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Molecular basis of interaction between NG2 proteoglycan and galectin‐3
Author(s) -
Wen Yunfei,
Makagiansar Irwan T.,
Fukushi Junichi,
Liu FuTong,
Fukuda Michiko N.,
Stallcup William B.
Publication year - 2006
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20768
Subject(s) - proteoglycan , microbiology and biotechnology , galectin , computational biology , chemistry , galectin 1 , basis (linear algebra) , biology , extracellular matrix , mathematics , geometry
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. J. Cell. Biochem. 98: 115–127, 2006. © 2005 Wiley‐Liss, Inc.