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Vol. 13, Issue 10, 3546-3559, October 2002
and
*Department of Medicine, Center for Cardiovascular Research and
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 on 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 Department of Pharmacology and Physiology, University of
Rochester Medical Center, Rochester, New York 14642
5
1 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
signaling events that regulate many aspects of cell behavior including
cell proliferation, migration, and differentiation.
Corresponding author. E-mail address:
jane_sottile{at}urmc.rochester.edu.
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