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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2017: 3.022

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 382, Issue 2


O-Glycosylation of the Mucin Type

Franz-Georg Hanisch
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2001.022


While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteins are glycoproteins. Mucintype Oglycosylation is a widespread posttranslational modification of proteins found in the entire animal kingdom, but also in higher plants. The structural complexity of the chains initiated by Olinked GalNAc exceeds that of Nlinked chains by far. The process during which serine and threonine residues of proteins become modified is confined to the cis to trans Golgi compartments. The initiation of this process by peptidyl GalNActransferases is ruled by the sequence context of putative Oglycosylation sites, but also by epigenetic regulatory mechanisms, which can be mediated by enzyme competition. The cellular repertoir of glycosyltransferases with their distinct donor sugar and acceptor sugar specificities, their sequential action at highlyordered surfaces, and their localizations in subcompartments of the Golgi finally determine the cellspecific Oglycosylation profile. Dramatic alterations of the glycosylation machinery are observed in cancer cells, resulting in aberrantly Oglycosylated proteins that expose previously masked peptide motifs and new antigenic targets. The functional aspects of Olinked glycans, which comprise among many others their potential role in sorting and secretion of glycoproteins, their influence on protein conformation, and their multifarious involvement in cell adhesion and immunological processes, appear as complex as their structures.

About the article

Published Online: 2005-06-01

Published in Print: 2001-02-12

Citation Information: Biological Chemistry, Volume 382, Issue 2, Pages 143–149, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2001.022.

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Ulrika Westerlind, Alexandra Hobel, Nikola Gaidzik, Edgar Schmitt, and Horst Kunz
Angewandte Chemie, 2008, Volume 120, Number 39, Page 7662
Louise Royle, Elizabeth Matthews, Anthony Corfield, Monica Berry, Pauline M. Rudd, Raymond A. Dwek, and Stephen D. Carrington
Glycoconjugate Journal, 2008, Volume 25, Number 8, Page 763
Flavio Mantelli and Pablo Argüeso
Current Opinion in Allergy and Clinical Immunology, 2008, Volume 8, Number 5, Page 477
Yongmei Qu, Jack Egelund, Paul R. Gilson, Fiona Houghton, Paul A. Gleeson, Carolyn J. Schultz, and Antony Bacic
Plant Molecular Biology, 2008, Volume 68, Number 1-2, Page 43
J. Lofling, M. Diswall, S. Eriksson, T. Boren, M. E Breimer, and J. Holgersson
Glycobiology, 2008, Volume 18, Number 7, Page 494
Shin-Yi Yu, Kay-Hooi Khoo, Zhangung Yang, Anthony Herp, and Albert M. Wu
Glycoconjugate Journal, 2008, Volume 25, Number 3, Page 199
Tilo Schwientek, Ulla Mandel, Udo Roth, Stefan Müller, and Franz-Georg Hanisch
PROTEOMICS, 2007, Volume 7, Number 18, Page 3264
Klaus W Wagner, Elizabeth A Punnoose, Thomas Januario, David A Lawrence, Robert M Pitti, Kate Lancaster, Dori Lee, Melissa von Goetz, Sharon Fong Yee, Klara Totpal, Ling Huw, Viswanatham Katta, Guy Cavet, Sarah G Hymowitz, Lukas Amler, and Avi Ashkenazi
Nature Medicine, 2007, Volume 13, Number 9, Page 1070
Ludwig Lehle, Sabine Strahl, and Widmar Tanner
Angewandte Chemie International Edition, 2006, Volume 45, Number 41, Page 6802
Antti Rivinoja, Nina Kokkonen, Ilmo Kellokumpu, and Sakari Kellokumpu
Journal of Cellular Physiology, 2006, Volume 208, Number 1, Page 167
Fernando J Irazoqui, Victor G Sendra, Ricardo D Lardone, and Gustavo A Nores
Immunology and Cell Biology, 2005, Volume 83, Number 4, Page 405
John W. Holland, Hilton C. Deeth, and Paul F. Alewood
PROTEOMICS, 2005, Volume 5, Number 4, Page 990

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