A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation.
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A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. / Woods, A; McCarthy, J B; Furcht, L T; Couchman, J R.
In: Molecular Biology of the Cell, Vol. 4, No. 6, 1993, p. 605-13.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation.
AU - Woods, A
AU - McCarthy, J B
AU - Furcht, L T
AU - Couchman, J R
N1 - Keywords: Amino Acid Sequence; Antibodies, Monoclonal; Binding, Competitive; Cell Adhesion; Cell Adhesion Molecules; Cells, Cultured; Chondroitinases and Chondroitin Lyases; Fibroblasts; Fibronectins; Heparin; Heparin Lyase; Humans; Molecular Sequence Data; Peptide Fragments; Polysaccharide-Lyases
PY - 1993
Y1 - 1993
N2 - Cell adhesion to extracellular matrix molecules such as fibronectin involves complex transmembrane signaling processes. Attachment and spreading of primary fibroblasts can be promoted by interactions of cell surface integrins with RGD-containing fragments of fibronectin, but the further process of focal adhesion and stress fiber formation requires additional interactions. Heparin-binding fragments of fibronectin can provide this signal. The COOH-terminal heparin-binding domain of fibronectin contains five separate heparin-binding amino acid sequences. We show here that all five sequences, as synthetic peptides coupled to ovalbumin, can support cell attachment. Only three of these sequences can promote focal adhesion formation when presented as multicopy complexes, and only one of these (WQPPRARI) retains this activity as free peptide. The major activity of this peptide resides in the sequence PRARI. The biological response to this peptide and to the COOH-terminal fragment may be mediated through cell surface heparan sulfate proteoglycans because treatment of cells with heparinase II and III, or competition with heparin, reduces the response. Treatment with chondroitinase ABC or competition with chondroitin sulfate does not.
AB - Cell adhesion to extracellular matrix molecules such as fibronectin involves complex transmembrane signaling processes. Attachment and spreading of primary fibroblasts can be promoted by interactions of cell surface integrins with RGD-containing fragments of fibronectin, but the further process of focal adhesion and stress fiber formation requires additional interactions. Heparin-binding fragments of fibronectin can provide this signal. The COOH-terminal heparin-binding domain of fibronectin contains five separate heparin-binding amino acid sequences. We show here that all five sequences, as synthetic peptides coupled to ovalbumin, can support cell attachment. Only three of these sequences can promote focal adhesion formation when presented as multicopy complexes, and only one of these (WQPPRARI) retains this activity as free peptide. The major activity of this peptide resides in the sequence PRARI. The biological response to this peptide and to the COOH-terminal fragment may be mediated through cell surface heparan sulfate proteoglycans because treatment of cells with heparinase II and III, or competition with heparin, reduces the response. Treatment with chondroitinase ABC or competition with chondroitin sulfate does not.
M3 - Journal article
C2 - 8374170
VL - 4
SP - 605
EP - 613
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 6
ER -
ID: 5165859