3 results on '"Duban-Deweer, Sophie"'
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2. Gel electrophoresis of human sperm: a simple method for evaluating sperm protein quality
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Buee Luc, Sigala Julien, Mitchell Valérie, Fernandez-Gomez Francisco-Jose, Jumeau Fanny, Béhal Hélène, Sergeant Nicolas, Eddarkaoui Sabiha, Duban-Deweer Sophie, Gamétogenèse et Qualité du Gamète - ULR 4308 (GQG), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université de Lille, and Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)
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0301 basic medicine ,endocrine system ,Electrophorèse unidimensionnelle ,Urology ,education ,Motility ,Sperm protein ,Biology ,Flagellum ,World health ,Andrology ,03 medical and health sciences ,0302 clinical medicine ,Fibrous sheath ,Sperme ,Sperm motility ,health care economics and organizations ,reproductive and urinary physiology ,Gel electrophoresis ,lcsh:R5-920 ,030219 obstetrics & reproductive medicine ,Gaine fibreuse ,urogenital system ,Correction ,[SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology ,Sperm ,030104 developmental biology ,Reproductive Medicine ,One-dimensional PAGE ,lcsh:Medicine (General) ,Research Article - Abstract
Background The limitations of conventional sperm analyses have highlighted the need for additional means of evaluating sperm quality. Methods In a study of a cohort of 245 men with known conventional sperm parameters, one-dimensional PAGE was used to monitor protein content and quality in samples from individual ejaculates. Results The sperm protein content varied markedly from sample to another, especially in the high-molecular-weight range. The intensity of the 80–110 kDa bands was correlated with progressive motility (r = 0.15, p = 0.015) and was significantly higher (p = 0.0367) in the group of men with conventional parameters above the World Health Organization’s 2010 reference values than in the group with at least one subnormal parameter (i.e. semen volume, sperm concentration, sperm count per ejaculate, progressive motility, proportion of normal forms or multiple anomaly index below the lower reference value). Using mass spectrometry, the 80–110 kDa bands were found to correspond primarily to three proteins from the flagellum’s fibrous sheath: A-kinase anchor protein 4, A-kinase anchor protein 3, and spermatogenic cell-specific type 1 hexokinase. Conclusion One-dimensional PAGE constitutes a simple, rapid, reliable, inexpensive method for analyzing proteins associated with sperm motility in individual human ejaculates.
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- 2018
3. An Optimized Fluorescence-Based Bidimensional Immunoproteomic Approach for Accurate Screening of Autoantibodies
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Dutoit-Lefèvre, Virginie, Dubucquoi, Sylvain, Launay, David, Sobanski, Vincent, Dussart, Patricia, Chafey, Philippe, Broussard, Cédric, Duban-Deweer, Sophie, Vermersch, Patrick, Prin, Lionel, Lefranc, Didier, Inflammation: mécanismes et régulation et interactions avec la nutrition et les candidoses, Université de Lille, Droit et Santé-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Immunologie (EA 2686), Université de Lille, Droit et Santé, Centre de Biologie Pathologie et Génétique, Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut d'Immunologie [CHRU Lille], Pôle de Biologie Pathologie Génétique [CHU Lille], Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Pôle de Biologie Pathologie Génétique [CHU Lille], Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Service de Médecine Interne et d'Immunologie clinique, Centre National de Référence Maladies rares-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Plateforme protéomique 3P5 [Institut Cochin] (3P5), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Physiopathologie de la Barrière Hémato-Encéphalique (LBHE), Université d'Artois (UA), Service de neurologie D, This study was funded in part by‘Action deRecherche Concertée d’Initiative Régionale’(ARCirno. 09.26.0082), Programme Hospitalier deRecherche Clinique (PHRC no. 2008/1926), theassociations'Max de Vie, Max d’Amour' and'Capucine', the Société Nationale Française deMédecine Interne, Pfizer and Merck Serono. the manuscript., Université de Lille, Droit et Santé-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Laboratoire d'Immunologie ( EA 2686 ), Centre Hospitalier Régional Universitaire [Lille] ( CHRU Lille ) -Institut d'Immunologie, Centre National de Référence Maladies rares-Centre Hospitalier Régional Universitaire [Lille] ( CHRU Lille ), Plateforme protéomique 3P5 [Institut Cochin] ( 3P5 ), Institut Cochin ( UM3 (UMR 8104 / U1016) ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Physiopathologie de la Barrière Hémato-Encéphalique ( LBHE ), Université d'Artois ( UA ), Centre Hospitalier Régional Universitaire [Lille] ( CHRU Lille ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé, Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Bos, Mireille
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Proteomics ,Blotting, Western ,lcsh:Medicine ,Autoantigens ,Two-Dimensional Difference Gel Electrophoresis ,Mice ,Image Processing, Computer-Assisted ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Animals ,Humans ,Lupus Erythematosus, Systemic ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,lcsh:Science ,[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Autoantibodies ,Fluorescent Dyes ,lcsh:R ,Antibodies, Monoclonal ,Hep G2 Cells ,Carbocyanines ,Molecular Weight ,Immunoglobulin G ,Luminescent Measurements ,lcsh:Q ,Isoelectric Focusing ,Research Article - Abstract
International audience; Serological proteome analysis (SERPA) combines classical proteomic technology with effective separation of cellular protein extracts on two-dimensional gel electrophoresis, western blotting, and identification of the antigenic spot of interest by mass spectrometry. A critical point is related to the antigenic target characterization by mass spectrometry, which depends on the accuracy of the matching of antigenic reactivities on the protein spots during the 2D immunoproteomic procedures. The superimposition, based essentially on visual criteria of antigenic and protein spots, remains the major limitation of SERPA. The introduction of fluorescent dyes in proteomic strategies, commonly known as 2D-DIGE (differential in-gel electrophoresis), has boosted the qualitative capabilities of 2D electrophoresis. Based on this 2D-DIGE strategy, we have improved the conventional SERPA by developing a new and entirely fluorescence-based bi-dimensional immunoproteomic (FBIP) analysis, performed with three fluorescent dyes. To optimize the alignment of the different antigenic maps, we introduced a landmark map composed of a combination of specific antibodies. This methodological development allows simultaneous revelation of the antigenic, landmark and proteomic maps on each immunoblot. A computer-assisted process using commercially available software automatically leads to the superimposition of the different maps, ensuring accurate localization of antigenic spots of interest.
- Published
- 2015
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