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Vol. 8, Issue 12, 2563-2573, December 1997
and
*Department of Molecular Biology, Princeton University, Princeton,
New Jersey 08544-1014; and
Initiation of fibronectin (FN) matrix assembly is dependent
on specific interactions between FN and cell surface integrin receptors. Here, we show that de novo FN matrix assembly exhibits a
slow phase during initiation of fibrillogenesis followed by a more
rapid growth phase. Mn2+, which acts by enhancing
integrin function, increased the rate of FN fibril growth, but
only after the initial lag phase. The RGD cell-binding sequence in type
III repeat 10 is an absolute requirement for initiation by Department of Surgery, Robert
Wood Johnson Medical School, New Brunswick, New Jersey 08903
5
1
integrin. To investigate the role of the cell-binding synergy
site in the adjacent repeat III9, a full-length recombinant
FN containing a synergy mutation, FN(syn
), was tested for
its ability to form fibrils. Mutation of this site drastically reduced
FN assembly by CHO5 cells. Only sparse short fibrils were formed
even after prolonged incubation, indicating that
FN(syn) is defective in progression of the
assembly process. These results show that the synergy site is essential
for 51-mediated accumulation of a FN matrix. However, the
incorporation of FN(syn) into fibrils and the
deoxycholate-insoluble matrix could be stimulated by Mn2+.
Therefore, exogenous activation of integrin receptors can
overcome the requirement for FN's synergy site as well as modulate the rate of FN matrix formation.
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