O-GalNAc Glycans

Inka Brockhausen; Pamela Stanley

doi:10.1101/glycobiology.3e.010

O-GalNAc Glycans

Review

In: Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015. Chapter 10.

2017.

Authors

Inka Brockhausen, Pamela Stanley

Book Editors

Book Affiliations

¹ Distinguished Professor of Medicine and Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
² Professor of Surgery, Director, National Center for Functional Glycomics, Harvard Medical School, Cambridge, Massachusetts, USA
³ Distinguished Professor of Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
⁴ Horace W. Goldsmith Foundation Chair and Professor of Cell Biology, Albert Einstein College of Medicine, New York, New York, USA
⁵ Professor and Chairman of Biological Chemistry, Johns Hopkins University, Baltimore, Maryland, USA
⁶ Professor of Mycology, ETH Zürich, Zürich, Switzerland
⁷ Regents Professor and Director, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
⁸ Professor, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
⁹ Professor of Glycoproteomics and Glycomics, Macquarie University and Institute for Glycomics, Griffith University, Sydney, Australia
¹⁰ Professor and Eminent Scholar, University of Georgia, Athens, Georgia, USA
¹¹ Professor, Departments of Pharmacology and Neuroscience, Johns Hopkins University, Baltimore, Maryland, USA
¹² Director, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany

Excerpt

Many glycoproteins carry glycans initiated by GalNAc attached to the hydroxyl of Ser or Thr residues. Mucins are the class of glycoproteins carrying the greatest number of O-GalNAc glycans (also called mucin-type O-glycans), but this posttranslational modification is common among many glycoproteins. The sugars found in O-GalNAc glycans include GalNAc, Gal, GlcNAc, Fuc, and Sia, whereas Man, Glc, or Xyl residues are not represented. Sialic acids may be modified by O-acetylation, and Gal and GlcNAc by sulfation. The length of O-GalNAc glycans may vary from a single GalNAc to more than 20 sugar residues and can include blood group and other glycan epitopes. This chapter describes the structures, biosynthesis, and functions of O-GalNAc glycans in mammals.

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