Peptidyl-Dipeptidase A ,Spermatozoa ,Benzamidines ,Protein Structure, Tertiary ,Enzyme Activation ,TRACTUS REPRODUCTEUR MALE ,Animals ,[INFO]Computer Science [cs] ,Amino Acid Sequence ,Sulfones ,Phosphorylation ,Protein Processing, Post-Translational ,Sequence Analysis - Abstract
International audience; The present report describes how the soluble germinal angiotensin 1-converting enzyme (gACE) appears in the epididymal fluid, where it has been identified in some laboratory rodents and domestic ungulates. We showed that this gACE results from an active proteolytic process that releases the enzyme's extracellular domain from sperm in a precise spatiotemporal location during epididymal transit and that this process involves serine protease activity. Using polyclonal antibodies against the C-terminal intracellular sequence of ACE, a fragment of approximately 10 kDa was detected on the sperm extract only in the epididymal region, where the gACE release occurs. The fluid enzyme was purified, and the cleavage site was determined by mass spectrometry to be between Arg(622) and Leu(623) of the mature sheep gACE sequence (equivalent to Arg(627) and Arg(1203) of the human mature gACE and somatic ACE sequences, respectively). Thereafter, the C-terminal Arg was removed, leaving Ala(621) as a C-terminal. Using an in vitro assay, gACE cleavage from sperm was strongly increased by the presence of epididymal fluid from the release zone, and this increase was inhibited specifically by the serine protease-inhibitor AEBSF but not by para-aminobenzamidine. None of the other inhibitors tested, such as metallo- or cystein-protease inhibitors, had a similar effect on release. It was also found that this process did not involve changes in gACE phosphorylation.
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- 2005
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3. Germinal angiotensin I-converting enzyme is totally shed from the rodent sperm membrane during epididymal maturation
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Metayer, Sonia, Dacheux, Françoise, Dacheux, J.L., Gatti, Jean-Luc, Station de Recherches Avicoles (SRA), Institut National de la Recherche Agronomique (INRA), Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS)
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Male ,endocrine system ,Blotting, Western ,Peptidyl-Dipeptidase A ,rattus rattus ,reproduction ,mâle ,Mice ,Biologie de la reproduction ,Animals ,reproductive and urinary physiology ,Epididymis ,Reproductive Biology ,épididyme ,urogenital system ,maturation ,angiotensine ,Cell Membrane ,[SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology ,pouvoir fecondant ,spermatozoide ,Spermatozoa ,Rats ,Molecular Weight ,enzyme ,protéine ,Rats, Inbred Lew ,RAT - Abstract
International audience; Acquisition of sperm fertilizing ability is due, in part, to the reorganization of plasma membrane proteins that occurs during epididymal sperm transit. Using polyclonal antibodies against angiotensin I-converting enzyme (ACE), we showed that this enzyme is immunolocalized mainly on the middle piece of rat and mouse testicular sperm and with less intensity along the initial part of the principal piece of the flagellum. In both species, only some sperm from the caput epididymis were still reactive, whereas no labeling was observed on cauda epididymal sperm. The 105- to 110-kDa germinal ACE was absent from the rat testicular fluid but appeared in the fluid of the anterior epididymis. Thereafter, its molecular weight shifted to 94 kDa in the corpus epididymal fluid and remained at this weight in the caudal region. The 105- to 110-kDa immunoreactive protein was present in testicular rat sperm extract but was completely absent from epididymal sperm extracts. Western blot analysis of testicular and epididymal tissue extracts from the rat and mouse also confirmed that the germinal enzyme was absent from the epididymal sperm cell. Our results demonstrated that the rodent germinal ACE is released from the testicular sperm membrane when sperm enter the epididymis, a process similar to that observed in domestic mammals. This result is discussed in view of the suggested role for this enzyme in sperm fertility.
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- 2002
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4. Figure S1;Figure S2;Figure S3;Supplementary file 1: Primer sequences and statistical data;Supplementary file 1: Primer sequences and statistical data from Aphid infestation differently affects the defences of nitrate-fed and nitrogen-fixing Medicago truncatula and alters symbiotic nitrogen fixation
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Gaurav Pandharikar, Gatti, Jean-Luc, Jean-Christophe Simon, Frendo, Pierre, and Poirie, Marylène
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fungi ,food and beverages ,biochemical phenomena, metabolism, and nutrition ,6. Clean water - Abstract
Experimental design, plants and aphids materials.;Comparison of the fresh and dry weight of NFS and NI plants before aphid infestation. ;Relative level of expression of PR1 and PI genes in NFS or NI control plants. ;Table S1. Primer sequences and conditions for qPCR analysis.;Tables S2 to S10: Statistical results for each experiment.
5. Figure S1;Figure S2;Figure S3;Supplementary file 1: Primer sequences and statistical data;Supplementary file 1: Primer sequences and statistical data from Aphid infestation differently affects the defences of nitrate-fed and nitrogen-fixing Medicago truncatula and alters symbiotic nitrogen fixation
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Gaurav Pandharikar, Gatti, Jean-Luc, Jean-Christophe Simon, Frendo, Pierre, and Poirie, Marylène
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fungi ,food and beverages ,biochemical phenomena, metabolism, and nutrition ,6. Clean water - Abstract
Experimental design, plants and aphids materials.;Comparison of the fresh and dry weight of NFS and NI plants before aphid infestation. ;Relative level of expression of PR1 and PI genes in NFS or NI control plants. ;Table S1. Primer sequences and conditions for qPCR analysis.;Tables S2 to S10: Statistical results for each experiment.
6. Time-course analysis of Drosophila suzukii interaction with endoparasitoid wasps evidences a delayed encapsulation response compared to D. melanogaster
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Jean-Luc Gatti, Nicolas Ris, Marylène Poirié, Alessia Iacovone, Institut Sophia Agrobiotech (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA), ANR-11-LABX-0028, Provence Alpes Côte d’Azur region, SPE INRA, European Project: 613678,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,DROPSA(2014), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA), Poirie, Marylène, and Gatti, Jean-Luc
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Male ,0301 basic medicine ,Life Cycles ,Time Factors ,Oviposition ,[SDV]Life Sciences [q-bio] ,Wasps ,lcsh:Medicine ,Pathogenesis ,Pathology and Laboratory Medicine ,interaction hôte parasitoïde ,Parasitoid ,Larvae ,Medicine and Health Sciences ,Melanogaster ,lcsh:Science ,Heterotoma ,Drosophila suzukii ,Immune Response ,ComputingMilieux_MISCELLANEOUS ,endoparasitoïde ,Larva ,Multidisciplinary ,Ecology ,biology ,Eukaryota ,Animal Models ,Trophic Interactions ,Insects ,Experimental Organism Systems ,Community Ecology ,Parasitism ,Host-Pathogen Interactions ,[SDE]Environmental Sciences ,Drosophila ,Female ,Drosophila melanogaster ,Research Article ,étude physiologique ,food.ingredient ,Arthropoda ,Immunology ,Zoology ,Research and Analysis Methods ,drosophila melanogaster ,Host-Parasite Interactions ,03 medical and health sciences ,Model Organisms ,food ,Animals ,leptopilina boulardi ,leptopilina hétérotoma ,Reproductive success ,Ecology and Environmental Sciences ,lcsh:R ,fungi ,Organisms ,Parasite Physiology ,Biology and Life Sciences ,biology.organism_classification ,Invertebrates ,Hymenoptera ,Species Interactions ,drosophila suzukii ,030104 developmental biology ,Parasitology ,lcsh:Q ,Developmental Biology - Abstract
Drosophila suzukii (the spotted-wing Drosophila) appears to be unsuitable for the development of most Drosophila larval endoparasitoids, be they sympatric or not. Here, we questioned the physiological bases of this widespread failure by characterizing the interactions between D. suzukii and various parasitoid species (Asobara japonica, Leptopilina boulardi, Leptopilina heterotoma and Leptopilina victoriae) and comparing them with those observed with D. melanogaster, a rather appropriate host. All parasitoids were able to oviposit in L1 and L2 larval stages of both hosts but their propensity to parasitize was higher on D. melanogaster. A. japonica and, to a much lesser extent, L. heterotoma, were the two species able to successfully develop in D. suzukii, the failure of the parasitism resulting either in the parasitoid encapsulation (notably with L. heterotoma) or the host and parasitoid deaths (especially with L. boulardi and L. victoriae). Compared to D. melanogaster, encapsulation in D. suzukii was strongly delayed and led, if successful, to the production of much larger capsules in surviving flies and, in the event of failure, to the death of both partners because of an uncontrolled melanization. The results thus revealed a different timing of the immune response to parasitoids in D. suzukii compared to D. melanogaster with a lose-lose outcome for parasitoids (generally unsuccessful development) and hosts (high mortality and possible reduction of the fitness of survivors). Finally, these results might suggest that some European endoparasitoids of Drosophila interact with this pest in the field in an unmeasurable way, since they kill their host without reproductive success.
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- 2018
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7. Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma
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Dominique Colinet, Séverine Lemauf, Caroline Anselme, Jean-Luc Gatti, Quentin Coulette, Geneviève Prévost, Marylène Poirié, Ecologie et Dynamique des Systèmes Anthropisés - UMR CNRS 7058 (EDYSAN), Centre National de la Recherche Scientifique (CNRS)-Université de Picardie Jules Verne (UPJV), Université de Picardie Jules Verne (UPJV), Institut Sophia Agrobiotech (ISA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA), ANR-09-BLAN-0243-01, ANR-11-LABX-0028, Ecologie et Dynamique des Systèmes Anthropisés (EDYSAN), Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS), Institut Sophia Agrobiotech [Sophia Antipolis] (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), and Gatti, Jean-Luc
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Models, Molecular ,glycoprotein ,0301 basic medicine ,Glycosylation ,Physiology ,Aspartylglucosaminuria ,[SDV]Life Sciences [q-bio] ,Wasps ,Glycobiology ,venom ,lcsh:Medicine ,Wasp Venoms ,enzyme intracellulaire ,Venom ,Toxicology ,Pathology and Laboratory Medicine ,Biochemistry ,Database and Informatics Methods ,0302 clinical medicine ,Medicine and Health Sciences ,Toxins ,Post-Translational Modification ,lcsh:Science ,reproductive and urinary physiology ,Gel Electrophoresis ,Staining ,chemistry.chemical_classification ,Multidisciplinary ,Drosophila Melanogaster ,Aspartylglucosylaminase ,Animal Models ,female genital diseases and pregnancy complications ,Insects ,Experimental Organism Systems ,dégradation ,Drosophila ,Cellular Structures and Organelles ,Drosophila melanogaster ,Sequence Analysis ,Braconidae ,Research Article ,Silver Staining ,Arthropoda ,Bioinformatics ,Toxic Agents ,education ,venin ,Electrophoretic Staining ,Biology ,Research and Analysis Methods ,Parasitoid wasp ,Electrophoretic Techniques ,03 medical and health sciences ,Model Organisms ,medicine ,Animals ,Secretion ,Amino Acid Sequence ,guêpe ,parasitoid ,glycoprotéine ,parasitoïde ,Venoms ,lcsh:R ,Aspartylglucosaminidase ,Organisms ,Biology and Life Sciences ,Proteins ,Cell Biology ,medicine.disease ,biology.organism_classification ,Invertebrates ,Hymenoptera ,body regions ,030104 developmental biology ,chemistry ,Specimen Preparation and Treatment ,lcsh:Q ,Lysosomes ,Physiological Processes ,Glycoprotein ,Sequence Alignment ,030217 neurology & neurosurgery - Abstract
Aspartylglucosaminidase (AGA) is a low-abundance intracellular enzyme that plays a key role in the last stage of glycoproteins degradation, and whose deficiency leads to human aspartylglucosaminuria, a lysosomal storage disease. Surprisingly, high amounts of AGA-like proteins are secreted in the venom of two phylogenetically distant hymenopteran parasitoid wasp species, Asobara tabida (Braconidae) and Leptopilina heterotoma (Cynipidae). These venom AGAs have a similar domain organization as mammalian AGAs. They share with them key residues for autocatalysis and activity, and the mature α- and β-subunits also form an (αβ)2 structure in solution. Interestingly, only one of these AGAs subunits (α for AtAGA and β for LhAGA) is glycosylated instead of the two subunits for lysosomal human AGA (hAGA), and these glycosylations are partially resistant to PGNase F treatment. The two venom AGAs are secreted as fully activated enzymes, they have a similar aspartylglucosaminidase activity and are both also efficient asparaginases. Once AGAs are injected into the larvae of the Drosophila melanogaster host, the asparaginase activity may play a role in modulating their physiology. Altogether, our data provide new elements for a better understanding of the secretion and the role of venom AGAs as virulence factors in the parasitoid wasps’ success.
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- 2017
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8. Expression, immunolocalization and processing of fertilins ADAM-1 and ADAM-2 in the boar (Sus domesticus) spermatozoa during epididymal maturation
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Elisabeth Pinart, A Fabrega, Sergi Bonet, Jean-Louis Dacheux, Jean-Luc Gatti, Marta Puigmulé, Benoit Guyonnet, Biotechnology of Animal and Human Reproduction (TechnoSperm), Universitat de Girona (UdG), Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Interactions Biotiques et Santé Végétale, Institut National de la Recherche Agronomique (INRA), Gatti, Jean-Luc, Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Université de Tours-Institut Français du Cheval et de l'Equitation [Saumur]-Institut National de la Recherche Agronomique (INRA)
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Male ,Swine ,Porcs -- Espermatozoides ,0302 clinical medicine ,Endocrinology ,FERTILIN ,Testis ,lcsh:Reproduction ,BOARS ,Integral membrane protein ,porc domestique ,IMMUNOBLOTTING ,0303 health sciences ,030219 obstetrics & reproductive medicine ,Membrane Glycoproteins ,biology ,IMMUNILOCALIZATION ,Obstetrics and Gynecology ,mammifère ,EPIDIDYMIS ,[SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism ,Epididymis ,ADAM Proteins ,Spermatozoa ,spermatozoide ,Pigs -- Spermatozoa ,medicine.anatomical_structure ,Fertilins ,protéine ,MEMBRANE PROTEIN ,BIOCHEMISTRY ,FERTILITY ,BIOCHIMIE ,Endocrinologie et métabolisme ,marqueur moléculaire ,Swine -- Spermatozoa ,Gene isoform ,endocrine system ,lcsh:QH471-489 ,Protein subunit ,Molecular Sequence Data ,lcsh:Gynecology and obstetrics ,Andrology ,03 medical and health sciences ,sus scrofa ,medicine ,Animals ,Amino Acid Sequence ,lcsh:RG1-991 ,030304 developmental biology ,immunotransfert ,Endocrinology and metabolism ,épididyme ,maturation ,urogenital system ,Research ,fertilité animale ,Sperm ,Sperm Maturation ,carbohydrates (lipids) ,Membrane glycoproteins ,membrane cellulaire ,Membrane protein ,Reproductive Medicine ,biology.protein ,Developmental Biology ,porc - Abstract
Fertilin alpha (ADAM-1) and beta (ADAM-2) are integral membrane proteins of the ADAM family that form a fertilin complex involved in key steps of the sperm-oocyte membrane interaction. In the present work, we analyzed the presence of ADAM-1 and ADAM-2 mRNAs, the spermatozoa proteins' processing and their sub-cellular localization in epididymal samples from adult boars. ADAM-1 and ADAM-2 mRNAs were highly produced in the testis, but also in the vas efferens and the epididymis. On immunoblots of sperm extracts, ADAM-1 subunit appeared as a main reactive band of ~50-55 kDa corresponding to occurrence of different isoforms throughout the epididymal duct, especially in the corpus region where isoforms ranged from acidic to basic pI. In contrast, ADAM-2 was detected as several bands of ~90 kDa, ~75 kDa, ~50-55 kDa and ~40 kDa. The intensity of high molecular mass bands decreased progressively in the distal corpus where lower bands were also transiently observed, and only the ~40 kDa was observed in the cauda. The presence of bands of different molecular weights likely results from a proteolytic processing occurring mainly in the testis for ADAM-1, and also throughout the caput epididymis for ADAM-2. Immunolocalization showed that fertilin migrates from the acrosomal region to the acrosomal ridge during the sperm transit from the distal corpus to the proximal cauda. This migration is accompanied by an important change in the extractability of a part of ADAM-1 from the sperm membrane. This suggests that the fertilin surface migration may be triggered by the biochemical changes induced by the epididymal post-translational processing of both ADAM1 and ADAM-2. Different patterns of fertilin immunolocalization then define several populations of spermatozoa in the cauda epididymis. Characterization of such fertilin complex maturation patterns is an important step to develop fertility markers based on epididymal maturation of surface membrane proteins in domestic mammals.
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