Collagen-binding motif peptide, a cleavage product of osteopontin, stimulates human neutrophil chemotaxis via pertussis toxin-sensitive G protein-mediated signaling

FEBS Lett. 2008 Oct 15;582(23-24):3379-84. doi: 10.1016/j.febslet.2008.09.023. Epub 2008 Sep 18.

Abstract

The collagen-binding motif (CBM) peptide, a cleavage product of osteopontin (OPN), stimulated intracellular calcium increase in human neutrophils. CBM peptide-stimulated calcium was inhibited by pertussis toxin (PTX), suggesting the influence of PTX-sensitive G-proteins. In addition CBM peptide stimulated the chemotactic migration of human neutrophils and human monocytes. CBM peptide-induced neutrophil chemotaxis was completely inhibited by PTX, once again indicating the influence of Gi proteins. CBM peptide was also found to induce mitogen activated protein kinase activation. CBM peptide-induced neutrophil chemotaxis was mediated by p38 kinase as well as an extracellular signal-regulated protein kinase. Taken together, the results suggest that a cleavage product of OPN, CBM peptide, initiates immune responses by inducing neutrophil trafficking via certain PTX-sensitive cell surface receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Cells, Cultured
  • Chemotaxis*
  • Collagen / metabolism
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • GTP-Binding Proteins / antagonists & inhibitors
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Neutrophils / drug effects*
  • Neutrophils / immunology
  • Osteopontin / metabolism
  • Osteopontin / pharmacology*
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology*
  • Pertussis Toxin / pharmacology

Substances

  • Peptide Fragments
  • Osteopontin
  • Collagen
  • Pertussis Toxin
  • Extracellular Signal-Regulated MAP Kinases
  • GTP-Binding Proteins