A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation.

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

SN - 1059-1524

VL - 4

SP - 605

EP - 613

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 6

ER -