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Volume 271, Number 42, Issue of October 18, 1996 pp. 26110-26116
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Binding of the NG2 Proteoglycan to Type VI Collagen and Other Extracellular Matrix Molecules

(Received for publication, May 9, 1996, and in revised form, July 9, 1996)

Michael A. Burg , Emmanuelle Tillet ^¶ , Rupert Timpl ^¶ and William B. Stallcup

From the  La Jolla Cancer Research Center, The Burnham Institute, La Jolla, California 92037 and ^¶ Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany

Previous studies have suggested that the NG2 proteoglycan interacts with type VI collagen. We have further characterized this interaction using a solid phase binding assay in which purified NG2 was shown to bind to pepsin-solubilized type VI collagen. In addition, NG2 bound a recombinant 2 (VI) collagen chain but did not appreciably bind to the recombinant 1 (VI) chain or the N-terminal domain of 3 (VI) (N9-N2). Binding of NG2 to type VI collagen was shown to be concentration-dependent and saturable and to depend mainly on the NG2 core protein, since chondroitinase-treated NG2 bound the collagen as well as undigested samples. In addition, the binding studies revealed several other possible ligands for NG2, including type II collagen, type V collagen, tenascin, and laminin. Binding of the proteoglycan to these molecules was also shown to be mediated by domains contained within the NG2 core protein. The ability of NG2 to bind to these extracellular matrix molecules was compared with that of the chondroitin sulfate proteoglycan decorin, revealing an almost identical binding pattern of the two proteoglycans to the different collagen types. In addition, decorin was found to effectively inhibit the ability of NG2 to bind to collagen, thus suggesting that the two proteoglycans may bind to some of the same regions on the collagen substrates. In contrast, decorin did not bind tenascin and was ineffective in inhibiting the binding of NG2 to tenascin or laminin, indicating that NG2 may bind these two molecules using a separate domain that is distinct from its collagen binding region.

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