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Biological Functions of C1GalT1 and Mucin-Type O-Glycans

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Abstract

O-linked glycosylation is an important posttranslational modification of proteins. O-linked N-acetylgalactosamine (O-GalNAc) glycans are a major O-glycan subtype found in most cells and tissues on a wide range of proteins with diverse functions. Mucin family molecules are among the best studied O-GalNAc glycoproteins, possessing hundreds of O-glycosylation sites in repeated domains rich in Ser/Thr; hence O-GalNAc glycans are also called mucin-type O-glycans. Mucins are highly expressed at mucosal surfaces, interfacing with the environment and protecting against noxious stimuli. Numerous mucin-like glycoproteins are also modified by O-GalNAc glycans that regulate immune cell trafficking and inflammation (e.g., PSGL-1, CD44) or vascular development and integrity (e.g., podoplanin). O-Glycosylation is highly regulated in every tissue and subject to alteration by diverse stimuli and pathologic states. Mucin-type O-glycans thus have critical physiologic functions that influence development, host-environment interactions, and disease pathogenesis.

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References

  • Fu J, Gerhardt H, McDaniel JM et al (2008) Endothelial cell O-glycan deficiency causes blood/lymphatic misconnections and consequent fatty liver disease in mice. J Clin Invest 118(11):3725–3737

  • Fu J, Wei B, Wen T et al (2011) Loss of intestinal core 1-derived O-glycans causes spontaneous colitis in mice. J Clin Invest 121(4):1657–1666

  • Herzog BH, Fu J, Wilson S et al (2013) Podoplanin maintains high endothelial venule integrity by interacting with platelet CLEC-2. Nature 502(7469):105–109

  • Ju T, Cummings RD (2002) A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β 3-galactosyltransferase. Proc Natl Acad Sci U S A 99(26):16613–16618

  • Kawakubo M, Ito Y, Okimura Y et al (2004) Natural antibiotic function of a human gastric mucin against Helicobacter pylori infection. Science 305(5686):1003–1006

  • Mazal D, Lo-Man R, Bay S et al (2013) Monoclonal antibodies toward different Tn-amino acid backbones display distinct recognition patterns on human cancer cells. Implications for effective immuno-targeting of cancer. Cancer Immunol Immunother 62(6):1107–1122

  • Springer GF (1984) T and Tn, general carcinoma autoantigens. Science 224(4654):1198–1206

  • Xia L, Ju T, Westmuckett A et al (2004) Defective angiogenesis and fatal embryonic hemorrhage in mice lacking core 1-derived O-glycans. J Cell Biol 164(3):451–459

  • Yago T, Fu J, McDaniel JM (2010) Core 1-derived O-glycans are essential E-selectin ligands on neutrophils. Proc Natl Acad Sci U S A 107:9204–9209

  • Yeh J, Hiraoka CN, Petryniak B et al (2001) Novel sulfated lymphocyte homing receptors and their control by a core1 extension β 1,3-N-acetylglucosaminyltransferase. Cell 105(7):957–969

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Acknowledgments

Work was supported by grants from the National Institute of Health (DK085691 and HL085607), Crohn’s and Colitis Foundation of America (#285148), and American Heart Association (SDG7410022).

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Authors and Affiliations

  1. Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, 73104, USA

    Kirk Bergstrom, Jianxin Fu & Lijun Xia

  2. Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, 73104, USA

    Lijun Xia

Authors
  1. Kirk Bergstrom
  2. Jianxin Fu
  3. Lijun Xia

Corresponding author

Correspondence to Lijun Xia .

Editor information

Editors and Affiliations

  1. Tokyo Metropolitan Institute of Gerontology, Tokyo Metropolitan Geriatric Hospital, Tokyo, Japan

    Tamao Endo

  2. Department of Biomolecular Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany

    Peter H. Seeberger

  3. Dept. Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA

    Gerald W. Hart

  4. Academia Sinica, Nankang, Taipei, Taiwan

    Chi-Huey Wong

  5. Systems Glycobiology Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Wako, Saitama, Japan

    Naoyuki Taniguchi

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Cite this entry

Bergstrom, K., Fu, J., Xia, L. (2014). Biological Functions of C1GalT1 and Mucin-Type O-Glycans. In: Endo, T., Seeberger, P., Hart, G., Wong, CH., Taniguchi, N. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54836-2_65-1

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  • DOI: https://doi.org/10.1007/978-4-431-54836-2_65-1

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  • Accepted:

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  • Publisher Name: Springer, Tokyo

  • Online ISBN: 978-4-431-54836-2

  • eBook Packages: Living Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

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