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A more recent version of this article appeared on October 1, 2002
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Submitted on January 28, 2002
Revised on June 14, 2002
Accepted on July 8, 2002
1 Department of Medicine, Center for Cardiovascular Research, University of Rochester Medical Center, 601 Elmwood Ave, Box 679, Rochester, NY 14642
2 Department of Pharmacology and Physiology, University of Rochester Medical Center, 601 Elmwood Ave, Box 679, Rochester, NY 14642
* Corresponding author. E-mail address: jane_sottile{at}urmc.rochester.edu.
Remodeling of extracellular matrices occurs during development, wound healing, and in a variety of pathological processes including atherosclerosis, ischemic injury, and angiogenesis. Thus, identifying factors that control the balance between matrix deposition and degradation during tissue remodeling is essential for understanding mechanisms that regulate a variety of normal and pathological processes. Using fibronectin-null cells, we found that fibronectin polymerization into the extracellular matrix is required for the deposition of collagen-I and thrombospondin-1, and that the maintenance of extracellular matrix fibronectin fibrils requires the continual polymerization of a fibronectin matrix. Further, integrin ligation alone is not sufficient to maintain extracellular matrix fibronectin in the absence of fibronectin deposition. Our data also demonstrate that the retention of thrombospondin-1 and collagen I into fibrillar structures within the extracellular matrix depends upon an intact fibronectin matrix. An intact fibronectin matrix is also critical for maintaining the composition of cell-matrix adhesion sites; in the absence of fibronectin and fibronectin polymerization, neither 
5ß1 integrin nor tensin localize to fibrillar cell-matrix adhesion sites. These data indicate that fibronectin polymerization is a critical regulator of extracellular matrix organization and stability. The ability of fibronectin polymerization to act as a switch that controls the organization and composition of the extracellular matrix and cell-matrix adhesion sites provides cells with a means of precisely controlling cell-extracellular matrix signalling events that regulate many aspects of cell behavior including cell proliferation, migration, and differentiation.
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