Importance of N-Glycosylation on CD147 for Its Biological Functions
Cell Engineering Research Centre and Department of Cell Biology, State Key Discipline of Cell Biology, Fourth Military Medical University, Xi'an 710032, Shaanxi, China
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Authors to whom correspondence should be addressed.
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These authors contributed equally to this work.
Int. J. Mol. Sci. 2014, 15(4), 6356-6377; https://doi.org/10.3390/ijms15046356
Received: 9 December 2013 / Revised: 25 February 2014 / Accepted: 4 April 2014 / Published: 15 April 2014
(This article belongs to the Special Issue Glycosylation and Glycoproteins)
Glycosylation of glycoproteins is one of many molecular changes that accompany malignant transformation. Post-translational modifications of proteins are closely associated with the adhesion, invasion, and metastasis of tumor cells. CD147, a tumor-associated antigen that is highly expressed on the cell surface of various tumors, is a potential target for cancer diagnosis and therapy. A significant biochemical property of CD147 is its high level of glycosylation. Studies on the structure and function of CD147 glycosylation provide valuable clues to the development of targeted therapies for cancer. Here, we review current understanding of the glycosylation characteristics of CD147 and the glycosyltransferases involved in the biosynthesis of CD147 N-glycans. Finally, we discuss proteins regulating CD147 glycosylation and the biological functions of CD147 glycosylation.
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Keywords:
CD147; N-glycosylation; glycosyltransferases; matrix metalloproteinase; cancer invasion and metastasis
This is an open access article distributed under the Creative Commons Attribution License
MDPI and ACS Style
Bai, Y.; Huang, W.; Ma, L.-T.; Jiang, J.-L.; Chen, Z.-N. Importance of N-Glycosylation on CD147 for Its Biological Functions. Int. J. Mol. Sci. 2014, 15, 6356-6377.
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