Interaction of fibronectin (FN) cell binding fragments and interleukin-8 (IL-8) in regulating neutrophil chemotaxis

Biochem Biophys Res Commun. 1994 Nov 30;205(1):706-13. doi: 10.1006/bbrc.1994.2723.


This study investigated the possible interaction of FN fragments in regulating IL-8-mediated neutrophil chemotaxis in vitro using Neuroprobe microchambers. Human neutrophil suspensions were incubated with purified FN fragments or an RGD-containing peptide and allowed to migrate in response to chemotactically active concentrations of human recombinant IL-8. The 120-kD fragment of FN containing the RGD sequence or an RGD peptide (GRGDSP) inhibited IL-8-mediated neutrophil chemotaxis; however, these RGD peptides did not inhibit neutrophil chemotaxis in response to other chemotactic agents. Furthermore, FN fragments not containing the RGD sequence had no effect on IL-8-mediated chemotaxis. These data suggest that directed migration of neutrophils in response to IL-8 is inhibited in the presence of cell-binding fragments of FN and may represent a local mechanism for terminating neutrophil migration at areas of tissue injury.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Chemotaxis, Leukocyte* / drug effects
  • Fibronectins / chemistry
  • Fibronectins / pharmacology*
  • Humans
  • Interleukin-8 / pharmacology*
  • Molecular Sequence Data
  • Neutrophils / cytology*
  • Oligopeptides / pharmacology
  • Peptide Fragments / pharmacology*
  • Recombinant Proteins / pharmacology


  • Fibronectins
  • Interleukin-8
  • Oligopeptides
  • Peptide Fragments
  • Recombinant Proteins
  • arginyl-glycyl-aspartic acid