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VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
http://icim.marseille.inserm.fr/proteomique
17 Juin 2015
IPC - CRCM - Marseille
Découverte de Biomarqueurs et analyse globale. Modifications Post-Traductionelles. Protéomique ciblée.
Cancer & Protéomique
Du protéome global au ciblé
Nos soutiens académiques
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
Organisation
Plateforme protéomique CRCM-IPC
Directeur Jean-Paul Borg
Comité local d’organisation :
Audebert Stéphane
Borg Jean-Paul Camoin Luc
Fourquet Patrick Granjeaud Samuel Pophillat Matthieu
Avec le soutien de Michel Baccini; Françoise Birg; François Coulier ; Valérie Depraetère; Laurence Duvivier; Amandine Gazull; Laurence
Laloum ; Claude Roux et Patrice Viens.
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
Sommaire
Programme 5 Résumé des conférences Découverte de biomarqueurs et analyse globale. - Christophe Masselon, BGE, Grenoble 9 - Ellen Van-Obberghen, IBV, Nice 11
Modifications post-traductionnelles. - Philippe Soubeyran, CRCM, Marseille 15 - Serge Urbach, FPP, Montpellier 17
Protéomique ciblée. - Bruno Domon, LCP, Luxembourg 21 - Christine Carapito, LSMBO, Strasbourg 23 - Damarys Loew, Institut Curie, Paris 25 - Frédéric Lopez, CRCT, Toulouse 27
Fournisseurs - Yannick Surroca, Expedeon 30 - Eric Niedo, Bio-Rad 31 - Thierry Legoupil, Shimadzu 33 Liste des inscrits. 35
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
17 Juin 2015
IPC - CRCM - Marseille
Cancer & Protéomique Du protéome global au ciblé
8h00 Accueil.
9h00 Séance d’ouverture. Jean-Paul BORG
9h15 Découverte de Biomarqueurs et analyse globale. - 9h15-10h00 « Discovery and Evaluation of Urothelial Bladder Cancer Protein Biomarker Candidates in Urine » Christophe MASSELON - 10h00-10h45 « Matrisome of Cancer-Associated Fibroblasts in Head and Neck Squamous Cell Carcinoma » Ellen VAN-OBBERGHEN
Pause et visite des stands fournisseurs.
11h15 Modifications Post-Traductionnelles. - 11h15-12h00 « Rôles de l'ubiquitine et des ubiquitine-likes dans les mécanismes de résistance aux traitements anticancéreux » Philippe SOUBEYRAN - 12h00-12h45 « Use of Quantitative phosphoproteomics to decipher SRC oncogenic signalling » Serge URBACH
12h45 Pause déjeuner.
14h00 Séance fournisseurs. - 14h00– 14h15 « Gelfree® 8100 Fractionation System » Yannick SURROCA - Expedeon - 14h15-14h30 « Couplage BIA-MS pour l’identification d’un ITAF (IRES transacting factor) du VEGF-D » Frédéric LOPEZ - CRCT - 14h30-14h45 « Electrophorèse et Normalisation des Western blots » Eric NIEDO - Bio-Rad
14h45 Protéomique ciblée. - 14h45-15h30 « New Approaches in Quantitative Proteomics » Bruno DOMON
Pause et visite des stands fournisseurs.
- 16h00-16h45 « Targeted proteomics using LC-SRM platforms to precisely quantify proteins in complex biological samples » Christine CARAPITO - 16h45-17h30 « L’analyse des tumeurs par haute résolution : de la recherche à la clinique » Damarys LOEW - 17h30-17h45 « Nouvelle solution de collection de plasma et son impact sur les dosages cliniques en LC-MS/MS » Thierry LEGOUPIL- Shimadzu - 17h45-18h00 «Glycoproteomics : getting ready for the next analytical challenge in Life Science » Pierre-Olivier SCHMIT - Bruker
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
Cancer & Protéomique
Du protéome global au ciblé
Résumés des présentations
Christophe Masselon Laboratoire d’Etude de la Dynamique des
Protéomes, CEA Grenoble, France
Discovery and Evaluation of Urothelial Bladder
Cancer Protein Biomarker Candidates in Urine High throughput proteomics measurements enable comparisons of clinical samples from
large populations of patients and controls. This represents a formidable opportunity for the discovery of early diagnostic or prognostic biomarkers, i.e. molecular indicators of a
pathological state or its probable evolution that are present before the onset of specific clinical symptoms. New challenges lie in the integration of these technologies in the
discovery and the evaluation of novel biomarkers, to translate initial findings into manageable lists of candidates for the purpose of designing new clinical assays. The
DECanBio project (EU-FP7) aimed at (i) developing reliable analytical protocols and strategies for the generation of robust quantitative proteomics data, (ii) using them for the
discovery and evaluation of new candidate biomarkers of bladder cancer in urine. Among available technologies for biomarkers discovery, two methods emerged with a
high potential for integration: the Accurate Mass and retention Time (AMT) tag proteomics method used for global sample profiling [1] and the Selected Reaction Monitoring SRM approach used for targeted candidate evaluation [2]. Importantly, both
methods relied on the same sample type and standardized preparation method [3]. Using the AMT tag approach on a 98 patients cohort (cancer vs. healthy controls), among 1180
monitored proteins, statistical analysis yielded a list of 97 candidates. SRM was used to evaluate a selection of 134 candidates originating in part from our AMT results, but also
from literature mining, from another 2DE study on the same cohort and from a separate transcriptomics screen on bladder tumors biopsies. This evaluation entailed estimation of
differential concentrations of these candidates in 121 urine samples from cancer patients and control patients with a suspicion of bladder cancer that had been cleared by
pathological examination. Among the 134 screened candidates, 108 could be accurately monitored in urine, and 71 showed potential for diagnosis or prognosis of bladder cancer
incidence or recurrence. References [1] Pasa-Tolic et al. Proteomic analyses using an accurate mass and time tag strategy. Biotechniques vol. 37 (2004), 621-624
[2] Lange et al. Selected reaction monitoring for quantitative proteomics: a tutorial. Molecular Systems Biology vol. 4 (2008) 222-235
[3] M. Court et al. Toward a standardized urine proteome analysis methodology. Proteomics vol 11 (2011) 1160-1171
Ellen Van Obberghen-Schilling Institute of Biology Valrose
CNRS UMR7277 – INSERM U1091
University of Nice-Sophia Antipolis, France
Matrisome of Cancer-Associated Fibroblasts in Head and
Neck Squamous Cell Carcinoma For a tumor to develop and spread, the growth-repressive environment of the host tissue
must undergo significant changes. These changes include dramatic modifications in the
molecular composition and architecture of the extracellular matrix (ECM), including de
novo expression of matrix proteins that participate in tissue morphogenesis during
embryonic development. For the past few years our laboratory has been investigating the
functional interplay between tumor cells and their matrix microenvironment in head and
neck squamous cell carcinomas (HNSCC). The tumor ECM is largely synthesized and
modulated by carcinoma-associated fibroblasts. Therefore, we set up a pseudo-3D culture
model that recapitulates several key features of the tumor matrix in vivo. In this model
carcinoma cells are plated on decellularized fibrillar matrices produced by fibroblasts
isolated from patient tumors. An MS-based proteomics approach (adapted from 1) was
used to provide a detailed portrait of the proteins present in the CAF-derived matrisome.
Fibronectin (FN) was found to be the major matrisomal component produced by CAFs
isolated from two independent tumors, followed by Tenascin C, Emilin-1 and the 1-3
subunits of collagen VI (2). The FN isoforms overexpressed in tumors, referred to as
“oncofetal” variants, harbor alternatively spliced exons encoding extra FN type III repeats.
Immunoprofiling of human tumors confirmed that FN is largely synthesized and
assembled by stromal cells and revealed that overexpression of FN in human tumors
(n=436) correlates with poor prognosis and higher locoregional recurrence. Interactions
between FN and two of its receptors, identified as key molecular determinants of the
tumor-stroma dialog in HNSCC, will be discussed. A better understanding of ECM
signatures of human tumors will be essential for the development of clinically relevant
tools to block disease progression.
References [1] Naba A, Clauser KR, Hoersch S, Liu H, Carr SA, Hynes RO. The matrisome: in silico definition and
in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol Cell Proteomics.
2012 Apr;11(4):M111.014647.
[2] Veracini, L, Gopal, S, Grall, D, Butori, C, Beghelli-de la Forest Divonne, S, Audebert, S, Camoin, L,
Radwanska, A, Schaub, S, Violette, SM, Weinreb, PH, Sudaka, A, Hofman, P and Van Obberghen-
Schilling, E. Stromal fibronectin promotes migration of carcinoma cohorts and paracrine TGF- signaling
through αvβ6 and α9β1 integrins in head and neck cancer. (in preparation)
Philippe SOUBEYRAN Equipe Stress Cellulaire, CRCM, Marseille,
France
Rôles de l'ubiquitine et des ubiquitine-likes dans les
mécanismes de résistance aux traitements anticancéreux.
Le cancer du pancréas est tellement agressif qu'il peut être considéré comme un modèle
d'étude de l'acquisition de la résistance aux traitements anticancéreux par les cellules
tumorales [1]. A l'heure actuelle, seule la Gemcitabine peut, dans certains cas, améliorer la
survie des patients. Notre but est d'identifier de nouveaux mécanismes de résistance
expliquant ce phénotype si particulier.
Or, ces mécanismes font intervenir des voies cellulaires de réponse au stress dont le
déclenchement et la transduction des signaux sont assurés par des modifications post-
traductionnelles (MPTs) de nombreuses protéines impliquées. Les MPTs par les protéines
de la famille de l'ubiquitine (ubiquitine, SUMOs, Nedd8, etc...) sont à présent reconnues
pour être impliquées dans la régulation de la plupart des processus biologiques d’une
cellule normale, et les exemples d'altérations de ce système associées aux pathologies
comme le cancer se multiplient [2].
Nous tentons donc d'identifier les altérations de ce type de MPTs qui sont impliquées dans
la résistance des cellules cancéreuses pancréatiques. Pour cela, nous avons établis les
variations de l’ubiquitine, Nedd8 et SUMO1 (modifomes) de la lignée cellulaire
MiaPaCa2 induites par la Gemcitabine [3]. Nous avons montré que le traitement altère les
MPTs de plusieurs voies et nombreuses protéines impliquées dans des fonctions cellulaires
majeurs. Nous avons poursuivi ce travail par l'étude des profiles de MPTs de la même
lignée cellulaire rendue résistante à de fortes doses de Gemcitabine. Nous avons ainsi mis
en évidence un remaniement important de partie importante du modifome de la cellule
cancéreuse lorsque celle-ci acquière de façon permanente le phénotype résistant.
References [1] A. Jemal et al., Cancer statistics. CA Cancer J Clin 60 (2010) 277.
[2] M. Hochstrasser, Origin and function of ubiquitin-like proteins. Nature 458 (2009) 422.
[3] T. Bonacci et al., Identification of New Mechanisms of Cellular Response to Chemotherapy by
Tracking Changes in Post-Translational Modifications by Ubiquitin and Ubiquitin-Like Proteins. J
Proteome Res 13 (2014) 2478.
Serge Urbach Functional Proteomics Platform, IGF, CNRS
UMR5203, France
Use of Quantitative phosphoproteomics to decipher SRC
oncogenic signalling SRC, a non-receptor tyrosine kinase (TK), is a critical regulator of signal transduction
induced by a large variety of cell-surface receptors. When deregulated, SRC shows strong
oncogenic activity, probably due to its capacity to regulate downstream signalling even in
absence of extracellular stimuli. Accordingly, SRC is frequently deregulated in human
cancer and may play important roles during tumorigenesis. However, knowledge on the
molecular mechanism by which SRC controls signalling remains incomplete.
This talk is focused on the use of MS-based proteomic approaches to decipher how SRC
and its downs tream substrates interact and transmit oncogenic signals, resulting in cell
tumorigenicity and invasiveness (for review see 1). Stable Isotope Labelling by Amino
acids in Cell culture (SILAC) based quantitative proteomics allow the identification of the
whole spectrum of TK substrates and the dynamic of phosphorylation events involved in
oncogenic signaling.
In a first instance, we used SILAC combined to phospho-tyrosine immunoprecipitation, in
colorectal cancer (CRC) cells. In this context (SRC overexpression in SW620 cells), we
showed that SRC phosphorylates a cluster of tyrosine-kinases that are essential for
promoting CRC tumorigenicity and invasiveness (2).
Next, we wanted to validate the relevance of this SRC signature in vivo by using a novel
SILAC approach dedicated to the analysis of experimental tumours obtained by
xenografting nude mice with human CRC cells (3). We could highlight the complexity of
SRC oncogenic signalling, as most of the targets identified in vivo (i.e. 60%) were not
found by in vitro analysis, demonstrating a significant difference between SRC signalling
in tumours and in cell culture.
This work result from a collaboration between FPP and Serge Roche’s research group
(Tyrosine kinase signalling and oncogenesis, CRBM, CNRS UMR5237, UM)
References 1: Sirvent A et al., Contribution of phosphoproteomics in understanding SRC signaling in normal and
tumor cells, Proteomics 15 (2015) 232-44.
2: Leroy C et al., Quantitative phosphoproteomics reveals a cluster of tyrosine kinases that mediates SRC
invasive activity in advanced colon carcinoma cells. Cancer Res. 69 (2009) 2279-86. 3: Sirvent A et al., Analysis of SRC oncogenic signaling in colorectal cancer by stable isotope labeling
with heavy amino acids in mouse xenografts, Mol Cell Proteomics 11 (2012) 1937-50.
Bruno Domon Luxembourg Clinical Proteomics Center, LIH,
Luxembourg
New Approaches in Quantitative Proteomics
Targeted quantitative proteomics studies are gradually shifting from low resolution
selected reaction monitoring (SRM) to high resolution parallel reaction monitoring (PRM)
methods, using quadrupole orbitrap instruments.
A new data acquisition scheme, called internal standard triggered-PRM (IS-PRM), has
recently been introduced to use internal standards not only to perform quantification by
isotope dilution but also to drive PRM acquisition. The approach was refined to carry out
quantitative screens for cancer drug response markers or to follow pathways.
The analyses were performed on a quadrupole-orbitrap instrument (Q-Exactive HF,
Thermo Scientific). Internal standards were synthetized and mixed at defined
concentrations. Spectral libraries of reference synthetic peptides were created. The IS-
PRM application was developed using the instrument programming interface (API).
A new PRM workflow for quantitative analyses was developed. The acquisition method
taking into account the m/z values and elution times of the precursors relies on the on-the-
fly detection of the internal standards added to the samples; this to drive in real-time the
measurement of endogenous peptides by optimizing the acquisition parameters. The
creation of spectral libraries using synthetic peptides is an essential element of the
approach as it is use to identify the analytes when they elute. The data processing method,
also based on the spectral library was used to confirm identity and qualify fragments. The
relevant traces were uploaded to Skyline to perform the quantification while reducing the
volume of data.
A proof-of-principle of IS-PRM was performed to precisely quantify in plasma samples
100 endogenous peptides representing 50 candidate protein markers of lung cancer drug
response. In addition, it was applied to monitor the MAPK, WnT and mTOR signaling
pathways in lysates of lung cancer cell lines.
A complete automated solution was established to design, execute and, process data of
PRM experiments; it was applied to systematic quantify peptides in biological and clinical
samples.
Christine Carapito Laboratoire de Spectrométrie de Masse BioOrganique,
Institut Pluridisciplinaire Hubert Curien, UMR 7178,
CNRS, Université de Strasbourg, Strasbourg, France
Targeted proteomics using LC-SRM platforms to precisely quantify proteins in
complex biological samples
Targeted proteomics via selected reaction monitoring (SRM) mass spectrometry has
recently emerged as an ideal complement to shotgun approaches. With its large dynamic
range, low limit of detection, high reproducibility, high multiplexing capacity and
exquisite quantitative accuracy, targeted proteomics is best suited for studies requiring the
consistent quantification of a predefined set of proteins across many samples. This is
especially the case in the biomarker verification/validation phases where robust
quantification assays are needed to measure candidate biomarkers on large sample cohorts.
A technical description of the possibilities and limitations of quantitative LC-SRM
analysis with the key steps of the development of an SRM assay will be presented. Then,
examples of applications will be detailed with a special focus on biomarker studies and in
particular on lymphoma biomarkers.
References [1] Schnell, G., et al, Discovery and targeted proteomics on cutaneous biopsies infected by Borrelia to
investigate Lyme disease, Mol Cell Proteomics, (2015), Epub ahead of print.
[2] Juste, C., et al, Bacterial protein signals are associated with Crohn's disease, Gut 63(10), (2014), 1566-
1577.
[3] Plumel, M.I., et al, Mass spectrometry-based sequencing and SRM-based quantitation of two novel
vitellogenin isoforms in the leatherback sea turtle (Dermochelys coriacea), J Proteome Res 12(9), (2013),
4122-35.
[4] Miguet, L., et al., Cell-surface expression of the TLR homolog CD180 in circulating cells from
splenic and nodal marginal zone lymphomas, Leukemia 27(8), (2013), 1748-50.
LOEW Damarys LSMP, Institut Curie, Paris France
L’analyse des tumeurs par haute résolution : de la
recherche à la clinique Le LSMP est une plateforme technologique qui accompagne depuis une dizaine d’années
les chercheurs de l’Institut Curie dans leurs études protéomiques à grande échelle. Avec
l’arrivée des techniques de spectrométrie de masse à haute résolution et le développement
de nouvelles méthodes (HRMS, SWATH[1]…), il est désormais possible d’identifier et de
quantifier presque toutes les protéines présentes dans un échantillon. Ses capacités, alliant
vitesse, spécificité, précision quantitative, reproductibilité, large gamme dynamique et
interrogation rétrospective in silico, pourraient modifier notre implication dans la
recherche générale et surtout dans les problématiques médicales de lutte contre le cancer.
Le LSMP a renouvelé son parc technique en 2014 et acquis successivement l’Orbitrap
Fusion puis l’ABSciex 6600 dans l’objectif de pouvoir également traiter des échantillons
cliniques, qui sont uniques en leur genre, limités et non renouvelables. Les échantillons de
tissus prélevés lors d’une biopsie ne permettent d’effectuer qu’un nombre très limité
d’analyses. Nous présenterons les différentes approches utilisées pour acquérir des
informations sur ces échantillons afin de pouvoir répondre aux cliniciens qui cherchent :
- à identifier des bio-marqueurs spécifiques à des sous-groupes tumoraux ou
- à identifier des protéines qui pourraient être ciblées par des traitements
thérapeutiques.
Après digestion enzymatique des échantillons tumoraux, les mélanges peptidiques sont
analysés par une approche super-SILAC et DDA (data-dependent acquisition). Différentes
méthodes de fractionnement ou d’enrichissement des peptides phosphorylés ont été
testées. Nous avons ensuite créé une base de données de spectres de fragmentation pour
pouvoir vérifier les apports d’une approche label free et DIA (data-independent
acquisition) pour l’analyse de ce type d’échantillon.
Reference(s) [1] Gillet LC, Navarro P, Tate S, Röst H, Selevsek N, Reiter L, Bonner R, Aebersold R. Targeted data
extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent
and accurate proteome analysis. Mol Cell Proteomics. 2012 Jun;11(6):O111.016717. doi:
10.1074/mcp.O111.016717.
Noak / Le Bar Floréal / Institut Curie
Yannick SURROCA
Expedeon France Sales Executive
Gelfree® 8100 Fractionation System: a powerful tool for
proteomics studies -
Recent advances and perspectives
In proteomics mass spectrometry analysis, protein mixtures are so complex that
thelow abundant proteins, the main ones of interest, are lost among the highly abundant
signals. Excising protein bands from preparative slab gels can result in little or noprotein.
Hence, effective fractionation of complex samples for in-depth proteomicanalysis by mass
spectrometry is critical.
GELFrEE is Gel Elution Liquid Fraction Entrapment Electrophoresis. The Gelfree8100
fractionation system enables molecular weight-based fractionation of intact proteins into
liquid-phase fractions. Gelfree bypasses both the low recovery of proteins and extensive
workup steps before mass spectrometry.
Up to eight samples are run in parallel using a programmable control module. The system
separates proteins by their molecular weight. Gelfree 8100 provides robust fractionation
over the mass range 3.5 kDa – 500 kDa.
Nowadays GELFrEE 8100 enhances Bottom-Up analysis by simplifying and reducing the
dynamic range of complex protein mixtures.
GELFrEE 8100 enables Top-Down proteomics approaches by fractionating and
recovering intact proteins. Isolate intact proteins can be then analysed for variants, post-
translational modifications and alterations.
Frédéric Lopez Groupe protéomique, CRCT,
Toulouse, France
Invité sur l’initiative de GE Healthcare
Couplage BIA-MS pour l’identification d’un ITAF (IRES
transacting factor) du VEGF-D
VEGF-D promotes tumor metastases by inducing lymphangiogenesis and lymphatic
vasculature dilatation. In this study, we demonstrated the molecular mechanisms involved
in VEGF-D-induced lymphatic dilatation. We identified a stress-induced translational
regulation of VEGF-D expression through an IRES activation under increased temperature
conditions. We showed that VEGF-D IRES activity was dependent of prostaglandin
pathway as non steroidal anti-inflammatory drugs are able to abolish the IRES-promoted
VEGF-D protein synthesis, and lymphatic vessels dilatation. Using plasmon surface
resonance on biotinylated VEGF-D mRNA coupled to mass spectrometry, we identified
the IRES transacting factor (ITAF), the Nucleolin, that allows the recruitment of the
ribosome to promote VEGF-D translational initiation thanks to a relocalization into the
cytoplasm.
Eric Niedochodowiez
National Product Specialist: Imaging & µPlates
Regional Product Specialist: Protein Electrophoresis and Transfert
Electrophorèse et Normalisation des Western blots
Les Gels StainFree permettent une visualisation sans coloration des protéines,
coloration affectant la structure des tryptophanes et toujours présente après transfert.
Cela va permettre une approche plus solide en terme de normalisation des "western blots"
car les approches à partir des "housekeeping" protéines soulèvent de plus en plus de
questions.
Cette normalisation sur protéines totales s'inscrit dans un flux technique maîtrisé allant de
la séparation à la révélation.
La présentation se calera sur le temps d'un transfert "Turbo", soit 10 minutes, pour vous
expliquer ce "workflow"...
Thierry LEGOUPIL
SHIMADZU France
Responsable Développement Biotech & Techniques MS
Nouvelle solution de collection de plasma et son impact sur
les dosages cliniques en LC-MS/MS
Pierre-Oliver Schmit
Proteomics market area manager
Bruker Daltonics LSC
Glycoproteomics : getting ready for the next analytical challenge
in Life Science
Protein glycosylation is a process involved in many major biological events, like cell
recognition, cell adhesion, immune and inflammatory reactions and many others. It can be
influenced by various factors like sex, age, and tissue type or health status. This makes
glycoproteins highly relevant compounds to focus on when it comes to the search for
candidate biomarkers or candidate therapeutic targets.
Mass spectrometry, on the other hand, is one of the most sensitive and powerful approach
to detect, identify and characterize glycoproteins. However, the limited ionization
efficiency, and the combinatorial nature of glycoconjugates, makes it difficult to get a
fully informative fragmentation pattern and complicates its analysis. These challenges
have to be addressed in order to target glycoproteins as potential candidate biomarkers.
In this talk we will describe how we deal with these obstacles when using the latest
proteomics analysis solution based on the Impact II UHR-Q-TOF. A special focus will be
made on glycopeptide analysis and on the solutions which have been developed to
increase their ionization efficiency, to obtain meaningful MS/MS in an LC timescale and
to facilitate their analysis while using dedicated bioinformatics tools. These features will
be illustrated with application examples.
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
Cancer & Protéomique
Du protéome global au ciblé
Liste des participants
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
A ARMSTRONG Nicholas URMITE [email protected] AUDEBERT Stéphane CRCM [email protected] B BAILLY Eric CRCM [email protected] BARTHEZ Marine IBDM [email protected] BAUDELET Emilie CRCM [email protected] BELGHAZI Maya CRN2M [email protected] BELLEMIN Patrick BIORAD [email protected] BOGARD Philippe Proteomics consult [email protected] BOGARD Chantal Proteomics consult BOTTOLLA Anne-Lyse GE Healthcare [email protected] BOUCHAIDI Ahmed PIT2 [email protected] BOYER Jean-baptiste CRCM [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
BRES Anne-Sophie GE Healthcare [email protected] BRUSCHI Mireille IMM-CNRS [email protected] BUHOT-ROCHE Blandine GE Healthcare [email protected] C CAMOIN Luc CRCM [email protected] CARAPITO Christine LSMBO [email protected] CARTIER-MICHAUD Amandine CRCM [email protected] D DAULAT Avais CRCM [email protected] DE SEPULVEDA Paulo CRCM [email protected] DEBAYLE Delphine IPMC [email protected] DECLOQUEMENT Philippe URMITE [email protected] DEHE Pierre-Marie CRCM [email protected] DERVIAUX Carine CRCM [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
DOMON Bruno LCP [email protected] F FERRACCI Geraldine CRN2M [email protected] FLAUDROPS Christophe URMITE [email protected] FOURQUET Patrick CRCM [email protected] FRANDON Isabelle Euromedex [email protected] FRELON Sandrine IRSN [email protected] G GAILLARD Pierre-Henri CRCM [email protected] GAY Anne-Sophie IPMC-CNRS [email protected] GENETTE Alexandre Galderma R&D [email protected] GONTERO MEUNIER Brigitte BIP2 [email protected] GUERIN Mathilde CRCM [email protected] GUIGONIS Jean-Marie Faculté de Médecine Nice [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
K KATSOGIANNOU Maria CRCM [email protected] KHANTANE Sabrina ThermoFisher SCIENTIFIC [email protected] L LAFFET Gilbert galderma R&D [email protected] Launay Hélène CRCM [email protected] Lebrun Régine IMM-CNRS [email protected] LEGOUPIL Thierry SHIMADZU [email protected] LEQUEUE Charlotte CRCM [email protected] LOEW Damarys Institut CURIE [email protected] LOPEZ Frédéric CRCT [email protected] M MABROUK Kamel ICR [email protected] MANSUELLE Pascal IMM-CNRS [email protected] MARFISI Claude Bruker [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
MAROC Nicolas IVD Dev consulting [email protected] MASSELON Christophe BGE [email protected] MASSEY-HARROCHE Dominique IBDM [email protected] MEHUL Bruno Galderma [email protected] MIGNOT Florian Promega France [email protected] MOAL Stéphane ThermoFisher SCIENTIFIC [email protected] N NIEDO Eric BIORAD [email protected] NUNES Jacques CRCM [email protected] P POPHILLAT Matthieu CRCM [email protected] PUPPO Rémy IMM-CNRS [email protected] PUVIRAJESSINGHE Tania CRCM [email protected] PYR dit Ruys Sébastien IRSN [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
R RESCH Sylvain SHIMADZU [email protected] RONCAGALLI Romain CIML [email protected] S SALOMON Thierry Protein Simple [email protected] SAURIN Andy IBDM [email protected] SCAGLIONE Sarah CRCM [email protected] SCHEMBRI Thérèse FACULTE PHARMACIE PIT2 [email protected] SIROIT Christophe Waters [email protected] SOUBEYRAN Philippe CRCM philippe,soubeyran@inserm,fr SURROCA Yannick EXPEDEON [email protected] T TAHA Mohammed CRCM [email protected] TAKEDACHI Arato CRCM [email protected] TOIRON YVES IPC/CRCM [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
U URBACH Serge FPP [email protected] V VALDEOLIVAS Alberto IML [email protected] VAN-OBBERGHEN Ellen IBV [email protected] VERDIER-PINARD Pascal CRCM [email protected] Z ZANZONI Andreas
TAGC [email protected]
VIIème Rencontre du réseau des plates-formes
protéomiques
de la région Provence Alpes Côte d’Azur
17 Juin 2015
IPC - CRCM - Marseille