Altered vitronectin receptor (alphav integrin) function in fibroblasts adhering on hydrophobic glass

J Biomed Mater Res. 1999 Mar 5;44(3):341-51. doi: 10.1002/(sici)1097-4636(19990305)44:3<341::aid-jbm13>;2-h.


Function of integrins is crucial for adhesion, movement, proliferation, and survival of cells. In a recent study we found impaired fibronectin receptor function on hydrophobic substrata (G. Altankov et al. J Biomater Sci Polym Edn 1997;8:712-740). Here, we have studied the distribution and function of the vitronectin receptor (alphav integrin) in fibroblasts adhering on hydrophilic glass and hydrophobic octadecyl glass (ODS). The morphology of fibroblasts and the organization of actin cytoskeleton were studied and found to be altered on ODS, where the cells did not spread and possessed condensed actin. Pretreatment of the surfaces with serum or pure vitronectin improved cell morphology on both substrata, resulting in the development of longitudinal actin stress fibers. It was found with biotinylated vitronectin that comparable quantities of vitronectin were adsorbed from single vitronectin solutions or serum on glass and on hydrophobic ODS. The organization of the vitronectin receptors on the ventral cell surface was investigated in permeabilized cells showing normal focal adhesions in fibroblasts plated on glass but none of these structures on ODS. The distribution of alphav integrin on the dorsal cell surface was studied on nonpermeabilized living cells after antibody tagging. While fibroblasts adhering on plain or serum-treated glass developed a linear organization of alphav integrin, cells on plain and serum-treated ODS were not able to reorganize the vitronectin receptor. Studies on signal transduction with antiphosphotyrosine antibodies revealed co-localization of alphav integrin and phosphotyrosine in focal adhesions on glass and serum-treated glass. However, signaling was almost absent on plain ODS and weak on serum-treated ODS. It was concluded that alterations in vitronectin receptor function on the ventral cell surface caused by the hydrophobic material surface inhibit signal transfer and subsequent intracellular events that are important for the organization and function of integrins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / analysis
  • Adsorption
  • Cell Adhesion
  • Cell Culture Techniques / instrumentation*
  • Cell Membrane Permeability
  • Cell Polarity
  • Cell Size
  • Cells, Cultured
  • Chemical Phenomena
  • Chemistry, Physical
  • Culture Media
  • Culture Media, Serum-Free
  • Cytoskeleton / ultrastructure
  • Fibroblasts / cytology
  • Fibroblasts / metabolism*
  • Glass / chemistry*
  • Humans
  • Phosphorylation
  • Phosphotyrosine / analysis
  • Protein Processing, Post-Translational
  • Receptors, Vitronectin / physiology*
  • Signal Transduction
  • Silanes / chemistry*


  • Actins
  • Culture Media
  • Culture Media, Serum-Free
  • Receptors, Vitronectin
  • Silanes
  • Phosphotyrosine