TPA Primes alpha2beta1 Integrins for Cell Adhesion

FEBS Lett. 2008 Oct 15;582(23-24):3520-4. doi: 10.1016/j.febslet.2008.09.022. Epub 2008 Sep 18.

Abstract

Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin alpha2beta1 (CHO-alpha2) to collagen at short contact times (0.5-60s) by single cell force spectroscopy (SCFS). The adhesion increased rapidly with contact time and was further strengthened by the addition of 12-O-tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC) and integrin activator. TPA also improved the strength of adhesive units. Furthermore, changes in membrane nanotube properties indicated better coupling of integrins to the cell cytoskeleton. We conclude that in addition to increasing integrin avidity TPA strengthens integrin-cytoskeletal linkage.

MeSH terms

  • Animals
  • CHO Cells
  • Cell Adhesion / drug effects
  • Collagen / chemistry
  • Cricetinae
  • Cricetulus
  • Humans
  • Integrin alpha2beta1 / agonists
  • Integrin alpha2beta1 / genetics
  • Integrin alpha2beta1 / metabolism*
  • Microscopy, Atomic Force
  • Nanotubes / chemistry
  • Protein Kinase C / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology*
  • Transfection

Substances

  • Integrin alpha2beta1
  • Collagen
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate