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Alpha v beta 5 integrin-dependent programmed cell death triggered by a peptide mimic of annexin V.

The diverse cytoplasmic domain sequences within the various integrin subunits are critical for integrin-mediated signaling into the cell (outside-in signaling) and for activation of ligand binding affinity (inside-out signaling). Here we introduce an approach based on phage display technology to identify molecules that specifically interact with the cytoplasmic domain of the beta 5 integrin subunit. We show that a peptide selected for binding specifically to the beta 5 cytoplasmic domain (VVISYSMPD) induces apoptosis upon internalization. The cell death process induced by VVISYSMPD is sensitive to modulation by growth factors and by protein kinase C (PKC), and it cannot be triggered in beta 5 null cells. Finally, we show that the VVISYSMPD peptide is a mimic of annexin V. Our results suggest a functional link between the alpha v beta 5 integrin, annexin V, and programmed cell death. We propose the term "endothanatos" to designate this phenomenon.

Pubmed ID: 12769841

Authors

  • Cardó-Vila M
  • Arap W
  • Pasqualini R

Journal

Molecular cell

Publication Data

May 28, 2003

Associated Grants

  • Agency: NCI NIH HHS, Id: CA91134

Mesh Terms

  • Amino Acid Sequence
  • Annexin A5
  • Apoptosis
  • Cell Adhesion
  • Cell Line
  • Cell Membrane
  • Eukaryotic Cells
  • Genetic Vectors
  • Growth Substances
  • Humans
  • Integrins
  • Molecular Mimicry
  • Molecular Sequence Data
  • Peptides
  • Protein Kinase C
  • Protein Structure, Tertiary
  • Receptors, Vitronectin
  • Signal Transduction