Journal Article

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

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

in Carcinogenesis

Volume 29, issue 12, pages 2259-2266
Published in print December 2008 | ISSN: 0143-3334
Published online September 2008 | e-ISSN: 1460-2180 | DOI:
The basic C-terminal amino acids of calcium-binding protein S100A4 promote metastasis

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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 characterized target, a recombinant C-terminal fragment of non-muscle myosin II heavy chain isoform A (NMMHC-IIA). In wild-type S100A4 protein, the presence of the C-terminal lysine, residue 101, enhances the rate of association between S100A4 and NMMHC-IIA. 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.

Journal Article.  7702 words.  Illustrated.

Subjects: Clinical Cytogenetics and Molecular Genetics

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