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J. Biol. Chem., Vol. 269, Issue 40, 24756-24761, Oct, 1994
S Aota, M Nomizu and KM Yamada
Synergistic sites in the central cell-adhesive domain of fibronectin (FN)
substantially enhance cell adhesion mediated by the alpha 5 beta 1 integrin
receptor for fibronectin. We characterized a critical minimal sequence
needed for synergistic activity using site-directed mutagenesis and
homology scanning using intramolecular chimeras. The minimal cell-binding
domain of FN consisting of the 9th and 10th type III FN repeat was
expressed in an Escherichia coli expression system. This protein retained
high biological activity when assayed using a competitive inhibition assay
for FN-mediated adhesion of baby hamster kidney or HT-1080 cells. In
contrast, a construct consisting of the 8th and 10th repeat displayed very
low biological activity. By replacing various portions of the 8th repeat
with homologous 9th repeat segments, we mapped the synergistic region to
the center of the 9th repeat. When a very short peptide sequence,
Pro-His-Ser-Arg-Asn (PHSRN), from the 9th repeat was substituted for the
homologous pentapeptide site in the 8th repeat sequence, the recombinant
protein showed markedly enhanced activity. Further mutagenesis analysis
suggested that the arginine residue of this pentapeptide sequence is
important for function. We also identified a weaker adjacent synergy region
other than the PHSRN region. Epitope mapping of an anti-FN monoclonal
antibody that inhibits FN-mediated adhesion identified the same critical
regions. A synthetic peptide containing the PHSRN sequence showed neither
competitive inhibitory activity in solution nor synergy with a soluble RGD-
containing peptide. However, when the same synthetic peptide was positioned
via a covalent bond at the corresponding site of the normally inactive 8th
repeat, it mediated an enhancement of adhesive activity. These results
identify a pentapeptide site that synergistically enhances the
cell-adhesive activity of the FN RGD sequence.
The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
Laboratory of Developmental Biology, NIDR, National Institutes of Health, Bethesda, Maryland 20892.
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