Conflict of interest: None.
CXCL14 enhances proliferation and migration of NCI-H460 human lung cancer cells overexpressing the glycoproteins containing heparan sulfate or sialic acid†
Article first published online: 14 MAR 2013
Copyright © 2012 Wiley Periodicals, Inc.
Journal of Cellular Biochemistry
Volume 114, Issue 5, pages 1084–1096, May 2013
How to Cite
Park, C. R., You, D.-J., Kim, D.-K., Moon, M. J., Lee, C., Oh, S.-H., Ahn, C., Seong, J. Y. and Hwang, J.-I. (2013), CXCL14 enhances proliferation and migration of NCI-H460 human lung cancer cells overexpressing the glycoproteins containing heparan sulfate or sialic acid. J. Cell. Biochem., 114: 1084–1096. doi: 10.1002/jcb.24449
- Issue published online: 14 MAR 2013
- Article first published online: 14 MAR 2013
- Accepted manuscript online: 13 NOV 2012 08:46AM EST
- Manuscript Accepted: 1 NOV 2012
- Manuscript Received: 13 SEP 2012
- National Research Foundation of Korea. Grant Number: 2009-0073875
- HEPARAN SULFATE PROTEOGLYCAN;
- SIALIC ACID;
CXCL14 is a chemokine family member that is involved in various cellular responses in addition to immune cell activation. Although constitutive CXCL14 expression in normal epithelial cells may help protect against infection by activating immune systems, its expression in cancer cells has raised controversy regarding its possible role in tumorigenesis. However, the underlying mechanisms for this disparity remain unknown. Investigation of cellular CXCL14 binding properties might increase our understanding of the peptide's roles in tumorigenesis. In the present study, we found that CXCL14 binds to various cell types. Interestingly, binding to NCI-H460 cells was prevented by heparan sulfate and N-acetyl neuraminic acid. Next, we examined effect of CXCL14 binding in NCI-H460 and NCI-H23. CXCL14 enhanced proliferation and migration in NCI-H460 but had no effect on NCI-H23. A reporter gene assay with various transcription factor response elements revealed that only nuclear factor-κB (NF-κB) signaling was activated by CXCL14 in NCI-H460 cells, which was blocked by BAPTA-AM, TPCA-1, and brefeldin A. Exogenous expression of some glycoproteins such as syndecan-4, podoplanin, and CD43 in these cells enhanced CXCL14 binding and NF-κB activity. Collectively, these results demonstrate that CXCL14 binding to glycoproteins harboring heparan sulfate proteoglycans and sialic acids leads proliferation and migration of some cancer cells. J. Cell. Biochem. 114: 1084–1096, 2013. © 2012 Wiley Periodicals, Inc.