Abstract
Integrins are transmembrane heterodimeric proteins sensing the cell microenvironment and modulating numerous signaling pathways. Changes in integrin function and expression between normal and tumor cells support involvement of specific integrins in tumor progression and aggressiveness. Integrin function on the cell surface is regulated by their cytoplasmic domains interacting with the intracellular proteins. It is widely accepted that integrin activation by specific proteins is essential for cell adhesion and integrin linkage to the actin cytoskeleton. However, a growing body of evidence indicates that the N-glycosylation of integrin plays crucial roles in heterodimer formation and its biological functions. In fact, tumor cells exhibit striking changes in cell surface glycosylation as a consequence of dysregulated glycosyltransferases and glycosidases. This chapter highlights the current knowledge about roles of N-glycosylation on biological function of α5β1 integrin, also called the fibronectin receptor.
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Gu, J., Hang, Q., Fukuda, T., Isaji, T. (2015). Integrin α5β1 and Its N-Glycosylation. In: Taniguchi, N., Endo, T., Hart, G., Seeberger, P., Wong, CH. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54841-6_53
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DOI: https://doi.org/10.1007/978-4-431-54841-6_53
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Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-54840-9
Online ISBN: 978-4-431-54841-6
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