Journal
BIOPHYSICAL JOURNAL
Volume 96, Issue 6, Pages L39-L41Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2009.01.005
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Funding
- National Institutes of Health [PN2 EY016586]
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Integrin-cadherin cross talk is an important aspect of cell function. We explored this signaling using substrates micropatterned with islands of fibronectin surrounded by E-cadherin, capturing the segregation of these signals in normal tissue. While MDCK cells were able to concurrently form adhesive structures with these two proteins, engagement of fibronectin by MCF-7 cells, an adenocarcinoma cell line, inhibited response of these cells to E-cadherin. We further demonstrated that this inhibition is rigidity dependent; on soft elastomer substrates with Young's modulus in the range of tens of kiloPascals, MCF-7 cells were able to engage both integrin and cadherin ligands.
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