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10 results on '"Biomedical Proteomics Research Group (BPRG)"'

1. Nucleolin interacts with US11 protein of herpes simplex virus 1 and is involved in its trafficking

Author

Jean-Charles Sanchez, Philippe Bouvet, Loredana Arata, Xavier Gaume, Jean-Jacques Diaz, Eric Soler, Aleth Callé, Yohann Couté, Alberto L. Epstein, Anna Greco, Karine Monier, Sabine Hacot, Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Laboratoire Joliot Curie, École normale supérieure de Lyon (ENS de Lyon)-Centre National de la Recherche Scientifique (CNRS), Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Centre de génétique et de physiologie moléculaire et cellulaire ( CGPhiMC ), Centre National de la Recherche Scientifique ( CNRS ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon, École normale supérieure - Lyon ( ENS Lyon ) -Centre National de la Recherche Scientifique ( CNRS ), Biomedical Proteomics Research Group ( BPRG ), Centre de Recherche en Cancérologie de Lyon ( CRCL ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie Moléculaire de la Cellule ( LBMC ), École normale supérieure - Lyon ( ENS Lyon ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), École normale supérieure - Lyon (ENS Lyon)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
Nucleolus, MESH: Blotting, Far-Western, viruses, RNA-binding protein, Plasma protein binding, MESH : RNA, Small Interfering, MESH : Protein Transport, MESH: RNA, Small Interfering, RNA, Small Interfering, Nuclear protein, MESH : Viral Proteins, 0303 health sciences, integumentary system, 030302 biochemistry & molecular biology, RNA-Binding Proteins, MESH : Protein Binding, Virus-Cell Interactions, 3. Good health, Transport protein, Phosphoproteins/metabolism, Protein Transport, Protein Binding, MESH: Protein Transport, Immunoprecipitation, Viral Proteins/metabolism, Immunology, MESH : RNA-Binding Proteins, Biology, Blotting, Far-Western, Microbiology, MESH: Phosphoproteins, MESH : Immunoprecipitation, Viral Proteins, 03 medical and health sciences, Virology, Humans, MESH: Protein Binding, MESH : HeLa Cells, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Far-western blotting, MESH : Blotting, Far-Western, ddc:576, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: Humans, MESH: Immunoprecipitation, MESH : Humans, Phosphoproteins, Molecular biology, MESH: Viral Proteins, MESH: RNA-Binding Proteins, Insect Science, MESH: HeLa Cells, RNA-Binding Proteins/metabolism, MESH : Phosphoproteins, Nucleolin, HeLa Cells
Abstract

Herpes simplex virus type 1 (HSV-1) infection induces profound nucleolar modifications at the functional and organizational levels, including nucleolar invasion by several viral proteins. One of these proteins is US11, which exhibits several different functions and displays both cytoplasmic localization and clear nucleolar localization very similar to that of the major multifunctional nucleolar protein nucleolin. To determine whether US11 interacts with nucleolin, we purified US11 protein partners by coimmunoprecipitations using a tagged protein, Flag-US11. From extracts of cells expressing Flag-US11 protein, we copurified a protein of about 100 kDa that was further identified as nucleolin. In vitro studies have demonstrated that nucleolin interacts with US11 and that the C-terminal domain of US11, which is required for US11 nucleolar accumulation, is sufficient for interaction with nucleolin. This association was confirmed in HSV-1-infected cells. We found an increase in the nucleolar accumulation of US11 in nucleolin-depleted cells, thereby revealing that nucleolin could play a role in US11 nucleocytoplasmic trafficking through one-way directional transport out of the nucleolus. Since nucleolin is required for HSV-1 nuclear egress, the interaction of US11 with nucleolin may participate in the outcome of infection.

Published
2012
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2. Isolation of nucleoli

Author

Sabine Hacot, Hichem C. Mertani, Yohann Couté, Marie Alexandra Albaret, Jean-Charles Sanchez, Jean-Jacques Diaz, Stephane Belin, Manuel Rosa-Calatrava, Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Idéalp' Pharma, Idealp, Institut de biologie et chimie des protéines [Lyon] (IBCP), Virologie et Pathologie Humaine (VirPath), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de génétique et de physiologie moléculaire et cellulaire ( CGPhiMC ), Centre National de la Recherche Scientifique ( CNRS ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon, Biomedical Proteomics Research Group ( BPRG ), Institut de biologie et chimie des protéines [Lyon] ( IBCP ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Virologie et Pathologie Humaine ( VirPath ), École normale supérieure - Lyon ( ENS Lyon ) -Université Claude Bernard Lyon 1 ( UCBL ), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH : Cell Culture Techniques, Nucleolus, Cell Culture Techniques/*methods, Cell, Cell Culture Techniques, Ribosome biogenesis, Biology, Bioinformatics, MESH : Electrophoresis, Polyacrylamide Gel, Cell Fractionation, Viral infection, Cell Fractionation/*methods, medicine, Animals, Humans, MESH: Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, ddc:576, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Ribonucleoprotein, MESH: Cell Culture Techniques, MESH: Humans, MESH : Humans, General Medicine, Cell biology, medicine.anatomical_structure, MESH : Cell Fractionation, MESH : Cell Nucleolus, Cell Nucleolus/*chemistry, MESH: Cell Fractionation, Cellular Ageing, Electrophoresis, Polyacrylamide Gel/*methods, Electrophoresis, Polyacrylamide Gel, MESH : Animals, Cell fractionation, MESH: Cell Nucleolus, TRNA maturation, Cell Nucleolus, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; Nucleoli are now recognized as multi-functional nuclear domains involved in several fundamental cell processes such as ribosome biogenesis, regulation of the assembly of non-ribosomal ribonucleoprotein complexes, tRNA maturation, sequestration of protein, viral infection, and cellular ageing. Extensive proteomic analyses of these nucleolar domains after their purification have contributed to the description of their multiple biological functions. Because nucleoli are the largest and densest nuclear structures, they are easily amenable to purification from nuclei of cultured animal cells using the protocol described in this unit.

Published
2010
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3. Identification of human, rat and chicken ribosomal proteins by a combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry

Author

Laure Granger, Olivier Gandrillon, Anh Thu Nguyen-Lefebvre, Alexander Scherl, Patrizia Arboit, Jean-Charles Sanchez, Jean Jacques Madjar, Jean-Jacques Diaz, Sandrine Gonin-Giraud, Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Multi-scale modelling of cell dynamics : application to hematopoiesis (DRACULA), Institut Camille Jordan [Villeurbanne] (ICJ), École Centrale de Lyon (ECL), Université de Lyon-Université de Lyon-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Lyon (ECL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Institut Camille Jordan (ICJ), Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet - Saint-Étienne (UJM)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Lyon (ECL), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet - Saint-Étienne (UJM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Ribosomal Proteins, Electrophoresis, Gel, Two-Dimensional/methods, Databases, Factual, Biophysics, Biology, Trypsin/metabolism, Tandem mass spectrometry, Tandem mass tag, Mass spectrometry, Tandem Mass Spectrometry/methods, Biochemistry, 03 medical and health sciences, Ribosomal protein, Tandem Mass Spectrometry, medicine, Tumor Cells, Cultured, Animals, Humans, Electrophoresis, Gel, Two-Dimensional, Trypsin, ddc:576, Polyacrylamide gel electrophoresis, 030304 developmental biology, Gel electrophoresis, 0303 health sciences, Chromatography, Molecular mass, 030302 biochemistry & molecular biology, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Rats, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Ribosomal Proteins/analysis/chemistry/metabolism, Chickens, medicine.drug, HeLa Cells
Abstract

International audience; To identify the exact spot position of human, rat and chicken ribosomal proteins (RP) separated by two-dimensional polyacrylamide gel electrophoresis (2-DE), a 2-DE system was designed to separate RP with a pI>8.6 according to their charge in the first dimension and to their molecular mass in the second dimension. Individual proteins were excised from the gels and identified by mass spectrometry after digestion by trypsin. In addition, a mixture of purified RP from these three species was also analyzed by tandem mass tag spectrometry. By combining those two methods 74 RP from human, 76 from rat and 67 from chicken were identified according to the nomenclature initially defined for rat liver RP and by using the Swiss-Prot/trEMBL databases. Whereas human and rat RP were well described, most of RP from chicken were not characterized in databases, since 35 out of 67 chicken RP identified in this study were not listed yet. We propose here the first comprehensive description of chicken RP and their comparison to those from human and rat.

Published
2010
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4. Cardiac biomarkers levels predict pulmonary embolism extent on chest computed tomography and prognosis in non-massive pulmonary embolism

Author

F. Verschuren, Nicolas Vuilleumier, Damien Gruson, Noury Mensi, Marc Philip Righini, Arnaud Perrier, Grégoire Le Gal, Natacha Turck, Jean-Charles Sanchez, Denis F. Hochstrasser, Calvez, Ghislaine, Department of Pathology, Clinical Chemistry (NV - DPCC), Geneva University Hospital (HUG), Service de médecine interne générale (SMIG), Hôpital Universitaire de Genève, Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO), Centre d'Investigation Clinique (CIC - Brest), Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Protéomique Clinique, Service de Médecine de Laboratoire, HCUG, and Service d'angiologie et d'hémostase (MR)

Subjects
MESH: Pulmonary Embolism, Male, Computed tomography, 030204 cardiovascular system & hematology, Chest pain, MESH: Aged, 80 and over, 0302 clinical medicine, X ray computed, 030212 general & internal medicine, ComputingMilieux_MISCELLANEOUS, MESH: Treatment Outcome, ddc:616, MESH: Aged, Aged, 80 and over, Venous Thrombosis, MESH: Middle Aged, [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, medicine.diagnostic_test, MESH: Chest Pain, Follow up studies, MESH: Follow-Up Studies, Hematology, Middle Aged, Prognosis, Thrombosis, 3. Good health, Pulmonary embolism, Treatment Outcome, MESH: Dyspnea, Disease Progression, MESH: Disease Progression, Female, Radiology, medicine.symptom, MESH: Tomography, X-Ray Computed, MESH: Hemorrhage, Adult, medicine.medical_specialty, Chest Pain, MESH: Myocardium, Cardiac biomarkers, Hemorrhage, MESH: Anticoagulants, MESH: Prognosis, 03 medical and health sciences, medicine, Humans, ddc:576, Aged, MESH: Humans, business.industry, Myocardium, Disease progression, MESH: Biological Markers, Anticoagulants, MESH: Adult, medicine.disease, MESH: Male, Dyspnea, MESH: Venous Thrombosis, business, Pulmonary Embolism, Tomography, X-Ray Computed, MESH: Female, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, Biomarkers, Follow-Up Studies
Abstract

Cardiac biomarkers levels predict pulmonary embolism extent on chest computed tomography and prognosis in non-massive pulmonary embolism

Published
2009

5. Cardiac biomarkers for risk stratification in non-massive pulmonary embolism: a multicenter prospective study

Author

Jean-Charles Sanchez, Nicolas Vuilleumier, Natacha Turck, G. Le Gal, Arnaud Perrier, Thomas V. Perneger, Noury Mensi, Denis F. Hochstrasser, Marc Philip Righini, F. Verschuren, Henri Bounameaux, Division of Laboratory Medicine (DLM), Geneva University Hospital (HUG), Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO), Centre d'Investigation Clinique (CIC - Brest), Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM), Emergency Department (FV - ED), Saint Luc University Hospital, Service de médecine interne générale (SMIG), Hôpital Universitaire de Genève, Service d'angiologie et d'hémostase (MR), Biomedical Proteomic Research Group (BPRG), University Medical Centre of Geneva, Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, and Division of Clinical Epidemiology (DCE)

Subjects
MESH: Pulmonary Embolism, 030204 cardiovascular system & hematology, Chest pain, MESH: Risk Assessment, Gastroenterology, 0302 clinical medicine, Natriuretic Peptide, Brain, Odds Ratio, 030212 general & internal medicine, MESH: Natriuretic Peptide, Brain, Prospective Studies, Prospective cohort study, MESH: Peptide Fragments, ddc:616, Univariate analysis, MESH: Middle Aged, Area under the curve, Hematology, Middle Aged, Prognosis, Troponin/blood, Troponin, MESH: Predictive Value of Tests, 3. Good health, Pulmonary embolism, MESH: Young Adult, Predictive value of tests, Biological Markers, Female, medicine.symptom, Adult, medicine.medical_specialty, Adolescent, Fibrin Fibrinogen Degradation Products/analysis, Fatty Acid-Binding Proteins, MESH: Fatty Acid-Binding Proteins, Risk Assessment, MESH: Prognosis, Fibrin Fibrinogen Degradation Products, Pulmonary Embolism/*diagnosis, 03 medical and health sciences, Young Adult, Predictive Value of Tests, Internal medicine, medicine, MESH: Fibrin Fibrinogen Degradation Products, Humans, ddc:576, ddc:613, MESH: Adolescent, MESH: Humans, business.industry, MESH: Biological Markers, MESH: Adult, Odds ratio, medicine.disease, Peptide Fragments, Confidence interval, MESH: Prospective Studies, MESH: Odds Ratio, Surgery, MESH: Troponin, Natriuretic Peptide, Brain/blood, Pulmonary Embolism, business, Peptide Fragments/blood, MESH: Female, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, Fatty Acid-Binding Proteins/blood
Abstract

International audience; BACKGROUND: Troponins (cTnI and cTnT), N-terminal pro-Brain Natriuretic Peptide (NT-proBNP), myoglobin, heart-type fatty acid-binding protein (H-FABP) and fibrin D-Dimer are emergent candidates for risk stratification in pulmonary embolism (PE). OBJECTIVE: To compare the respective prognostic values of biomarker with non-massive PE to predict an adverse outcome at 3 months. PATIENTS/METHODS: One hundred and forty-six consecutive patients with non-massive PE were included in this multicenter prospective study. The combined outcome consisted of intensive care monitoring on admission, death or hospitalization attributable to either a PE-related complication [defined by PE/deep vein thrombosis (DVT) relapse or major bleeding under anticoagulation] or to dyspnoea with or without chest pain during follow-up. RESULTS: The outcome was met in 12% of patients. In univariate analysis, a NT-proBNP level above 300 pg/ml was the strongest predictor of unfavorable outcome with an odds ratio (OR) of 15.8 [95% confidence interval (CI): 2.05-122). ORs for the other variables were: 8.0 for D-dimer >2000 ng/ml (95% CI: 1.1-64), 4.7 for H-FABP >6 ng/ml (95% CI:1.5-14.8), 3.5 for cTnI >0.09 ng/ml (95% CI:1.2-9.7), 3.4 for myoglobin >70 ng/ml (95% CI:0.9-12.2). Receiver operating curve (ROC) analysis indicated that NT-proBNP was the best predictor [area under the curve (AUC) 0.84; 95%CI: 0.76-0.92; P < 0.0001] with a negative predictive value of 100% (95% CI: 91-100) at 300 pg/ml. At that cut-off, the true negative rate for NT-proBNP was 40%. In multivariate analysis, NT-proBNP was the only significant independent predictors. CONCLUSIONS: NT-proBNP appears to be a good risk stratification marker in identifying low-risk patients with non-massive PE who could be treated in an outpatient setting.

Published
2009
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6. EuPA achieves visibility - an activity report on the first three years

Author

Ole N. Jensen, Patricia M. Palagi, Luca Bini, C. Jimenez, Michael J. Dunn, Friedrich Lottspeich, Jean-Charles Sanchez, Peter James, Deborah Penque, Antony F. Quinn, Juan-Pablo Albar, Christine Hoogland, Thierry Rabilloud, H-J Kraus, Jesús V. Jorrín-Novo, Dimitrios Noukakis, Garry L. Corthals, Stephen R. Pennington, Fernando J. Corrales, C. Kleinhammer, Michael Fountoulakis, Concha Gil, Hannelore Meyer, Proteome Research Centre, UCD Conway Institute for Biomolecular and Biomedical Research, University College Dublin [Dublin] (UCD), Departamento de Microbiología [Madrid], Universidad Complutense de Madrid = Complutense University of Madrid [Madrid] (UCM), protein chemistry, Max-Planck-Institut, Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Proteomics facility, Centro Nacional de Biotecnología, Functional Proteomics Laboratory, Università degli Studi di Siena = University of Siena (UNISI), División de Hepatología y Terapia Génica, Universidad de Navarra, Proteomics Research Group, University of Turku, Roche Center for Medical Genomics, Hoffmann Laroche, Swiss Institute of Bioinformatics [Genève] (SIB), Department of Protein Technology, Lund University [Lund], Department of Biochemistry and Molecular Biology, University of Southern Denmark (SDU), OncoProteomics Laboratory, Dept. Medical Oncology, VU University Medical Center, Universiteit van Amsterdam (UvA), Bioquimica y Biologia Molecular, Universidad de Córdoba [Cordoba], Proteomics managing editor, Verlag Chemie Wiley, Functional Proteomics, Medizinisches Proteom-Center, Ruhr-Universität Bochum [Bochum], Marketing and Communication in Life Sciences, N! light, Laboratorio de Proteómica, Centro de Genética Humana, Instituto Nacional de Saùde Dr Ricardo Jorge [Portugal] (INSA), Biochimie et biophysique des systèmes intégrés (BBSI), Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF), Medical oncology laboratory, CCA - Disease profiling, Centro Nacional de Biotecnología [Madrid] (CNB-CSIC), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC)-Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Universidad de Córdoba = University of Córdoba [Córdoba], and Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Proteomics, Societies, Scientific, European level, Operations research, Educational material, Biophysics, Tutorials, Bioinformatics for Proteomics, Technology development, Courses, Biochemistry, History, 21st Century, 03 medical and health sciences, Proteomics journals, Time frame, European Proteomics Association, Education Committee, Courses, Workshops, EuPA meetings, Educational material, Tutorials, Summer School, Gel-based Proteomics, Chromatography-based Proteomics, Mass Spectrometry for Proteomics, Bioinformatics for Proteomics, Proteomics journals, Mass Spectrometry for Proteomics, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Political science, Chromatography-based Proteomics, ddc:576, Proteomics/education/organization & administration, 030304 developmental biology, EuPA meetings, 0303 health sciences, Education Committee, Gel-based Proteomics, business.industry, MESH: Proteomics, 030302 biochemistry & molecular biology, Visibility (geometry), Public relations, Societies, Scientific/history/*organization & administration/trends, MESH: Societies, Scientific, Europe, European Proteomics Association, Workshops, Organizational structure, Science policy, MESH: Europe, MESH: History, 21st Century, business, Summer School
Abstract

Udgivelsesdato: 2008-Apr-30 Plans for the European Proteomics Association (EuPA) were conceived and established during 2004 and 2005, and culminated in the formal inception of the organisation during the 4th HUPO World Congress held in Munich in 2005. The mission from the outset has been three-tiered and is to: i) strengthen the national Proteomics organizations in their efforts; ii) to co-ordinate and provide educational programs, and iii) to advance the networking of scientists through meetings, workshops and student exchange. Linked to the mission were objectives to emphasise the benefits and contributions of Proteomics to biological and industrial researchers, the general public and science policy makers in Europe. In addition, the EuPA set out to promote scientific exchange for all applications and technology development related to Proteomics, and coordinate joint activities of national Proteomics societies at the European level. To achieve these tasks an organisational structure was conceived whereby four Activity Committees (Conferences/Communications, Education, EuPA-HUPO-Interactions and Funding) were implemented and a General Council consisting of all member countries. The remarkable rise and progress the EuPA has achieved in this small time frame is reported here.

Published
2008
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7. ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis

Author

Régis Dieckmann, Jean-Charles Sanchez, Laurent Bezin, Jean-Jacques Diaz, Karine Kindbeiter, Laurent Duret, Yohann Couté, Stephane Belin, Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Idéalp' Pharma, Idealp, Bioinformatique, phylogénie et génomique évolutive (BPGE), Département PEGASE [LBBE] (PEGASE), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Physiologie intégrative, cellulaire et moléculaire (PICM), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)

Subjects
Exosome complex, Nucleolus, Exodeoxyribonucleases/chemistry/metabolism, Ribosome biogenesis, Biochemistry, Analytical Chemistry, Substrate Specificity, Mutant Proteins/metabolism, 0302 clinical medicine, Exoribonuclease, Large ribosomal subunit, RNA Precursors, RNA Precursors/metabolism, Phylogeny, Genetics, 0303 health sciences, Cell biology, Protein Transport, 030220 oncology & carcinogenesis, Vertebrates, Saccharomyces cerevisiae Proteins/genetics, Ribosomal Proteins/metabolism, Recombinant Fusion Proteins/metabolism, Exoribonuclease activity, Cell Nucleolus, Protein Binding, Ribosomal Proteins, [SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], Saccharomyces cerevisiae Proteins, Recombinant Fusion Proteins, Molecular Sequence Data, Biology, 03 medical and health sciences, Animals, Humans, Immunoprecipitation, Amino Acid Sequence, Gene Silencing, Ribosomes/metabolism, ddc:576, Molecular Biology, 030304 developmental biology, Computational Biology, RNA Ribosomal/metabolism, Cell Nucleolus/enzymology, Ribosomal RNA, Protein Structure, Tertiary, Protein Structure Tertiary, Exodeoxyribonucleases, RNA, Ribosomal, Hela Cells, Mutant Proteins, Ribosomes, Biogenesis, HeLa Cells
Abstract

International audience; Proteomic analyses of human nucleoli provided molecular bases for an understanding of the multiple functions fulfilled by these nuclear domains. However, the biological roles of about 100 of the identified proteins are unpredictable. The present article describes the functional characterization of one of these proteins, ISG20L2. We demonstrate that ISG20L2 is a 3' to 5' exoribonuclease involved in ribosome biogenesis at the level of 5.8S rRNA maturation, more specifically in the processing of the 12S pre-rRNA. The use of truncated forms of ISG20L2 demonstrated that its N-terminal half promotes the nucleolar localization and suggested that its C-terminal half bears the exoribonuclease activity. Identification of the binding partners of ISG20L2 confirms its involvement in the biogenesis of the large ribosomal subunit. These results strongly support the notion that, in human, as it was demonstrated in yeast, 5.8S rRNA maturation requires several proteins in addition to the exosome complex. Furthermore, this observation sustains greatly the idea that the extremely conserved need for correctly processed rRNAs in vertebrates and yeast are achieved by close but different mechanisms.

Published
2008
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8. Correlation between cardiac biomarkers and right ventricular enlargement on chest CT in non massive pulmonary embolism

Author

Nicolas Vuilleumier, Jean-Charles Sanchez, Denis F. Hochstrasser, Grégoire Le Gal, Noury Mensi, Antoine Rosset, Marc Philip Righini, Henri Bounameaux, Arnaud Perrier, Natacha Turck, Department of Pathology, Clinical Chemistry (NV - CPCC), Geneva University Hospital (HUG), Service d'angiologie et d'hémostase (MR), Hôpital Universitaire de Genève, Service de médecine interne générale (SMIG), Biomedical Proteomics Research Group (BPRG), Centre médical universitaire, Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO), Centre d'Investigation Clinique (CIC - Brest), Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM), Departement of Pathology, Clinical Chemistry (NV - CPCC), and Laboratoire de Protéomique Clinique, Service de Médecine de Laboratoire, HCUG

Subjects
Male, MESH: Pulmonary Embolism, Natriuretic Peptide Brain/blood, 030204 cardiovascular system & hematology, Muscle hypertrophy, 0302 clinical medicine, MESH: Aged, 80 and over, Natriuretic Peptide, Brain, Troponin I, Pulmonary Embolism/blood/radiography, Natriuretic peptide, 030212 general & internal medicine, Prospective Studies, MESH: Natriuretic Peptide, Brain, Prospective cohort study, MESH: Peptide Fragments, Aged, 80 and over, ddc:616, MESH: Aged, MESH: Middle Aged, Myoglobin, Myoglobin/blood, Respiratory disease, MESH: Hypertrophy, Right Ventricular, Hematology, Middle Aged, 3. Good health, Pulmonary embolism, Tomography Spiral Computed, Cardiology, Radiography, Thoracic, Biological Markers, Female, Adult, medicine.medical_specialty, MESH: Troponin I, MESH: Myoglobin, medicine.drug_class, Hypertrophy Right Ventricular/blood/radiography, 03 medical and health sciences, Internal medicine, medicine, Humans, ddc:576, Radiography Thoracic, Aged, MESH: Humans, Hypertrophy, Right Ventricular, business.industry, Vascular disease, MESH: Biological Markers, MESH: Adult, MESH: ROC Curve, MESH: Radiography, Thoracic, medicine.disease, Peptide Fragments, MESH: Prospective Studies, MESH: Male, Endocrinology, Aged 80 and over, ROC Curve, Heart-type fatty acid binding protein, MESH: Tomography, Spiral Computed, Pulmonary Embolism, business, Peptide Fragments/blood, Tomography, Spiral Computed, MESH: Female, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

International audience; BACKGROUND: Troponin I (cTnI), myoglobin, heart-type fatty acid binding protein (H-FABP), and natriuretic peptides (BNP, NTproBNP) were all reported to be elevated in patients with pulmonary embolism (PE). METHODS: To assess the correlation between the aforementioned markers and helical computed tomography (hCT) right ventricular dysfunction (RVD) in non massive PE, we performed this prospective pilot study on 50 patients. RESULTS: Patients with RVD had significant higher natriuretic peptides prevalence than cardiomyocytes damage-related markers (48% vs 20%, P=0.006). Significant prevalence differences were observed only for natriuretic peptides when patients with RVD and those without were compared (74% vs 33% for NT-pro BNP, P=0.005 and 65% vs 22% for BNP, P=0.003). Patients with RVD had significant higher biomarkers median plasmatic values than those without (BNP: 170 vs 36 pg/ml, P=0.0027; NT-proBNP: 1369 vs 170.7 pg/ml, P=0.0024; cTnI: 0.032 vs 0 ng/ml, P=0.0034; H-FABP: 4.32 vs 2.23 ng/ml, P=0.0032; myoglobin: 36.7 vs 28.2 ng/ml, P=0.03). Significant correlations were only obtained between RV/LV index and plasmatic natriuretic peptides (NT-proBNP: r=0.36, P=0.009; BNP r=0.28; P=0.047). CONCLUSIONS: Natriuretic peptides prevalence elevation and median values are significantly higher when RVD is present and significantly correlate with hCT RVD.

Published
2008
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9. Inhibition of insulin secretion by betagranin, an N-terminal chromogranin A fragment.

Author

Schmid GM, Meda P, Caille D, Wargent E, O'Dowd J, Hochstrasser DF, Cawthorne MA, and Sanchez JC

Subjects
Animals, Cell Line, Female, Glucose metabolism, Glucose pharmacology, Insulin Secretion, Islets of Langerhans ultrastructure, Mice, Potassium metabolism, Potassium pharmacology, Sweetening Agents pharmacology, Calcium Signaling drug effects, Chromogranins pharmacology, Insulin metabolism, Islets of Langerhans metabolism
Abstract

Betagranin, an N-terminal fragment of chromogranin A, results from a proteolytic processing, and is co-secreted with insulin. While other chromogranin A-derived peptides negatively modulate hormone secretion, the role of betagranin in pancreatic beta-cells is so far unknown. We have recently shown that pancreatic islet betagranin levels are down-regulated in obese, leptin-deficient mice. In the present study, we have investigated the distribution of betagranin in primary mouse islets and cells of the MIN6 line and have evaluated its effects on insulin secretion. We showed that betagranin co-localizes with insulin within secretory granules and strongly inhibited insulin secretion in response to both glucose and potassium, by blocking the influx of calcium. The data demonstrated a hitherto unknown inhibitory effect of betagranin on insulin secretion.

Published
2007
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10. Effect of high-fat diet on the expression of proteins in muscle, adipose tissues, and liver of C57BL/6 mice.

Author

Schmid GM, Converset V, Walter N, Sennitt MV, Leung KY, Byers H, Ward M, Hochstrasser DF, Cawthorne MA, and Sanchez JC

Subjects
Animals, Biomarkers, Electrophoresis, Gel, Two-Dimensional, Glucose Tolerance Test, Humans, Insulin Resistance physiology, Mass Spectrometry, Mice, Mice, Inbred C57BL, Models, Biological, Obesity metabolism, Adipose Tissue metabolism, Dietary Fats metabolism, Liver metabolism, Muscle, Skeletal metabolism
Abstract

In the present study, the effect of a high fat diet on the expression of proteins in insulin target tissues was analyzed using a proteomic approach. Gastrocnemius muscle, white and brown adipose tissue, and liver were taken from C57BL/6 mice either fed on a high-fat or a chow diet. Expression levels of approximately 10 000 polypeptides for all the four tissues were assessed by two-dimensional gel electrophoresis (2-DE). Computer-assisted image analysis allowed the detection of 50 significantly (p < 0.05) differentially expressed proteins between obese and lean mice. Interestingly, more than half of these proteins were detected in the brown adipose tissue. The differentially expressed proteins were identified by tandem mass spectrometry. Several stress and redox proteins were modulated in response to the high-fat diet. A key glycolytic enzyme was found to be downregulated in adipose tissues and muscle, suggesting that at elevated plasma fatty acid concentrations, fatty acids compete with glucose as an oxidative fuel source. Furthermore, in brown adipose tissue there were significant changes in mitochondrial enzymes involved in the Krebs tricarboxylic acid (TCA) cycle and in the respiratory chain in response to the high-fat diet. The brown adipose tissue is an energy-dissipating tissue. Our data suggest that the high-fat diet treated mice were increasing energy expenditure to defend against weight gain.

Published
2004
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