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J Biol Chem, Vol. 274, Issue 1, 368-375, January 1, 1999
From the
Functional
1-Integrins Release the Suppression of Fibronectin
Matrix Assembly by Vitronectin
,,,,
Departments of Medicine and Biomolecular
Chemistry, University of Wisconsin, Madison, Wisconsin 53706 and
§ Department of Experimental Pathology, Lund University,
S-221 85 Lund, Sweden
1-null GD25 fibroblasts adherent to
vitronectin fail to bind the N-terminal 70-kDa matrix assembly domain
of fibronectin or to assemble fibronectin (Sakai, T., Zhang, Q.,
Fässler, R., and Mosher, D. F. (1998) J. Cell
Biol. 141, 527-538). We have made four observations that extend
this finding. First, the presence of vitronectin on a substrate that
otherwise can support fibronectin assembly has a dominant-negative
effect on assembly. Second, the dominant-negative effect is lost when
active 1A is expressed. Third, 1A containing the extracellular
D130A inactivating mutation has a dominant-negative effect on
fibronectin assembly. Fourth, 1-null cells adherent to vitronectin
are flat and lack filopodia, whereas 1-null cells adherent to
fibronectin or 1A-expressing cells adherent to either vitronectin or
fibronectin are contracted and exhibit numerous filopodia. These
results reveal, therefore, that GD25 cells adherent to vitronectin can
only assume a shape suitable for assembly of fibronectin when there is
a countervailing signal from functional 1-integrins.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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