| Abstract | Cell-ECM interactions play a significant role in cancer cell proliferation, growth, adhesion, and migration. Integrin αvβ6 has been implicated in numerous cancers for promoting tumor development via interactions with the ECM. It is overexpressed in MDA-MB-468 TNBC breast cancer cells, but not in MDA-MB-231 breast cancer cells. Both cell lines have vastly different structures. The role of the integrin in MDA-MB-468 cells’ structure and adhesion was assessed by suppressing its function using siRNAs, CRISPR, and antibody blocking methods. Preliminary results indicated that the change in structure in the 231 cell line was not caused by the lack of this integrin, and that the integrin was indeed required for cell-cell adhesion in the 468 cell line. In addition, interactions between ECM proteins fibrinogen, fibronectin, and collagen and signaling kinases FAK and SRC were assessed in prostate cancer cell lines DU145 and PC3. Both cell lines were seen to respond differently to the proteins, indicating key differences between the signaling pathways between the cell lines.
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