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

Anne Woods, James B. McCarthy, Leo T. Furcht, John R. Couchman

Research output: Contribution to journalArticlepeer-review

180 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)605-613
Number of pages9
JournalMolecular biology of the cell
Volume4
Issue number6
DOIs
StatePublished - 1993

Fingerprint Dive into the research topics of 'A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation'. Together they form a unique fingerprint.

Cite this