| Autor: |
Ismail TM; Cancer and Polio Research Fund Laboratories, Biosciences Building, University of Liverpool, Liverpool, UK., Fernig DG, Rudland PS, Terry CJ, Wang G, Barraclough R |
| Jazyk: |
angličtina |
| Zdroj: |
Carcinogenesis [Carcinogenesis] 2008 Dec; Vol. 29 (12), pp. 2259-66. Date of Electronic Publication: 2008 Sep 10. |
| DOI: |
10.1093/carcin/bgn217 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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