Effect of DRB on the biological characteristics of human laryngeal carcinoma Hep-2 cell line

Abstract

In order to study the effect of 5, 6-Dichloro-1-β-D-ribofuranosyl-benzimidazole (DRB) on the biological characteristics of human laryngeal carcinoma Hep-2 cell line in vitro, Hep-2 cells cultured in vitro were treated with different concentrations of DRB. Changes in cell proliferation, apoptotic rate and invasiveness were detected by MTT assay, flow cytometry (FCM) and matrigel in vitro invasion assay, respectively. It was found that DRB inhibited the proliferation of Hep-2 cells in a dose-and time-dependent manner. After being treated with 0, 10, 20, 40, 80 μmmol/L DRB for 24 h, the apoptotic rate in Hep-2 cells was (0.68±0.19)%, (1.95±0.12)%, (8.51±0.26)%, (11.26±0.17)% and (14.99±0.32)%, respectively. The matrigel in vitro invasion assay revealed that DRB began to inhibit the invasion of Hep-2 cells at the concentration of 5 μmmol/L, and with the increase of DRB concentration, the inhibitory effect was enhanced. It was suggested that DRB could influence the essential biological characteristics of Hep-2 cells, inhibit Hep-2 cells proliferation, reduce invasive ability and induce apoptosis of Hep-2 cells.

Keywords

protein-serine-threonine kinases / 5,6-Dichloro-1-β-D-ribofuranosyl-benzimidazole / laryngeal neoplasms / Hep-2 cell line

References

[1] PinnaL. A.. Protein kinase CK2: a challenge to canons. J Cell Sci, 2002, 115: 3873-3878

[2] ChannavajhalaP., SeldinD. C.. Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene, 2002, 21: 5280-5288

[3] FilholO., CochetC.. Protein kinase CK2 and cancer: further clues are accumulating. Bull Cancer, 2002, 89: 261-265

[4] McCafferyJ. D., GapanyM., FaustR. A., et al.. Nuclear matrix proteins as malignant markers in squamous cell carcinoma of the head and neck. Arch Otolaryngol Head Neck Surg, 1997, 123: 283-288

[5] UngerG. M., DavisA. T., SlatonJ. W., et al.. Protein kinase CK2 as regulator of cell survival: implication for cancer therapy. Curr Cancer Drug Targets, 2004, 4: 77-84

[6] FaustR. A., NiehansG., GapanyM., et al.. Subcellular immunolocalization of protein kinase CK2 in normal and carcinoma cells. Int J Biochem Cell Biol, 1999, 31: 941-949

[7] DanilewiczM., SikorskaB., Wagrowska-DanilewiczM.. Prognostic significance of the immunoexpression of matrix metalloproteinase MMP2 and its inhibitor TIMP2 in laryngeal cancer. Med Sci Monit, 2003, 9: MT42-47

[8] LiP. F., LiJ., MullerE. C., et al.. Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC. Mol Cell, 2002, 10: 247-258

[9] SlatonJ. W., UngerG. M., SloperD. T., et al.. Induction of apoptosis by antisense CK2 in human prostate cancer xenograft model. Mol Cancer Res, 2004, 2: 712-721