期刊
CARCINOGENESIS
卷 29, 期 12, 页码 2259-2266出版社
OXFORD UNIV PRESS
DOI: 10.1093/carcin/bgn217
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资金
- Cancer Research UK (Translational Committee) [C1440/A3019]
- Cancer and Polio Research Fund Ltd
- Biotechnology and Biological Sciences Research Council
- CASE [BBS/S/L/2003/10212]
- Breast Cancer Campaign [NGBU10]
- North West Cancer Research Fund [CR574]
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.
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