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Vol. 13, Issue 10, 3601-3613, October 2002
Department of Molecular Biology, Princeton University, Princeton,
New Jersey 08544-1014
A provisional matrix consisting of fibrin and fibronectin (FN) is
deposited at sites of tissue damage and repair. This matrix serves as a
scaffold for fibroblast migration into the wound where these cells
deposit new matrix to replace lost or damaged tissue and eventually
contract the matrix to bring the margins of the wound together.
Tenascin-C is expressed transiently during wound repair in tissue
adjacent to areas of injury and contacts the provisional matrix in
vivo. Using a synthetic model of the provisional matrix, we have found
that tenascin-C regulates cell responses to a fibrin-FN matrix through
modulation of focal adhesion kinase (FAK) and RhoA activation. Cells on
fibrin-FN+tenascin-C redistribute their actin to the cell cortex,
downregulate focal adhesion formation, and do not assemble a FN matrix.
Cells surrounded by a fibrin-FN+tenascin-C matrix are unable to induce
matrix contraction. The inhibitory effect of tenascin-C is circumvented
by downstream activation of RhoA. FAK is also required for matrix
contraction and the absence of FAK cannot be overcome by activation of
RhoA. These observations show dual requirements for both FAK and RhoA
activities during contraction of a fibrin-FN matrix. The effects of
tenascin-C combined with its location around the wound bed suggest that
this protein regulates fundamental processes of tissue repair by
limiting the extent of matrix deposition and contraction to
fibrin-FN-rich matrix in the primary wound area.
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