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Carcinogenesis Advance Access originally published online on March 14, 2006
Carcinogenesis 2006 27(9):1748-1757; doi:10.1093/carcin/bgl005
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5

Thomas C. Sroka, Michael E. Pennington and Anne E. Cress*

Department of Cell Biology and Anatomy, The University of Arizona Tucson, AZ 85724, USA

*To whom correspondence should be addressed. Tel: 520 626 7479; Fax: 520 626 4979; Email: acress{at}azcc.arizona.edu

Cell motility is partially dependent on interactions between the integrins and the extracellular matrix. Our previous studies have identified synthetic D-amino acid cell adhesion peptides using a combinatorial screening approach. In this study, we demonstrate that HYD1 (kikmviswkg) completely blocks random haptotactic migration and inhibits invasion of prostate carcinoma cells on laminin-5. This effect is adhesion independent and reversible. The inhibition of migration by HYD1 involves a dramatic remodeling of the actin cytoskeleton resulting in increased stress fiber formation and actin colocalization with cortactin at the cell membrane. HYD1 interacts with {alpha}6ß1 (not {alpha}6ß4) and {alpha}3ß1 integrins and surprisingly elevates laminin-5-dependent intracellular signals including focal adhesion kinase, mitogen-activated protein kinase kinase and extracellular signal-regulated kinase. HYD1 does not contain a previously characterized binding sequence for integrins. A scrambled derivative of HYD1, called HYDS (wiksmkivkg), does not interact with the {alpha}6 or {alpha}3 integrin subunits and is not biologically active. Taken together, these results indicate that HYD1 is a biologically active integrin-targeting peptide that reversibly inhibits tumor cell migration on laminin-5 and uncouples phosphotyrosine signaling from cytoskeletal-dependent migration.


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