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GLYCO 21 XXI International Symposium on Glycoconjugates Abstracts August 21-26, 2011 Vienna, Austria Glycoconj J (2011) 28: 197–36 9 Organising Committee Erika Staudacher (Austria) Leopold März (Austria) Günter Allmaier (Austria) Lothar Brecker (Austria) Josef Glössl (Austria) Hanspeter Kählig (Austria) Paul Kosma (Austria) Lukas Mach (Austria) Paul Messner (Austria) Walther Schmid (Austria) Igor Tvaroška (Slovakia) Reinhard Vlasak (Austria) Iain Wilson (Austria) Scientifi c Program Committee Iain Wilson (Austria) Paul Messner (Austria) Günter Allmaier (Austria) Reginald Bittner (Austria) Paul Kosma (Austria) Eva Stöger (Austria) Graham Warren (Austria) John Hanover (USA; nominated by the Society for Glycobiology) Kelly ten Hagen (USA; nominated by the Society for Glycobiology) supported in abstract selection by Michael Duchêne (Austria) Catherine Merry (UK) Tadashi Suzuki (Japan) Abstracts of the 21st International Symposium on Glycoconjugates The International Glycoconjugate Organisation Gerald W. Hart, President Leopold März, President-elect Paul Gleeson, Immediate Past-president Sandro Sonnino, Secretary Thierry Hennet, Treasurer National Representatives Pedro Bonay (Spain) to replace Angelo Reglero Nicolai Bovin (Russia) Jin Won Cho (Korea) Henrik Clausen (Denmark) Anne Dell (UK) Jukka Finne (Finland) Paul Gleeson (Australia) Jianxin Gu (China) Gerald Hart (USA) Thierry Hennet (Switzerland) Jim Jamieson (Canada) Gordan Lauc (Croatia) Hakon Leffl er (Sweden) Jean-Claude Michalski (France) Werner Reutter (Germany) Sandro Sonnino (Italy) Avadhesha Surolia (India) Ken Kitajima (Japan) Maciej Ugorski (Poland) Johannes F.G. Vliegenthart (The Netherlands) Iain Wilson (Austria) to replace Leopold März Albert M. Wu (Taiwan) Lode Wyns (Belgium) Yehiel Zick (Israel) Glycoconj J (2011) 28: 197–369 Past Presidents Eugene. A. Davidson (USA) Alan B. Foster (UK) Paul Gleeson (Australia) Mary Catherine Glick (USA) Colin Hughes (UK) Roger W. Jeanloz (USA) Akira Kobata (Japan) Jerzy Koscielak (Poland) Bengt Lindberg (Sweden) Jean Montreuil (France) Jürgen Roth (Switzerland) Harry Schachter (Canada) Roland Schauer (Germany) Nathan Sharon (Israel) Avadhesha Surolia (India) Guido Tettamanti (Italy) Johannes F.G. Vliegenthart (The Netherlands) Tamio Yamakawa (Japan) Abstracts of the 21st International Symposium on Glycoconjugates 201 International Glycoconjugate Organisation Award 2011 Professor Jeffrey ESKO Jeffrey D. ESKO, Ph.D., M.D. (h.c) is a Professor of Cellular and Molecular Medicine (cmm.ucsd.edu) and Co-Director of the Glycobiology Research and Training Center (grtc.ucsd.edu) at the University of California, San Diego. Dr. Esko received his Ph.D. in Biochemistry at the University of Wisconsin in Madison. After an independent fellowship at the Molecular Biology Institute at the University of California, Los Angeles, he moved to the University of Alabama at Birmingham and then to Department of Cellular and Molecular Medicine at the University of California, San Diego in 1996 to help build a program in Glycobiology. Work in his laboratory focuses on the structure, biosynthesis, and function of proteoglycans, including structural studies of heparan sulphate by mass spectrometry, application of genome-wide methods to identify genes involved in heparan sulphate assembly and lysosomal turnover, analysis of guanidinylated glycosides that act as molecular transporters, studies of proteoglycans in lipoprotein metabolism, and analysis of proteoglycans in modulating vascular permeability (eskolab.ucsd.edu). His work is supported by grants from the National Institutes of Health and the private sector. Dr. Esko has served on the numerous editorial boards and scientifi c boards and is currently on the board for Journal of Cell Biology and as an Associate Editor for Glycobiology. He was past President of the Society for Glycobiology, past Director of the Biomedical Sciences Graduate Program at UCSD (biomedsci.ucsd.edu), and he cofounded Zacharon Pharmaceuticals, Inc (www.zacharon.com). His work has been recognized by the Karl Meyer Award, the highest honor from the Society for Glycobiology, a MERIT Award from the National Institutes of Health, and an honorary degree from the University of Uppsala. In 2011, he is the recipient of the International Glycoconjugate Organisation Award. Gerald W. Hart The Johns Hopkins University, School of Medicine, Baltimore, USA 202 Glycoconj J (2011) 28: 197–369 Plenary Lectures The structure, analysis and biochemistry of carbohydrates were matters of much scientifi c prominence in the fi rst half of the 20th century, garnering several Nobel prizes 001: Heparan sulfate proteoglycans as receptors and and attracting much attention to their roles in metabolism, coreceptors (IGO Award Lecture) cell wall structure, cell surface antigens and microbe-host interactions. The International Symposium on J.D. Esko; Department of Cellular and Molecular Glycoconjugates was a natural outcome of such exciting Medicine, University of California, San Diego, La Jolla/ discoveries. However, the development of viable lectin- CA/US resistant animal cell lines with major defects in [email protected] glycosylation raised questions about whether complex glycans had specifi c functions intrinsic to the vertebrate Heparan sulfate proteoglycans (HSPGs) are glycoproteins, organism itself. The discovery of the Ashwell receptor in with the defi ning characteristic of containing one or more 1969 and specifi c effects of heparin on antithrombin covalently attached heparan sulfate (HS) chains, a type of provided indirect evidence that complex glycans might glycosaminoglycan (GAG). Cells elaborate a relatively carry out such functions. While many complex glycan small set of HSPGs (~17), which show strong conservation biosynthetic pathways were also being elegantly worked through evolution. Much of the early work in the fi eld out, there still remained no direct proof that glycans played concentrated on composition (size, chain number, and intrinsic biological roles within vertebrate systems. As a structure of the HS chains), biosynthesis, and binding trainee, I was fortunate to play a small part in the discovery properties, which led to a large list of potentially relevant by Kornfeld, Von Figura and others about 3 decades ago, ligands and interactions. In 1985, the fi rst somatic cell that mannose 6-phosphate residues on lysosomal enzymes mutants altered in HSPG expression were identifi ed, appeared critical for targeting of newly synthesized which allowed functional studies in the context of a cell enzymes to the lysosome. This proposed biological role culture model. A decade later, the fi rst HSPG mutants in a was confi rmed by the elucidation of human genetic model organism (Drosophila melanogaster) were diseases in which the pathway was affected. The following identifi ed, which was followed by identifi cation of mutants decades have provided a fl ood of information regarding in nematodes, tree frogs, zebrafi sh, and mice. A particularly other biological roles of glycans in vertebrate systems, interesting area of concentration concerns the biological and the suggestion that “all of the theories are correct, but function of rare modifi cations of heparan sulfate. exceptions to each can be found” has proven correct. I will Biochemical and genetic approaches are underway to provide an outline of this historical overview and then identify novel ligands and genes involved in positioning focus on examples of specifi c biological roles of sialic of sulfate groups along the chain. Other studies focus on acids intrinsic to vertebrates, including their contribution the action of cell surface HSPGs as coreceptors, in to selectin ligands, to neuronal stability and plasticity, and particular their capacity to dock with signaling receptors to the recognition of self by the Siglec family of sialic that modulate vascular biology. HSPGs also act as acid-recognizing Ig-like lectins. Finally, I will discuss adsorptive endocytic receptors, resulting in uptake of multiple changes to sialic acid biology during human bound ligands. For example, hepatic HSPGs mediate the evolution and the potential implications for human clearance of triglyceride-rich lipoprotein remnants, diseases. working in parallel with members of the LDL receptor family. When HSPGs enter the cell, they undergo lysosomal catabolism. Defects in enzymes involved in 003: Regulation of spermatogenesis by complex heparan sulfate turnover result in mucopolysaccharidoses N-glycans (Company of Biologists Lecture) (MPS) characterized by lysosomal storage and profound developmental and physiological effects. Efforts are H.-H. Huang, F. Batista, P. Stanley; Cell Biology, Albert underway to improve diagnosis and therapy for MPS Einstein College Medicine, New York/US based on diagnostic carbohydrate biomarkers and [email protected] techniques to exploit HSPGs turnover for delivery of lysosomal enzymes to cells. In database searches to identify novel glycosyltransferase genes we discovered NM_026233.2 that encodes a physiological inhibitor of N-acetylglucosaminyl- 002: Biological roles of vertebrate glycans: a look back transferase I (GlcNAcT-I or Mgat1). We termed this over the decades activity GlcNAcT-I Inhibitory Protein (GnT1IP). When expressed in cultured cells, membrane-anchored GnT1IP A. Varki; Glycobiology Research and Training Center, inhibits GlcNAcT-I activity but not other glycosyl- Medicine & Cellular and Molecular Medicine, Center for transferases such as GlcNAcT-III or galactosyltransferases. Academic
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