Functional and Structural Proteomics of Glycoproteins
It has been predicted that nearly half of all human proteins are glycosylated indicating the significance of glycoproteins in human health and disease. For example, the glycans attached to proteins have emerged as important biomarkers in the diagnosis of
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Raymond J. Owens · Joanne E. Nettleship Editors
Functional and Structural Proteomics of Glycoproteins
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Editors Raymond J. Owens Oxford Protein Production Facility-UK University of Oxford The Research Complex at Harwell R92 Rutherford Appleton Laboratory Harwell Science and Innovation Campus Oxfordshire OX11 0FA UK [email protected]
Joanne E. Nettleship Oxford Protein Production Facility-UK University of Oxford The Research Complex at Harwell R92 Rutherford Appleton Laboratory Harwell Science and Innovation Campus Oxfordshire OX11 0FA UK [email protected]
ISBN 978-90-481-9354-7 e-ISBN 978-90-481-9355-4 DOI 10.1007/978-90-481-9355-4 Springer Dordrecht Heidelberg London New York © Springer Science+Business Media B.V. 2011 No part of this work may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording or otherwise, without written permission from the Publisher, with the exception of any material supplied specifically for the purpose of being entered and executed on a computer system, for exclusive use by the purchaser of the work. Printed on acid-free paper Springer is part of Springer Science+Business Media (www.springer.com)
Preface
Large-scale sequencing of the human and other mammalian genomes has created an enormous database of protein sequences for functional and structural analyses. It has been predicted that nearly half of all human proteins are glycosylated indicating the functional importance of glycoproteins in human health and disease. However, the study of glycoproteins presents major challenges. Unlike nucleic acid and amino acid sequences, the glycans attached to proteins are not directly coded for by a template. Rather, they are the result of a complex processing mechanism which acts on proteins destined for the cell surface either to be secreted or retained in the membrane. The glycans attached to proteins are no longer regarded as a byproduct of biosynthesis but are functionally significant in their own right. Importantly, these glycans have emerged as biomarkers in the diagnosis of human diseases such as cancers and play a significant role in the mechanisms by which pathogenic viruses gain entry into human cells. Manipulation of the glycosylation patterns of therapeutic antibodies has led to improvements in their mechanism of action which may ultimately translate into increased clinical efficacy. In the last few years, technology developments, in particular, advances in high throughput separation methods and detection techniques, have accelerated the characterization of the glycosylation patterns of cells and tissues. The use of lectin microarrays coupled to highly sensitive fluorescence-based detection systems has enabled the rapid profiling of glycan expression. Structural analysis is central to understanding the function of glycosylated proteins, though due to their heterogeneity, the attached glycans make glycoproteins difficult to crystallize for x-ray crystallography. The recent d
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