Phorbol ester-induced migration of HepG2 cells is accompanied by intensive stress fibre formation, enhanced integrin expression and transient down-regulation of p21-activated kinase 1

Annamaária Gujdaár, Szabolcs Sipeki, Erzseébet Bander, Laászlo÷ Buday, Anna Farago÷

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Previously, we observed that phorbol ester induced more intensive scattering of HepG2 human hepatoma cells than hepatocyte growth factor (HGF). Regulatory components accounting for this intensive migration were studied. Phorbol ester-activated protein kinase C induced the early appearance of a great number of actin stress fibres. Whereas in response to HGF, the activation of phosphatidylinositol 3-kinase initiates the rearrangements of the actin cytoskeleton, in phorbol ester-treated cells, the activation of this enzyme was not required to the actin polymerisation. Activation of Erk1/Erk2 MAP kinases that was essential to the migration had a key role in enhancing the adherence of cells to the extracellular matrix via the increased expression of integrins α2, α6 and β1. Protein kinase C stimulated the activation of p21-activated kinase (PAK), as well. However, it also stimulated the selective and transient down-regulation of PAK1, which coincided with the formation of stress fibres.

Original languageEnglish
Pages (from-to)307-318
Number of pages12
JournalCellular Signalling
Volume15
Issue number3
DOIs
Publication statusPublished - Mar 1 2003

Keywords

  • Cell migration
  • HepG2 cells
  • Integrin expression
  • PAK activation
  • PAK1 down-regulation
  • Protein kinase C
  • Rho activation
  • Stress fibre

ASJC Scopus subject areas

  • Cell Biology

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