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.
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
Mol. Cell
Date: May. 01, 2003
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