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Carcinogenesis Advance Access published online on September 10, 2008
Carcinogenesis, doi:10.1093/carcin/bgn217
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

The basic C-terminal amino acids of calcium-binding protein S100A4 promote metastasis

Thamir Ismail, David G Fernig, Philip S. Rudland, Carla J Terry, Guozheng Wang and Roger Barraclough*

Cancer and Polio Research Fund Laboratories, Biosciences Building, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK

* To whom correspondence and proofs should be addressed : Dr R. Barraclough, Biosciences Building, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK. e-mail: brb{at}liv.ac.uk, Tel.: 44 151 795 4469, Fax: 44 151 795 4406.

The calcium-binding protein, S100A4 can induce a metastatic phenotype in animal model systems and its expression in various human cancers has been shown to be associated with metastasis and reduced patient survival. Using a series of nested deletion mutants, it is now shown that the two C-terminal lysine residues are required for the enhanced metastasis, invasion and migration abilities that S100A4 confers on cells in a model system of metastasis. Basic C-terminal residues enhance the affinity between S100A4 and its best characterised target, a recombinant C-terminal fragment of non-muscle myosin II heavy chain, isoform A. In wild type S100A4 protein, the presence of the C-terminal lysine, residue 101, enhances the rate of association between S100A4 and non-muscle myosin II heavy chain, isoform A. These results identify the amino acids of S100A4 that are involved in metastasis induction and show that the C-terminal region of S100A4 is a possible target for inhibitors of its metastatic action.

Key Words: breast cancer • metastasis • calcium-binding proteins • S100A4 • myosin II

Received June 16, 2008; revised August 15, 2008; accepted September 6, 2008.


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