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Expression Profile of Epithelial Protein Lost in Neoplasm-Alpha (EPLIN-α) in Human Pulmonary Cancer and Its Impact on SKMES-1 Cells in vitro

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DOI: 10.4236/jct.2012.324058    3,091 Downloads   5,007 Views   Citations

ABSTRACT

Epithelial Protein Lost in Neoplasm (EPLIN) is a cytoskeletal associated protein implicated in regulating actin dynamoics and cellular motility and whose expression is frequently downregulated in a number of human cancers. The current study examined the expression levels of EPLIN-α in a pulmonary cancer cohort and its association with clinical pathological factors using quantitative polymerase chain reaction. Additionally, EPLIN-α was over-expressed in the SKMES-1 pulmonary cancer cell line through transfection with a plasmid containing the expression sequence for EPLIN-α. The role of EPLIN-α was subsequently examined using a variety of in vitro functional assays. Decreased levels of EPLIN-α were seen in cancerous tissues compared to normal background tissue. Lower levels of EPLIN-α were also associated with higher TNM stage and nodal involvement. In vitro over-expression of EPLIN-α inhibited SKMES-1 growth rates (p = 0.05 vs. plasmid control) and motility (p = 0.002 vs. plasmid control), though did not have any significant effects on cell-matrix adhesion or cell invasion. Taken together, the current study indicates that lower levels of EPLIN-α may be associated with poorer prognosis and more advanced pulmonary cancer, where this molecule appears to play a suppressive role on cell growth and migration.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Y. Liu, A. Sanders, L. Zhang and W. Jiang, "Expression Profile of Epithelial Protein Lost in Neoplasm-Alpha (EPLIN-α) in Human Pulmonary Cancer and Its Impact on SKMES-1 Cells in vitro," Journal of Cancer Therapy, Vol. 3 No. 4A, 2012, pp. 452-459. doi: 10.4236/jct.2012.324058.

References

[1] Y. Song, R. E. Maul, C. S. Gerbin and D. D. Chang, “Inhibition of Anchorage-Independent Growth of Transformed NIH3T3 Cells by Epithelial Protein Lost in Neoplasm (EPLIN) Requireslocalization of EPLIN to Actin Cytoskeleton,” Molecular Biology of the Cell, Vol. 13, No. 4, 2002, pp. 1408-1416. doi:10.1091/mbc.01-08-0414
[2] R. S. Maul, Y. Song, K. J. Amann, S. C. Gerbin, T. D. Pollard and D. D. Chang, “EPLIN Regulates Actin Dynamics by Cross-Linking and Stabilizing Filaments,” The Journal of Cell Biology, Vol. 160, No. 3, 2003, pp. 399-407. doi:10.1083/jcb.200212057
[3] K. Abe and M. Takeichi, “EPLIN Mediates Linkage of the Cadherin-Catenin Complex to F-Actin and Stabilizes the Circumferential Actin Belt,” Proceedings of the National Academy of Sciences, Vol. 105, No. 1, 2008, pp.13-19. doi:10.1073/pnas.0710504105
[4] D. D. Chang, N.-H. Park, C. T. Denny, S. F. Nelson and M. Pe, “Characterization of Transformation Related Genes in Oral Cancer Cells,” Oncogene, Vol. 16, No. 15, 1998, pp. 1921-1930. doi:10.1038/sj.onc.1201715
[5] W. G. Jiang, T. A Martin, J. M. Lewis-Russell, A. Douglas-Jones, L. Ye and R. E. Mansel, “Eplin-Alpha Expression in Human Breast Cancer, the Impact on Cellular Migration and Clinical Outcome,” Molecular Cancer, Vol. 7, 2008, pp. 71-80. doi:10.1186/1476-4598-7-71
[6] A. J. Sanders, T. A. Martin, L. Ye, M. D. Mason and W. G. Jiang, “EPLIN Is a Negative Regulator of Prostate Cancer Growth and Invasion,” Journal of Urology, Vol. 186, No. 1, 2011, pp. 295-301. doi:10.1016/j.juro.2011.03.038
[7] Y. Liu, A. J. Sanders, L. Zhang and W. G. Jiang, “EPLIN-Alpha Expression in Human Oesophageal Cancer and Its Impact on Cellular Aggressiveness and Clinical Outcome,” Anticancer Research, Vol. 32, No. 4, 2012, pp. 1283-1289.
[8] R. S. Maul and D. D. Chang, “EPLIN, Epithelial Protein Lost in Neoplasm,” Oncogene, Vol. 18, No. 54, 1999, pp. 7838-7841. doi:10.1038/sj.onc.1203206
[9] S. Chen, R. S. Maul, H. R. Kim and D. D. Chang, “Characterization of the Human EPLIN (Epithelial Protein Lost in Neoplasm) Gene Reveals Distinct Promoters for the Two EPLIN Isoforms,” Gene, Vol. 248, No. 1-2, 2000, pp. 69-76. doi:10.1016/S0378-1119(00)00144-X
[10] M. Chircop, V. Oakes, M. E. Graham, M. P. Ma, C. M. Smith, P. J. Robinson and K. K Khanna, “The Actin-Binding and Bundling Protein, EPLIN, Is Required for Cytokinesis,” Cell Cycle, Vol. 8, No. 5, 2009, pp. 757-764. doi:10.4161/cc.8.5.7878
[11] S. Zhang, X. Wang, A. O. Osunkoya, S. Iqbal, Y. Wang, Z. Chen, S. Muller, S. Josson, I. M. Coleman, P. S. Nelson, Y. A. Wang, R. Wang, D. M. Shin, F. F. Marshall, O. Kucuk, W. L.Chung, H. E. Zhau and D. Wu, “EPLIN Downregulation Promotes Epithelial-Mesenchymal Transition in Prostate Cancer Cells and Correlates with Clinical Lymph Node Metastasis,” Oncogene, Vol. 30, No. 50, 2011, pp. 4941-4952. doi:10.1038/onc.2011.199
[12] M. Y. Han, H. Kosako, T. Watanabe and S. Hattori, “Extracellular Signal-Regulated Kinase/Mitogen-Activated Protein Kinase Regulates Actin Organization and Cell Motility by Phosphorylating the Actin Cross-Linking Protein EPLIN,” Molecular and Cellular Biology, Vol. 27, No. 23, 2007, pp. 8190-8204. doi:10.1128/MCB.00661-07
[13] A. J. Sanders, L. Ye, M. D. Mason and W. G. Jiang, “The Impact of EPLINα (Epithelial Protein Lost in Neoplasm) on Endothelial Cells, Angiogenesis and Tumorigenesis,” Angiogenesis, Vol. 13, No. 4, 2010, pp. 317-326. doi:10.1007/s10456-010-9188-7

  
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