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Changes in cell spreading and cytoskeletal organization are induced by
adhesion to a fibronectin-fibrin matrix
SA Corbett, CL Wilson and JE Schwarzbauer
Department of Molecular Biology, Princeton University NJ; 08544-1014, USA.
Plasma fibronectin (pFN) cross-linked to fibrin during the injury response
provides a provisional matrix required for cells to begin tissue repair.
Using a synthetic matrix of pFN and fibrin as a substrate for cell adhesion
and spreading, we have determined that pFN covalently cross-linked to
fibrin into a complex multimer is functionally distinct from pFN
immobilized onto a plastic surface. NIH- 3T3 cells on a FN-fibrin matrix
reach 50% of the maximal cell area of cells spread on FN-coated plastic.
They neither attach nor spread on cross-linked fibrin alone. Cells on
pFN-fibrin matrices form few prominent stress fibers and exhibit clear
differences in membrane ruffling and filopodial extension when stained with
rhodamine-labeled phalloidin. Interestingly, these differences are enhanced
by upregulation of protein kinase C. These data suggest that cell-FN
interactions can be modified by the molecular context of the protein within
the extracellular matrix resulting in distinct cell morphology and
cytoskeletal organization.
Volume 88,
Issue 1,
pp. 158-166,
07/01/1996
Copyright © 1996 by The American Society of Hematology

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