Fibronectin binding promotes a PKC-dependent modulation of NF-κB in human T cells

A. Bearz, G. Tell, A. Colombatti, S. Formisano, C. Pucillo

Research output: Contribution to journalArticlepeer-review


NF-κB was identified as one of the transcription factors leading to antigen-independent stimulation through activation of integrin receptors. This effect was dependent upon stimulation of a α4β1 and α5β1 integrins, the major fibronectin-binding integrins of Jurkat T cells, since either RGD or CS-1 peptides at 10-4 M could prevent NF-κB activation. At variance with fibroblasts and smooth muscle cells, in which only p50 and p65 components of the NF-κB complex are induced, adhesion of T cells to fibronectin resulted in a strong upregulation of p50 and c-Rel and in a partial increase in p65 activity. The upregulation of NF-κB activity was abrogated by calphostin C, an inhibitor of protein kinase C. Cell adhesion determined a strong reduction in the cytoplasmic levels of the NF-κB inhibitor IκBα, reduction that was prevented after treatment with calphostin C, suggesting that PKC-dependent IκBα phosphorylation might be involved in the upregulation of NF-κB.

Original languageEnglish
Pages (from-to)732-737
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - Feb 24 1998

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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