Importance of N-glycosylation on CD147 for its biological functions

Int J Mol Sci. 2014 Apr 15;15(4):6356-77. doi: 10.3390/ijms15046356.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Basigin / chemistry
  • Basigin / genetics
  • Basigin / metabolism*
  • Glycosylation
  • Glycosyltransferases / metabolism
  • Humans
  • Matrix Metalloproteinases / metabolism
  • Mutagenesis, Site-Directed
  • Neoplasms / metabolism
  • Neoplasms / pathology

Substances

  • Basigin
  • Glycosyltransferases
  • Matrix Metalloproteinases