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Am J Physiol Cell Physiol 280: C1394-C1402, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 6, C1394-C1402, June 2001

Soluble heparin-binding peptides regulate chemokinesis and cell adhesive forces

John H Chon and Elliot L. Chaikof

School of Chemical Engineering, Georgia Institute of Technology, Atlanta 30332; and Departments of Surgery and Bioengineering, Emory University, Atlanta, Georgia 30322

The ability of a soluble heparin-binding peptide sequence derived from fibronectin to modulate the adhesion and chemokinetic migration behavior of arterial smooth muscle cells was assessed using a novel glass microsphere centrifugation assay and automated time-lapse fluorescence videomicroscopy, respectively. Treatment of cells grown on fibronectin-coated substrates with the soluble heparin-binding peptide resulted in the disassembly of focal adhesions, as assessed by immunohistochemical staining. These observations were consistent with an observed dose-dependent two- to fivefold reduction in cell-substrate adhesive strength (P < 0.001) and a biphasic effect on migration speed (P < 0.05). Moreover, heparin-binding peptides induced a twofold reduction (P < 0.01) in two-dimensional cell dispersion in the presence of a non-heparin-binding growth factor, platelet-derived growth factor-AB (PDGF-AB). Heparin-binding peptides were unable to mediate these effects when cells were grown on substrates lacking a heparin-binding domain. These data support the notion that competitive interactions between cell surface heparan sulfates with heparin-binding peptides may modulate chemokinetic cell migration behavior and other adhesion-related processes.

heparan sulfates; focal contact; extracellular matrix


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