Day 1 :
KTH-Royal Institute of Technology
Time : 09:40-10:05
Peter Nilsson is a Professor in Proteomics at the SciLifeLab Stockholm, KTH-Royal Institute of Technology. Since 2002, he has been heading the Protein Microarray Technology group within the Human Protein Atlas project. He is the Executive Platform Director of Affinity Proteomics at SciLifeLab and the Site Director of the Human Protein Atlas at SciLifeLab Stockholm. He is also the Vice Dean of the School of Biotechnology at KTH. The main research focus is within development and utilization of various protein microarray technologies for peptide, antigen and antibody based proteomic profiling and biomarker discovery.
The Human Protein Atlas currently contains more than 24.000 validated antibodies targeting 17000 proteins corresponding to approximately 83% of the encoded human proteins. The publicly available portal contains several million high-resolution images generated by immunohistochemistry on tissue microarrays and confocal microscopy for subcellular localization. The antibodies are antigen-purified and the long-term objective is to generate paired antibodies towards all human protein targets. A systematic biomarker discovery approach has been implemented utilizing array-based platforms and the massive antigen and antibody production pipeline as well as whole proteome ultra-high-density peptide microarrays. Proteomic profiling of serum, plasma and CSF in multi-disease cohorts are performed with large number of peptides and antigens on planar microarrays for the analysis of autoimmunity repertoires with subsequent verifications with on suspension bead arrays. Furthermore, large set of samples are also profiled with massive numbers of antibodies on highly multi-parallel suspension bead arrays which utilizes magnetic color-coded beads functionalized with antibodies to generate protein profiles from labeled samples for biomarker discovery. The results from both autoimmunity and antibody-based neuroproteomic profiling utilizing both platforms will be presented within the context of multiple sclerosis, ALS, Alzheimer’s disease, Parkinson’s disease, narcolepsy as well as various psychiatric disorders.
University of Palermo
Time : 10:05-10:30
Ida Pucci Minafra is the Director of the Research Centre “Centro di Oncobiologia Speimentale” affiliated to the University of Palermo and operating at the “La Maddalena” Cancer Center. She has been Full Professor of Cytology and Histology, Director of the Dipartimento di Oncologia e Applicazioni Cliniche (University of Palermo), President of the Società Italiana per lo Studio del Connettivo. She has been Visiting Researcher/Visiting Professor at several Institutions among which the City University of New York, the Institut de Biologie et Chimie des Protéines of Lyone, the Hebrew University of Jerusalem. She has more than 75 publications and has been Editorial Board Member of reputed journals.
Despite the extensive progress on the omics strategies realized in the last decade, the 2D procedure followed by spot excision and Mass spectrometric identification remains one of the best method to obtain a reliable quali-quantitative proteomic portrait of a cell. In recent years, our research group has collected and cryo-preserved a large number of surgical fragments from patients operated for breast cancer with the intention of generating proteomic biomarkers potentially useful for clinical applications. In this presentation we report some data obtained by the analysis of 120 tissue samples of breast cancers. To correct for the known heterogeneity of breast cancer tissues due to variations in cellular contents versus stromal proteins, the expression levels of individual protein spots were normalized to the actin content. The protein spots identity was assessed by mass spectrometry and when necessary immunologically validated. To date we have identified about 400 proteins including isoforms which were classified into 14 major functional groups. Among these, “ubiquitous” and “sporadic” proteins were observed. A major portion of ubiquitous proteins expressed at high levels in the majority of patients belong to the group of glycolytic enzymes. Among the sporadic proteins which were absent or present at very low levels in many patients and highly expressed in others were some proteins of the motility group of the heat shock machinery and some S100 proteins. We suggest that some of these proteins represent potentially useful biomarkers for sub-classification of breast cancers and follow up of patients.