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The NG2 chondroitin sulfate proteoglycan is a membrane-associated molecule of approximately 500 kD with a core glycoprotein of 300 kD. Both the complete proteoglycan and a smaller quantity of the 300-kD core are immunoprecipitable with polyclonal and monoclonal antibodies against purified NG2. From some cell lines, the antibodies coprecipitate NG2 and type VI collagen, the latter appearing on SDS-PAGE as components of 140 and 250 kD under reducing conditions. The immunoprecipitation of type VI collagen does not seem to be due to recognition of the collagen by the antibodies, but rather to binding of the collagen to NG2. Studies on the NG2-type VI collagen complex suggest that binding between the two molecules is mediated by protein-protein interactions rather than by ionic interactions involving the glycosaminoglycans. Immunofluorescence double labeling in frozen sections of embryonic rat shows that NG2 and type VI collagen are colocalized in structures such as the intervertebral discs and arteries of the spinal column. In vitro the two molecules are highly colocalized on the surface of several cell lines. Treatment of these cells resulting in a change in the distribution of NG2 on the cell surface also causes a parallel change in type VI collagen distribution. Our results suggest that cell surface NG2 may mediate cellular interactions with the extracellular matrix by binding to type VI collagen.
Authors : Stallcup W B , Dahlin K , Healy P ,
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WP1017: Type II interferon signaling (IFNG)
WP1136: Type II interferon signaling (IFNG)
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 Adipocyte-derived collagen VI affects early mammary tumor progression in vivo, demonstrating a critical interaction in the tumor/stroma microenvironment.
 NG2 proteoglycan mediates beta1 integrin-independent cell adhesion and spreading on collagen VI.
 Identification and functional characterization of two type VI collagen receptors, alpha 3 beta 1 integrin and NG2, during avian corneal stromal development.
 A central segment of the NG2 proteoglycan is critical for the ability of glioma cells to bind and migrate toward type VI collagen.
 Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules.
 Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis.
 Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface.
 Interaction of the NG2 chondroitin sulfate proteoglycan with type VI collagen.
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