Syndecan- and integrin-binding peptides synergistically accelerate cell adhesion

FEBS Lett. 2010 Aug 4;584(15):3381-5. doi: 10.1016/j.febslet.2010.06.032. Epub 2010 Jun 26.

Abstract

Integrins and syndecans mediate cell adhesion to extracellular matrix and their synergistic cooperation is implicated in cell adhesion processes. We previously identified two active peptides, AG73 and EF1, from the laminin alpha1 chain LG4 module, that promote cell attachment through syndecan- and alpha2beta1 integrin-binding, respectively. Here, we examined time-dependent cell attachment on the mixed peptides AG73/EF1. The AG73/EF1 promoted stronger and more rapid cell attachment, spreading, FAK phosphorylation that reached a maximum at 20 min than that on AG73 (40 min) or EF1 (90 min) supplied singly. Thus, the syndecan- and alpha2beta1 integrin-binding peptides synergistically affect cells and accelerate cell adhesion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Cell Adhesion / drug effects
  • Cell Movement / drug effects
  • Fibroblasts / cytology*
  • Fibroblasts / drug effects*
  • Fibroblasts / enzymology
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism
  • Humans
  • Integrin alpha2beta1 / metabolism*
  • Peptides / metabolism*
  • Peptides / pharmacology
  • Phosphorylation / drug effects
  • Phosphotyrosine / metabolism
  • Protein Binding / drug effects
  • Signal Transduction / drug effects
  • Stress Fibers / drug effects
  • Stress Fibers / metabolism
  • Syndecans / metabolism*
  • Time Factors

Substances

  • Actins
  • Integrin alpha2beta1
  • Peptides
  • Syndecans
  • Phosphotyrosine
  • Focal Adhesion Protein-Tyrosine Kinases