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JIOMICS | VOL 5 | ISSUE 2 | DECEMBER 2015 | 1-62 JOURNAL OF INTEGRATED OMICS Journal of Integrated Omics A METHODOLOGICAL JOURNAL HTTP://WWW.JIOMICS.COM Special Issue: Proceeding Abstracts of the 4 th International Congress on Analytical Proteomics (ICAP 2015) One gene, many changes: a long history involving soybean Marco Aurélio Zezzi Arruda* 1,2 1 Spectrometry, Sample Preparation and Mechanization Group – GEPAM, 2 Institute of Science and Technology for Bioanalytics, Institute of Chemistry, Department of Analytical Chemistry, University of Campinas - Unicamp, PO Box 6154, 13803-970, Campinas, Brazil. *Corresponding author: zezzi@iqm.unicamp.br Available Online: 31 December 2015 Abstract Exogenous genes are successfully introduced into plants since the 80´s, and that one, which confer the resistance of the soybeans to glyphosate, the most used herbicide in the world, the first reported in the literature [1]. Since then, genetically modified organisms (GMOs) are being exponentially produced, so that 170 million hectares is nowadays related to crops engineered in at least 28 countries [2]. This fact not only reinforce the importance of such organisms, but also shows a good appeal to sustainability once that these GMOs produce enhanced characteristics such as high amount of fibers, proteins, are resistant to pests and/or insects, among others [2]. In this way, our research group is deeply interested in studying, since long time ago, the effects that a transgenic modification has on the proteome, the metabolome, the ionome, besides others of an organism [3-5], also evaluating different generations of plants. In this way, enzymatic evaluation, proteomics, and bioaccessibility will be presented for investigating some aspects regarding soybean [Glycine max (L.) Merril] seeds and plants. Platforms like 2-D DIGE, ICP-MS, and ESI-MS/MS will be presented, as well as some results regarding stress production and the cultivation of this culture in the presence of nanoparticles. Acknowledgements: FAPESP, CNPq, CAPES References: [1] Monsanto do Brasil. http://www.monsanto.com.br/produtos/sementes/ soja_roundup_ready/soja_round_ready.asp. [accessed at June, 24th, 2015] [2] Gilbert N. Nature 497(2013)21 [3] Mataveli, LVR, Fioramonte, M, Gozzo, FC, Arruda, MAZ. Metallomics 4(2012)373 [4] Barbosa HS, Arruda SCC, Azevedo RA, Arruda MAZ. Anal Bioanal Chem 402(2012)299. [5] Arruda SCC, Barbosa HS, Azevedo RA, Arruda MAZ. J Proteom, 93(2013)107 1-62: 1
JIOMICS | VOL 5 | ISSUE 2 | DECEMBER 2015 | 1-62 JOURNAL OF INTEGRATED OMICS Journal of Integrated Omics A METHODOLOGICAL JOURNAL HTTP://WWW.JIOMICS.COM Special Issue: Proceeding Abstracts of the 4 th International Congress on Analytical Proteomics (ICAP 2015) Proteomic profiling of neuromuscular disorders K. Ohlendieck*, S. Murphy, A. Holland Muscle Biology Laboratory, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland. *Corresponding author: kay.ohlendieck@nuim.ie Available Online: 31 December 2015 Abstract Purpose: Neuromuscular disorders are associated with a great variety of pathophysiological triggering mechanisms, including primary genetic defects, acquired autoimmune processes, traumatic tissue injury, drug-induced abnormalities, cytotoxic insults and disuse-related atrophy, as well as changes during natural aging. In order to establish robust biomarker signatures for developing improved diagnostic, prognostic and therapy-monitoring test systems that can differentiate between individual muscular diseases, systematic evaluations of proteome-wide changes in pathological muscle specimens have been carried out. Experimental description: Mass spectrometry-based proteomic profiling was used to compare skeletal muscle samples from normal versus pathological samples. Both, animal models of common neuromuscular disorders and human biopsy material was used in large-scale comparative studies. Subcellular fractionation procedures, fluorescence two-dimensional gel electrophoresis and/or liquid chromatography were employed for the efficient separation of the assessable muscle proteome. The independent verification of proteomic findings was carried out by enzyme assays, protein binding experiments, immunoblotting surveys and immunofluorescence microscopy. Results: The systematic profiling of pathological skeletal muscle specimens has resulted in the establishment of a variety of novel biomarker candidates for the detailed characterization of muscular dystrophy, motor neuron disease, myotonia, diabetes-associated muscle weakness and sarcopenia of old age. Identified proteins are associated with cellular signalling, ion homeostasis, excitation-contraction coupling, the contractile apparatus, the cytoskeleton, the extracellular matrix and the cellular stress response. Conclusions: The newly identified proteomic biomarker candidates can now be further characterized and tested for their suitability as diagnostic, prognostic and therapy-monitoring indicator molecules in the field of neuromuscular pathology. Keywords: biomarker, diabetes, motor neuron disease, muscular dystrophy, myotonia, sarcopenia of old age. Acknowledgements: Research was funded by the Irish Higher Education Authority, the Deutsche Duchenne Stiftung aktion benni & co e.V., Muscular Dystrophy Ireland and the Hume scholarship programme of Maynooth University. The Programme for Research in Third Level Institutions PRTLI Cycle 5 is co-funded by the Irish Government and the European Union under Ireland’s EU Structural Funds Programme 2007-2013. References: [1] Ohlendieck K. Proteomic identification of biomarkers of skeletal muscle disorders. Biomarkers in Medicine 2013;7:169-86. [2] Brinkmeier H, Ohlendieck K. Chaperoning heat shock proteins: proteomic analysis and relevance for normal and dystrophin-deficient muscle. Proteomics Clinical Applications 2014;8:875-95. [3] Holland A, Dowling P, Meleady P, Henry M, Zweyer M, Mundegar RR, Swandulla D, Ohlendieck K. Label-free mass spectrometric analysis of the mdx-4cv diaphragm identifies the matricellular protein periostin as a potential factor involved in dystrophinopathy-related fibrosis. Proteomics 2015 (in press). 1-62: 2
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Page 5 and 6: Biodiversity Research Center, Acade
Page 7 and 8: Belgium Bart De Spiegeleer Ghent Un
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Page 11 and 12: Veronica Mainini Dept. Health Scien
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