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Biochem Biophys Res Commun. 1994 Mar 30;199(3):1509-17.

The binding of fibronectin to entactin is mediated through the 29 kDa amino terminal fragment of fibronectin and the G2 domain of entactin.

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1
Department of Biological Sciences, University of Pittsburgh, PA 15260.

Abstract

Previous work has shown that fibronectin and entactin, an ubiquitous basement membrane glycoprotein, co-localize in the extracellular matrix of the embryonal carcinoma-derived 4CQ cell. Glutathione-S-transferase (GST) fusion proteins containing different domains of entactin have been obtained in the pGEX3X expression vector. These fusion proteins, GST-G1, GST-G2, GST-E and GST-G3, were purified with a glutathione affinity column. By using a solid phase binding assay, it was shown that the 125I-labeled 29 kDa amino terminal fragment of bovine fibronectin bound specifically to the immobilized GST-G2 fusion protein but not to GST-G1, GST-E, and GST-G3. Half saturation for binding of the 29 kDa fibronectin fragment to the immobilized GST-G2 fusion protein was obtained at a concentration of approximately 5 nM. It is suggested that the strong association between GST-G2, which contains the second globular domain of entactin, and the 29 kDa amino terminal fragment of fibronectin may be involved in the assembly of certain types of extracellular matrices.

PMID:
8147897
DOI:
10.1006/bbrc.1994.1402
[Indexed for MEDLINE]

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