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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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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© 2014 Springer Japan
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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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Publisher Name: Springer, Tokyo
Online ISBN: 978-4-431-54836-2
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