cancer & protéomiqueicim.marseille.inserm.fr/img/pdf/proteopaca_2015_livret.pdf · university...

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


protéomiques


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.


protéomiques


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


protéomiques


17 Juin 2015


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


protéomiques




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.


protéomiques




Liste des participants


protéomiques


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]


protéomiques


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]


protéomiques


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]


protéomiques


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]


protéomiques


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]


protéomiques


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]


protéomiques


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]


protéomiques


17 Juin 2015


cancer & protéomiqueicim.marseille.inserm.fr/img/pdf/proteopaca_2015_livret.pdf · university...

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