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

24 Citations (Scopus)

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

Galectin 3
Integrins
Carbohydrates
Pericytes
Proteoglycans
chondroitin sulfate proteoglycan 4
Oligosaccharides
Morphogenesis
Endothelial cells
Glioma
Cell Movement
Melanoma
Proteins
Endothelial Cells
Tumors
Binding Sites
Cells
Membranes
Molecules

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

Molecular basis of interaction between NG2 proteoglycan and galectin-3. / Wen, Yunfei; Makagiansar, Irwan T.; Fukushi, Jun Ichi; Liu, Fu-Tong; Fukuda, Michiko N.; Stallcup, William B.

In: Journal of Cellular Biochemistry, Vol. 98, No. 1, 01.05.2006, p. 115-127.

Research output: Contribution to journalArticle

Wen, Y, Makagiansar, IT, Fukushi, JI, Liu, F-T, Fukuda, MN & Stallcup, WB 2006, 'Molecular basis of interaction between NG2 proteoglycan and galectin-3', Journal of Cellular Biochemistry, vol. 98, no. 1, pp. 115-127. https://doi.org/10.1002/jcb.20768
Wen Y, Makagiansar IT, Fukushi JI, Liu F-T, Fukuda MN, Stallcup WB. Molecular basis of interaction between NG2 proteoglycan and galectin-3. Journal of Cellular Biochemistry. 2006 May 1;98(1):115-127. https://doi.org/10.1002/jcb.20768
Wen, Yunfei ; Makagiansar, Irwan T. ; Fukushi, Jun Ichi ; Liu, Fu-Tong ; Fukuda, Michiko N. ; Stallcup, William B. / Molecular basis of interaction between NG2 proteoglycan and galectin-3. In: Journal of Cellular Biochemistry. 2006 ; Vol. 98, No. 1. pp. 115-127.
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