Cancers 2017, 9(7), 79; https://doi.org/10.3390/cancers9070079
Roles of Integrin α6β4 Glycosylation in Cancer
1
Department of Biochemistry, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima City, Fukushima 960-1295, Japan
2
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan
*
Authors to whom correspondence should be addressed.
Academic Editor: Helen M. Sheldrake
Received: 30 May 2017 / Revised: 30 June 2017 / Accepted: 30 June 2017 / Published: 5 July 2017
(This article belongs to the Special Issue Integrins in Cancer)
Abstract
Malignant transformation is accompanied with aberrant glycosylation of proteins. Such changes in glycan structure also occur in the integrins, which are a large family of cell surface receptors for the extracellular matrix and play key roles in tumor progression. There is now increasing evidence that glycosylation of integrins affects cellular signaling and interaction with the extracellular matrix, receptor tyrosine kinases, and galectins, thereby regulating cell adhesion, motility, growth, and survival. Integrin α6β4 is a receptor for laminin-332 and the increased expression level is correlated with malignant progression and poor survival in various types of cancers. Recent studies have revealed that integrin α6β4 plays central roles in tumorigenesis and the metastatic process. In this review, we summarize our current understanding of the molecular mechanisms of tumor progression driven by integrin α6β4 and also discuss the modification of glycans on integrin β4 subunit to address the important roles of glycan in integrin-mediated tumor progression. View Full-TextKeywords:
integrin; glycosylation; cancer; N-acetylglucosaminyltransferase-V (GnT-V); epithelial to mesenchymal transition (EMT); galectin-3
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Kariya, Y.; Kariya, Y.; Gu, J. Roles of Integrin α6β4 Glycosylation in Cancer. Cancers 2017, 9, 79.
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