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Vol. 10, Issue 3, 785-798, March 1999
Department of Microbiology, University of Pennsylvania,
Philadelphia, Pennsylvania 19104
Integrin-mediated cell adhesion to extracellular matrices
provides signals essential for cell cycle progression and
differentiation. We demonstrate that substrate-dependent changes in the
conformation of adsorbed fibronectin (Fn) modulated integrin
binding and controlled switching between proliferation and
differentiation. Adsorption of Fn onto bacterial polystyrene (B),
tissue culture polystyrene (T), and collagen (C) resulted in
differences in Fn conformation as indicated by antibody binding. Using
a biochemical method to quantify bound integrins in cultured
cells, we found that differences in Fn conformation altered the
quantity of bound 
5 and 
1
integrin subunits but not v or 3.
C2C12 myoblasts grown on these Fn-coated substrates proliferated to
different levels (B > T > C). Immunostaining for
muscle-specific myosin revealed minimal differentiation on B,
significant levels on T, and extensive differentiation on C. Differentiation required binding to the RGD cell binding site in Fn and
was blocked by antibodies specific for this site. Switching between
proliferation and differentiation was controlled by the levels of
51 integrin bound to Fn, and
differentiation was inhibited by anti-5, but not
anti-v, antibodies, suggesting distinct
integrin-mediated signaling pathways. Control of cell
proliferation and differentiation through conformational changes in
extracellular matrix proteins represents a versatile mechanism to
elicit specific cellular responses for biological and biotechnological applications.
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