Abstract
Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase and a major phosphotyrosine-containing protein. FAK is found in cell-matrix attachment sites (focal adhesions), and is activated on integrin-ligand binding and by other signaling pathways. Several roles have been proposed for FAK; here we report a novel function. We observed abundant FAK protein in all human melanoma cell lines tested except COLO839, a line that grows predominantly in suspension and was derived from peripheral blood. Five adherent lines, isolated from solid metastases in the same patient as COLO839, did express FAK. We derived four adherent sublines from COLO839. These did express FAK, even when plated on bacteriological plastic, to which they did not adhere. Thus, substrate attachment was not required for FAK expression. Three of the adherent sublines were then grown in the presence of antisense oligonucleotides to the initial FAK coding sequence. All showed substantially reduced FAK expression and, interestingly, the cells largely detached from the substrate while continuing to grow. Similar results were obtained with an independent melanoma line, DX3. Thus, FAK expression appears to be required by melanoma cells for substrate adhesion.
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Acknowledgements
We are greatly indebted to George Moore, Meenhard Herlyn, lan Hart and Bernard Souberbielle for melanoma cell lines. This work was supported by Cancer Research Campaign Grant no. SP 1923/0503.
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Maung, K., Easty, D., Hill, S. et al. Requirement for focal adhesion kinase in tumor cell adhesion. Oncogene 18, 6824–6828 (1999). https://doi.org/10.1038/sj.onc.1203094
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DOI: https://doi.org/10.1038/sj.onc.1203094
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