Pharmacological inhibition of the vitronectin receptor abrogates PDGF-BB-induced hepatic stellate cell migration and activation in vitro

J Hepatol. 2007 May;46(5):878-87. doi: 10.1016/j.jhep.2006.11.011. Epub 2006 Dec 12.

Abstract

Background/aims: Activated hepatic stellate cells (HSC) play a central role in the development of liver fibrosis. Platelet-derived growth factor (PDGF)-BB and the integrin alphavbeta3 mediate mesenchymal cell migration and proliferation. However, their contribution and interaction during fibrogenic activation of HSC remains unclear. To this aim we investigated if PDFGF-BB and alphavbeta3 interact, and how far small molecular inhibitors of alphavbeta3 modulate PDGF-BB and serum-induced migration, proliferation and fibrogenic activation of HSC.

Methods: Rat and human HSC were subjected to migration and proliferation assays in the presence or absence of a peptide or a nonpeptide alphavbeta3 inhibitor. Activation of mitogen-activated protein kinases (ERK1/2, p38), Akt, focal adhesion kinase (FAK), paxillin and beta3 integrin was evaluated by phospho-specific Western blotting. Fibrosis related transcripts were determined by quantitative real-time PCR.

Results: PDGF-BB-stimulated HSC migration which was blocked dose-dependently by the alphavbeta3 antagonists, with complete inhibition at 10(-6)M. alphavbeta3 blockage did not affect cell viability or proliferation, while it decreased phosphorylation of FAK, paxillin, beta3 integrin and p38, but not of ERK1/2 or Akt. alphavbeta3 inhibition led to downregulation of certain profibrogenic transcripts, while it upregulated fibrolytic MMP-13 mRNA.

Conclusions: Inhibition of integrin alphavbeta3 leads to abrogation of migration of HSC stimulated with PDGF-BB and to an antifibrogenic gene expression pattern.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Becaplermin
  • Cell Adhesion / drug effects
  • Cell Adhesion / physiology
  • Cell Movement / drug effects
  • Cell Movement / physiology*
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Down-Regulation
  • Focal Adhesion Kinase 1 / metabolism
  • Gene Expression Regulation / drug effects
  • Hepatocytes / cytology
  • Hepatocytes / drug effects
  • Hepatocytes / metabolism*
  • Humans
  • Integrin alphaVbeta3 / antagonists & inhibitors*
  • Integrin alphaVbeta3 / metabolism*
  • Liver / cytology
  • Liver / drug effects
  • Liver / growth & development
  • Liver / metabolism
  • Male
  • Paxillin / metabolism
  • Peptides, Cyclic / pharmacology
  • Phosphoproteins / metabolism
  • Platelet-Derived Growth Factor / pharmacology
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Proto-Oncogene Proteins c-sis
  • RNA, Messenger / genetics
  • Rats
  • Rats, Wistar
  • Signal Transduction / drug effects
  • Snake Venoms

Substances

  • Integrin alphaVbeta3
  • Paxillin
  • Peptides, Cyclic
  • Phosphoproteins
  • Platelet-Derived Growth Factor
  • Proto-Oncogene Proteins c-sis
  • RNA, Messenger
  • Snake Venoms
  • Becaplermin
  • Cilengitide
  • Protein-Tyrosine Kinases
  • Focal Adhesion Kinase 1
  • PTK2 protein, human
  • Protein Serine-Threonine Kinases