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Overexpression of selenoprotein SelK in BGC-823 cells inhibits cell adhesion and migration

Biochemistry (Moscow) volume 80, pages 1344–1353 (2015)Cite this article

Abstract

Effects of human selenoprotein SelK on the adhesion and migration ability of human gastric cancer BGC-823 cells using Matrigel adhesion and transwell migration assays, respectively, were investigated in this study. The Matrigel adhesion ability of BGC-823 cells that overexpressed SelK declined extremely significantly (p < 0.01) compared with that of the cells not expressing the protein. The migration ability of BGC-823 cells that overexpressed SelK also declined extremely significantly (p < 0.01). On the other hand, the Matrigel adhesion ability and migration ability of the cells that overexpressed C-terminally truncated SelK did not decline significantly. The Matrigel adhesion ability and migration ability of human embryonic kidney HEK-293 cells that overexpressed SelK did not show significant change (p > 0.05) with the cells that overexpressed the C-terminally truncated protein. In addition to the effect on Matrigel adhesion and migration, the overexpression of SelK also caused a loss in cell viability (as measured by 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H tetrazolium bromide (MTT) colorimetric assay) and induced apoptosis as shown by confocal microscopy and flow cytometry. The cytosolic free Ca2+ level of these cells was significantly increased as detected by flow cytometry. But the overexpression of SelK in HEK-293 cells did not cause either significant loss in cell viability or apoptosis induction. Only the elevation of cytosolic free Ca2+ level in these cells was significant. Taken together, the results suggest that the overexpression of SelK can inhibit human cancer cell Matrigel adhesion and migration and cause both the loss in cell viability and induction of apoptosis. The release of intracellular Ca2+ from the endoplasmic reticulum might be a mechanism whereby the protein exerted its impact. Furthermore, only the full-length protein, but not C-terminally truncated form, was capable of producing such impact. The embryonic cells were not influenced by the elevation of free Ca2+ level in cytosol, probably due to their much greater tolerance to the variation.

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Abbreviations

BGC-823:

human gastric cancer cell line

DU145 and PC3:

human prostatic carcinoma cell lines

FITC:

fluorescein isothiocyanate

HEK-293:

human embryonic kidney cell line

LNCaP:

lymph node carcinoma of prostate

MTT:

3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H tetrazolium bromide

SelS:

-T, -N, -K are selenoproteins S, T, N, K

Sep15:

15-kDa selenoprotein

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Authors and Affiliations

  1. School of Life Science, Liaoning University, Shenyang, 110036, China

    S. B. Ben, B. Peng, G. C. Wang & H. F. Gu

  2. Departments of Pediatrics and Medicine, University of Colorado School of Medicine, Aurora, CO, USA

    S. B. Ben & H. Jiang

  3. School of Pharmaceutical Science, Liaoning University, Shenyang, 110036, China

    C. Li, X. L. Meng & C. L. Chen

  4. Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, 151-742, Korea

    B. J. Lee

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  1. S. B. Ben
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Correspondence to C. L. Chen.

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Ben, S.B., Peng, B., Wang, G.C. et al. Overexpression of selenoprotein SelK in BGC-823 cells inhibits cell adhesion and migration. Biochemistry Moscow 80, 1344–1353 (2015). https://doi.org/10.1134/S0006297915100168

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  • DOI: https://doi.org/10.1134/S0006297915100168

Keywords

  • selenoprotein
  • SelK
  • cancer cells
  • adhesion
  • migration
  • calcium homeostasis