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J Biol Chem, Vol. 274, Issue 30, 20943-20948, July 23, 1999

Requirements for ₅₁ Integrin-mediated Retraction of Fibronectin-Fibrin Matrices

Siobhan A. Corbett and Jean E. Schwarzbauer^¶

From the  Department of Surgery, UMDNJ-Robert Wood Johnson Medical School, New Brunswick, New Jersey 08903 and the ^¶ Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014

Retraction of the blood clot by nucleated cells contributes both to hemostasis and to tissue remodeling. Although plasma fibronectin (FN) is a key component of the clot, its role in clot retraction is unclear. In this report, we demonstrate that the incorporation of FN into fibrin matrices significantly improves clot retraction by nucleated cells expressing the integrin ₅₁. Further, we show that FN-fibrin clots support increased cell spreading when compared with fibrin matrices. To determine the structural requirements for FN in this process, recombinant FN monomers deficient in ligand binding or fibrin cross-linking were incorporated into fibrin clots. We show that recombinant FN monomers support clot retraction by Chinese hamster ovary cells expressing the integrin ₅₁. This process depends on both the Arg-Gly-Asp (RGD) and the synergy cell-binding sites and on covalent FN-fibrin binding, demonstrating that cross-linking within the clot is important for cell-FN interactions. These data show that ₅₁ can bind to FN within a clot to promote clot retraction and support cell shape change. This provides strong evidence that ₅₁-FN interactions may contribute to the cellular events required for wound contraction.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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