Additional Recognition Sites in the C-Terminal Heparin-Binding Domain of Fibronectin Promote Adhesion of PMA-Treated U937 Cells

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Recently we have shown an evidence that a peptide, corresponding to residues Gln1892 to Gly1910, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of phorbol-12-myristate 13-acetate (PMA)-treated U937 cells and binds to both integrin alpha 4 beta 1 and glycosaminoglycans on U937 cells surface. We present additional adhesion-promoting sites to PMA-treated U937 cells present in the C-terminal heparin-binding domain of fibronectin. Three synthetic peptides (residues Ala1819 to Lys1830, designated E5; Thr1828 to Gly1940, E4; and Lys1946 to Leu1963, D1) were active to inhibit adhesion of PMA-treated U937 cells to the 29-kDa fragment comprising the C-terminal heparin-binding domain of fibronectin. Scrambled versions of these peptides had no inhibitory activity on this adhesion. The IgG-conjugated peptides (IgG-E5, IgG-E4, and IgG-D1) were also active and supported adhesion to an extent comparable to that of the 29-kDa fragment. The adhesion of PMA-treated U937 cells on these three IgG-conjugated peptides was only inhibited by glycosaminoglycans and not by integrin alpha 4 beta 1. These results indicate that additional adhesion-promoting sequences are present in the C-terminal heparin-binding domain of fibronectin and that the activity of these peptides depends on peptide sequence, mainly the result of net charges or net hydropathy indices.