Molecular basis of interaction between NG2 proteoglycan and galectin-3

Yunfei Wen, Irwan T. Makagiansar, Jun Ichi Fukushi, Fu-Tong Liu, Michiko N. Fukuda, William B. Stallcup

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

Previous work has demonstrated the ability of the NG2 proteoglycan, a component of microvascular pericytes, to stimulate endothelial cell motility and morphogenesis. This function of NG2 depends on formation of a complex with galectin-3 and α3β1 integrin to stimulate integrin-mediated transmembrane signaling. In addition, the co-expression of galectin-3 and NG2 in A375 melanoma cells suggests that the malignant properties of these cells may be affected by interaction between the two molecules. Here, we extend the theme of co-expression and interaction of NG2 and galectin-3 to human glioma cells. We also establish a molecular basis for the NG2/galectin-3 interaction. The C-terminal carbohydrate recognition domain of galectin-3 is responsible for binding to the NG2 core protein. Within the NG2 extracellular domain, the membrane-proximal D3 segment of the proteoglycan contains the primary binding site for interaction with galectin-3. The interaction between galectin-3 and NG2 is a carbohydrate-dependent one mediated by N-linked rather than O-linked oligosaccharides within the D3 domain of the NG2 core protein. These studies establish a foundation for attempts to reduce the aggressive properties of tumor cells by disrupting the NG2/galectin-3 interaction.

Original languageEnglish (US)
Pages (from-to)115-127
Number of pages13
JournalJournal of Cellular Biochemistry
Volume98
Issue number1
DOIs
StatePublished - May 1 2006

    Fingerprint

Keywords

  • Carbohydrate-dependent protein-protein interaction
  • Galectin-3
  • Glioma
  • Glycosylation
  • NG2

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Wen, Y., Makagiansar, I. T., Fukushi, J. I., Liu, F-T., Fukuda, M. N., & Stallcup, W. B. (2006). Molecular basis of interaction between NG2 proteoglycan and galectin-3. Journal of Cellular Biochemistry, 98(1), 115-127. https://doi.org/10.1002/jcb.20768