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Cell adhesion

New way to activate caspases

Nature volume 397, pages 479–480 (1999)Cite this article

Most cells need to be attached to a self-produced external meshwork known as the extracellular matrix in order to survive — without such anchorage they undergo apoptosis1. The cells attach through integrins, heterodimeric membrane proteins that link the intracellular cytoskeleton with the extracellular matrix. Many of the 25 or so known integrins recognize a tripeptide, arginine-glycine-aspartate (or RGD in single-letter code), in target proteins of the extracellular matrix2. And on page 534 of this issue, Buckley et al.3 provide a startling new interpretation for the role of these RGD peptides in apoptosis.

In vitro experiments have shown that small peptides containing the RGD motif bind to integrins and, when presented to a cell in a soluble form, inhibit cell attachment. According to current thinking, the peptide-blocked integrins cannot provide the signals that cells would receive from matrix-bound integrins, resulting in changes in cell shape and, ultimately, apoptosis1,4. Because RGD-based anti-thrombotic drugs are already in clinical use, and RGD drugs to treat osteoporosis and inhibit angiogenesis (the development of new blood vessels) are under development2, knowing how these peptides act is of considerable importance.

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Figure 1: The arginine-glycine-aspartate (RGD) peptide in apoptosis.

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  1. the Burnham Institute, 10901 North Torrey Pines Road, La Jolla, 92037, California, USA

    Erkki Ruoslahti & John Reed

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  1. Erkki Ruoslahti
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  2. John Reed
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Ruoslahti, E., Reed, J. New way to activate caspases. Nature 397, 479–480 (1999). https://doi.org/10.1038/17229

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