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Extracellular matrix assembly of cell‐derived and plasma‐derived fibronectins by substrate‐attached fibroblasts
Author(s) -
Allio Andrea E.,
McKeownLongo Paula J.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041350313
Subject(s) - fibronectins , fibronectin , extracellular matrix , fibroblast , chemistry , cell , matrix (chemical analysis) , microbiology and biotechnology , biochemistry , biology , in vitro , chromatography
Using a previously described model system for the incorporation of plasma fibronectin into the extracellular matrix (McKeown‐Longo, P.J. and Mosher, D.F., 1985. J. Cell Biol., 100 : 364–374), we compared the binding of cell‐derived and plasma‐derived fibronectins to human fibroblast cell layers. Binding was measured in time course experiments using metabolically labeled cell‐derived, iodinated cell‐derived, and iodinated plasma‐derived fibronectins. The kinetics of matrix assembly of cell‐ and plasma‐derived fibronectins were the same. Competitive binding curves using intact fibronectin or the 70‐kD amino‐terminal fragment of fibronectin suggested that cell surface binding sites have equal affinity for cell‐ and plasma‐derived fibronectins. Iodinated fibronectins did not bind to isolated matrices containing collagen type I, fibronectin, and thrombospondin. These results suggest that fibroblasts do not distinguish between cell‐derived and plasma‐derived fibronectins when assembling exogenous fibronectin into extracellular matrix.