Next Article in Journal
The Role of the Core Non-Homologous End Joining Factors in Carcinogenesis and Cancer
Next Article in Special Issue
Inside the Cell: Integrins as New Governors of Nuclear Alterations?
Previous Article in Journal
Erratum: Tanaka, T. et al. Cimetidine and Clobenpropit Attenuate Inflammation-Associated Colorectal Carcinogenesis in Male ICR Mice. Cancers, 2016, 8, 25
Previous Article in Special Issue
Can Integrin Agonists Have Cards to Play against Cancer? A Literature Survey of Small Molecules Integrin Activators

Roles of Integrin α6β4 Glycosylation in Cancer

Department of Biochemistry, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima City, Fukushima 960-1295, Japan
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
Cancers 2017, 9(7), 79;
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)
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-Text
Keywords: integrin; glycosylation; cancer; N-acetylglucosaminyltransferase-V (GnT-V); epithelial to mesenchymal transition (EMT); galectin-3 integrin; glycosylation; cancer; N-acetylglucosaminyltransferase-V (GnT-V); epithelial to mesenchymal transition (EMT); galectin-3
Show Figures

Figure 1

MDPI and ACS Style

Kariya, Y.; Kariya, Y.; Gu, J. Roles of Integrin α6β4 Glycosylation in Cancer. Cancers 2017, 9, 79.

AMA Style

Kariya Y, Kariya Y, Gu J. Roles of Integrin α6β4 Glycosylation in Cancer. Cancers. 2017; 9(7):79.

Chicago/Turabian Style

Kariya, Yoshinobu, Yukiko Kariya, and Jianguo Gu. 2017. "Roles of Integrin α6β4 Glycosylation in Cancer" Cancers 9, no. 7: 79.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop