Roles of Integrin α6β4 Glycosylation in Cancer
AbstractMalignant 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
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Kariya, Y.; Kariya, Y.; Gu, J. Roles of Integrin α6β4 Glycosylation in Cancer. Cancers 2017, 9, 79.
Kariya Y, Kariya Y, Gu J. Roles of Integrin α6β4 Glycosylation in Cancer. Cancers. 2017; 9(7):79.Chicago/Turabian Style
Kariya, Yoshinobu; Kariya, Yukiko; Gu, Jianguo. 2017. "Roles of Integrin α6β4 Glycosylation in Cancer." Cancers 9, no. 7: 79.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.