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J. Biol. Chem., Vol. 279, Issue 34, 35749-35759, August 20, 2004

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Assembly of Exogenous Fibronectin by Fibronectin-null Cells Is Dependent on the Adhesive Substrate^*

Eunnyung Bae, Takao Sakai, and Deane F. Mosher

From the Departments of Pathology and Laboratory Medicine and of Medicine, University of Wisconsin, Madison, Wisconsin 53706

The role of endogenously synthesized fibronectin (FN) in assembly was studied with cells lacking or expressing FN. Cells were cultured as homogeneous or mixed populations on surfaces coated with different matrix proteins. Compared with FN-expressing cells, FN-null cells poorly assembled exogenous plasma FN (pFN) when adhered to vitronectin or the recombinant cell-binding domain (III_7–10) of FN. Vitronectin had a suppressive effect that was overcome by co-adsorbed pFN or laminin-1 but not by soluble FN. In co-cultures of FN-expressing cells and FN-null cells, endogenous FN was preferentially assembled around FN-expressing cells regardless of the adhesive ligand. If the adhesive ligand was vitronectin, exogenous pFN assembled preferentially around cells expressing cellular FN or recombinant EDa- or EDa+ FN. In co-cultures on vitronectin of FN-null cells and ₁ integrin subunit-null cells, fibrils of cellular FN and pFN were preferentially deposited by FN-null (₁-expressing) cells immediately adjacent to (FN-secreting) ₁-null cells. In co-cultures on vitronectin of FN-null cells and ₁-null cells expressing a chimera with the extracellular domain of ₁ and the cytoplasmic domain of ₃, preferential assembly was by the chimera-expressing cells. These results indicate that the adhesive ligand is a determinant of FN assembly by cells not secreting endogenous FN (suppressive if vitronectin, non-suppressive but non-supportive if III_7–10, supportive if pFN or laminin-1) and suggest that efficient interaction of freshly secreted cellular FN with a ₁ integrin, presumably ₅₁, substitutes for integrin-mediated adherence to a preformed matrix of laminin-1 or pFN to support assembly of FN.

Received for publication, June 7, 2004

^* This work was supported by National Institutes of Health Grant HL 21644. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Rm. 4285, Medical Science Center, 1300 University Ave., Madison, WI 53706. Tel.: 608-262-1576; Fax: 608-263-4969; E-mail: dfmosher{at}wisc.edu.

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