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Agenda
Day One - Thursday 5 November 2009
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08:00 |
Registration |
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Arrays |
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09:00 |
Keynote Presentation
Applications of Profiling the Autoantibody Repertoire – overview of biomedical and diagnostic applications
Dolores Cahill, Professor, University College Dublin
High content protein and antibody arrays have applications in biomedical and large scale research. Recent results of profiling the antibody repertoire in cancer and auto-immune diseases will be presented, including their biomedical and clinical relevance. |
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09:30 |
Synthesis of High Complexity Peptide Arrays for Proteome Research
Thomas Felgenhauer, Scientist, German Cancer Research Center
A new technique for the combinatorial synthesis of high complexity peptide arrays is presented. Many applications in proteome research which were restricted in former times by availability and high costs are now feasible. |
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10:00 |
Study of Anti-glycan Autoantibodies Induction in Colorectal Cancer Using a Tumour Glycan Microarray
Manfred Wuhrer, Associate Professor, Leiden University Medical School
Cell-surface glycans are known to be target of an anti-tumour humoral response. In order to systematically this response in colorectal cancer, glycoproteins as well as glycolipids were extracted from cancer tissue. N-glycans and glycolipid-linked glycans were enzymatically released, labeled with the fluorescent tag 2-aminobenzoic acid, and fractionated by HPLC. Using a microarray printer, nanoliter aliquots of all glycan fractions were printed onto epoxide-activated glass slides, resulting in a natural glycan microarray of more than 1000 glycan fractions spotted in triplicate. Microarrays were incubated with cancer patient sera, and anti-glycan IgG and IgM were detected using fluorescently labeled secondary antibodies. An induction of various anti-glycolipid antibodies was demonstrated with development of colorectal cancer. The target glycolipid glycans are currently being structurally elucidated and may represent anti-cancer vaccine candidates. The diagnostic and prognostic potential of the antibody responses is being evaluated. |
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10:30 |
Coffee Break and Networking in the Exhibition Hall
compliments of  |
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11:15 |
Proteomics as a Tool to Investigate Metabolic Modulations in the Energy-producing Pathways in Lactic Acid Bacteria
Enrica Pessione, Professor, University of Torino
The study of microbial metabolism through comparative proteomics (detection of enzymes expressed in a stimulated versus a control condition) has proved to be an effective approach to investigate the modulation of energy producing routes in Lactic acid Bacteria, pathways of great importance in food science and in basic research. |
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11:45 |
In Search of New Biomarkers for Pancreatic Cancer - Proteomic Approaches
Cristiana Tanase, Head of Biochemistry/Proteomics Department, "Victor Babes" National Institute of Pathology
This study identified molecules, especially new serum proteins, that can be biomarkers candidates useful in the early detection of pancreatic cancer. Novel technology could delineate molecular targets for innovative therapy in pancreatic cancer. |
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12:15 |
Lunch and Networking in the Exhibition Hall
compliments of
Free Workshop:Biological Mass Spectrometry and Proteomics
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13:30 |
Poster Session |
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Proteomics in Biomarker Discovery |
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14:30 |
Two-Dimensional Liquid Chromatography Coupled With Esi-Ms For Protein Identification And Quantification
Keith R Compson, Proteomics Business Manager, Waters Corporation, Manchester UK
Mass spectrometry is widely accepted as an essential tool to better understand protein function, facilitating both the identification and quantification of proteins in complex samples. Mass spectrometry based protein identification strategies have previously been described that facilitate the simultaneous acquisition of qualitative and quantitative information, in a data independent fashion.
We have extended this approach to generate precise relative quantification values for proteins contained in biological systems, and have constructed protein abundance curves for specific tissues, cell lysates and bio-fluids. |
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15:00 |
Insight Into Novel Proteomic Biomarkers as Host Defense Mechanism Against Infection and Fetal Damage in Pregnancies Complicated by Preterm Birth
Catalin Buhimschi, Assistant Professor, Yale University
Amniotic fluid proteomic biomarkers characteristic of inflammation are associated with and an increased fetal inflammatory status. In such clinical scenarios particularities of the fetal immune response to infection appear to cause pathology unique to the premature fetus that act synergistically with microbial insult to induce damage. |
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15:30 |
Coffee Break and Networking in the Exhibition Hall
compliments of |
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16:00 |
Biomarkers of Thoracic Aortic Aneurysms: Biofluid Analysis with a Novel Platform
John E. Wiktorowicz, Associate Professor/Director of Proteomics, University of Texas Medical Branch
Candidate cytokine and protein and peptide biomarkers in conditioned media that differentiate normals from stable and acute thoracic aortic aneurysms were identified using a novel biofluids separation strategy. Pathway analysis was used to establish their biological relevance to the disease. |
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16:30 |
Plasma Proteome Profiling Reveals Biomarker Patterns Associated with Prognosis and Therapy Selection in Glioblastoma Multiforme Patients
Christer Wingren, Associate Professor, Lund University
A high-content proteome screening tool, based on recombinant antibody microarrays, will be presented using gliblastoma multiforme as case study. |
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17:00 |
Drinks Reception
compliments of |
Day Two - Friday 6 November 2009
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Free Workshop: Combining the precision of LaserMicrodissection with the sensitivity of Nano-immunoassays and Two-dimensional Gel Electrophoresis in Biomarker Discovery
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09:30 |
Keynote Presentation
Strategies for Quantitative Proteomics
Rob Beynon, Professor, Proteomics and Functional Genomics Group, University of Liverpool
Proteomics is now maturing into a discipline that requires statistically defendable, quantitative data streams. This lecture will discuss strategies for quantitative proteomics, emphasising an optimal solution based on overlapping different approaches. |
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10:00 |
Proteome Signatures of Breast Cancer, or how to Find Essential Needles in a Haystack of Data
Serhiy Souchelnytskyi, Head of Laboratory, Karolinska Institute
We develop tools to find common features of proteome changes related to the carcinogenesis, and not to sample origin. This required use of systems biology tools. This is an efficient way to extract clinically relevant data from proteomics data. |
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10:30 |
Coffee Break and Networking in the Exhibition Hall
compliments of |
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11:15 |
Peptide Ligand Libraries as a Mean to Reduce Dynamic Concentration Range and Reach Low-Abundance Proteins
Egisto Boschetti, Research Director, Bio-Rad
The use of peptide libraries will be presented as a mean to enhance and identify low-abundance proteins from biological extracts. The properties of peptide libraries, their mechanism of action as well as experimental conditions of capture and elution will be described. Several examples will be given, from biological fluids (serum, urine, bile, CSF) and of cell lysates (platelets, red blood cells). |
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11:45 |
Indexing and Retrieval of Multiple 3D Protein Structure Representations for the Protein Data Bank
Eric Paquet, Senior Research Officer, National Research Council
We present a system that describes and retrieves similar proteins based on their three-dimensional shapes. The system performs an exhaustive search in the 50 000+ entries of Protein Data Bank, in less than a second. |
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12:15 |
Lunch and Networking in the Exhibition Hall
compliments of |
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13:30 |
Poster Session |
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14:30 |
New Orbitrap MS Technology and its Application to Proteomics
Madalina Oppermann
The impact of the continuing development of mass spectrometry generally in recent decades and orbitrap technology specifically in the last 4 years to the analytical sciences can hardly be overstated. The most recent developments in the design of the LTQ Orbitrap have resulted in huge improvements in the performance of the mass spectrometer when applied to the analysis of complex, biological samples. These improvements include the new dual pressure linear ion trap cell with both high and low pressure regions allowing much increased speed of data acquisition and the replacement of the tube lens and skimmer with an S-lens apparatus resulting in 5 to 10x increase in signal in the mass spectrometer without concomitant increase in noise. In addition a new combination c-trap-axial field HCD cell has replaced the older c-trap and HCD cell assemblies resulting in faster, more sensitive HCD. These combined developments allow for increased depth of analysis in complex samples having a broad range of analyte concentrations.The technological improvements to the design of the linear ion trap and orbitrap will be discussed and their subsequent effect on mass spectrometric performance. |
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15:00 |
Immobilized native membrane proteins - Probing solvent exposed domains through enzymatic digestion
Anders Karlsson, CSO, Nanoxis AB
LPI (lipid-based protein immobilization) technology enables immobilization of native membrane proteins on a solid support inside a flow cell. By applying different enzymatic digestion protocols one can probe the solvent exposed domains or perform epitope mapping of the immobilized native membrane proteins. Results indicate that adding a second step of protease treatment on a previously digested sample gives more protein sequence coverage and an increased number of confident protein identifications. Peptides emanating from digestion of native membrane proteins may also be used as linear epitopes for antibody production. A case study will be presented where the localization of a target membrane protein was determined by immunogold-EM studies. |
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15:30 |
Coffee Break and Networking in the Exhibition Hall
compliments of |
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16:00 |
Quantitative Proteome Analysis of Slow and Fast Skeletal Muscle Tissue Using in vivo SILAC
Marcus Krueger, Group Leader, Max-Planck Inst. for Heart and Lung Research
This technique was used to analyze protein levels of slow soleus and fast extensor digitorum longus (EDL) muscle isolated from the lower leg of the mouse hind limb. By mixing lysine-6 labelled soleus with non labelled EDL we were able to quantify more than 2500 proteins. Of the identified proteins approx. 500 proteins were detected with a differential expression pattern between Soleus and EDL, including, Myosins, SERCAs and troponins. Moreover, bioinformatics analysis revealed regulated proteins involved in contraction, ion homeostasis, glycolysis, and oxidation. Our finding demonstrates substantial differences between slow and fast muscles in the mouse and uncovers several novel marker proteins to specify type I and II muscle fibers. Thus, the SILAC-mouse is applicable to study protein changes in vivo. |
| 16.30 |
Family Reunion - Encounter of Molecular Cousins Uncovers Trace to Founder of Prion Protein Gene Family
Gerold Schmitt-Ulms, Assistant Professor, University of Toronto
A simple hypothesis is presented which accounts for the majority of interactions observed and suggests that PrPC organizes its molecular environment on account of its ability to bind to adhesion molecules harbouring immunoglobulin-like domains, which in turn recognize oligomannose-bearing membrane proteins. Our data further explain structural and functional features found within mammalian prion proteins as elements of an ancient involvement in the transport of divalent cations. The connection to ZIP proteins is expected to open new avenues to elucidate the biology of the prion protein in health and disease. |
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17:00 |
Close of Conference | |