Background
Integrin-linked kinase (ILK) is a serine-threonine kinase that regulates interactions
between the cell and the extracellular matrix. In many cancers, overexpression of
ILK leads to increased cell proliferation, motility, and invasion. We hypothesized
that ILK functions as a regulator of viability and migration in thyroid cancer cells.
Methods
Eleven human thyroid cancer cell lines were screened for ILK protein expression. The
cell lines with the greatest expression were treated with either ILK small interfering
RNA (siRNA) or a novel ILK inhibitor, T315, and the effects were evaluated via Western
blot and migration assay. 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium
bromide assays were performed to assess cell viability.
Results
siRNA against ILK decreased phosphorylation of downstream effectors Akt and MLC, as
well as decreased migration. Treatment with T315 showed a dose-related decrease in
both Akt and MLC phosphorylation, as well as decreased migration. 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium
bromide assays showed T315 to have an half maximal inhibitory concentration of less
than 1 μM in cell lines with high ILK expression.
Conclusion
ILK is expressed differentially in thyroid cancer cell lines. Both ILK siRNA and T315
inhibit motility of thyroid cancer cell lines, and T315 is shown to be cytotoxic at
low concentrations. Altogether, our study suggests that ILK may represent an important
kinase in aggressive thyroid cancers.
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Article info
Publication history
Published online: November 05, 2015
Accepted:
October 14,
2015
Identification
Copyright
© 2016 Elsevier Inc. Published by Elsevier Inc. All rights reserved.
