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http://dx.doi.org/10.5352/JLS.2017.27.3.267

Cyanate Induces Apoptosis of Rat Glioma Cell Line  

Choi, Hye-Jung (Department of Emergency Medical Technology, Gyeongbuk Provincial College)
Lee, Sang-Hee (Department of Emergency Medical Technology, Gyeongbuk Provincial College)
Publication Information
Journal of Life Science / v.27, no.3, 2017 , pp. 267-274 More about this Journal
Abstract
The patient with end-stage renal disease show several nervous complications. The factors contributing to the nervous complications are still incompletely characterized. Cyanate, known as one of the uremic toxins, is derived spontaneously from urea. To investigate the mechanism of cyanate-induced effect on C6 glioma cells, the glioma cells were treated with 0, 1, 5, 10, 20 and 40 mM cyanate. There was a dose-dependent decrease in cell viability and the decreased number of cell was observed in glioma cells by treatment with cyanate. Western blot showed the down- regulation of procaspase-3, which means up-regulation of caspase-3, and the up-regulation of caspase-8, but the down-regulation by cyanate. In addition, cDNA microarray showed 934 down-regulated genes and 165 up-regulated genes on 1,099 genes in cyanate treated group. Treatment with cyanate led to 16 down-regulated genes and 6 up-regulated genes on apoptosis category, and especially heat shock 70 kD protein 1A gene on the category of apoptosis was significantly up-regulated. These results suggest that cyanate can induce apoptosis through caspase-8 and caspase-3 in glioma cells and decrease of gene expression including apoptosis category in glioma cells. These effects of cyanate may play a role in the nervous complications of patient with end-stage renal disease.
Keywords
Apoptosis; cyanate; end-stage renal disease; glioma cell; nervous complications;
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1 Kimani, S., Sinei, K., Bukachi, F., Tshala-Katumbay, D. and Maitai, C. 2014. Memory deficits associated with sublethal cyanide poisoning relative to cyanate toxicity in rodents. Metab. Brain Dis. 29, 105-112.   DOI
2 Kraus, L. M. and Kraus, A. P. 2001. Carbamylation of amino acids and proteins in uremia. Kidney Int. 78, S102-S107.
3 Lim, J. B., Kim, H. S., Park, Q., Lee, S. K., Park, Y. B. and Han, C. T. 1999. Clinical significance of anti-HSP 70 antibody in the patients with systemic lupus erythematosus. Kor. J. Clin. Pathol. 19, 548-553.
4 Liu, Q., Zhou, Y. H., Xuan, B., Chiou, G. C. and Okawara, T. 2000. Effect of interleukin-1 blocks on corneal fibroblast proliferation in vitro and ocular inflammation in vivo. J. Ocul. Pharmacol. Ther. 16, 81-96.   DOI
5 Majno, G. and Joris, I. 1995. Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol. 146, 3-15.
6 Miller, L. K. 1999. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9, 323-328.   DOI
7 Mun, K. C., Yeo, M. Y., Kim, S. P., Kim, H. C. and Kwak, C. S. 2000. Chronic peritoneal inflammation by cyanate in rats. Perit. Dial. Int. 20, 699-702.
8 Park, K. D., Mun, K. C., Chang, E. J., Park, S. B. and Kim, H. C. 2004. Inhibition of erythropoietin activity by cyanate. Scand. J. Urol. Nephrol. 38, 69-72.
9 Roxborough, H. E., Miller, C. A., McEneny, J. and Young, I. S. 1995. Carbamylation inhibits the ferroxidase activity of caeruloplasmin. Biochem. Biophys. Res. Commun. 214, 1073-1078.   DOI
10 Sasaki, H., Sheng, Y., Kotsuji, F. and Tsang, B. K. 2000. Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells. Cancer Res. 60, 5659-5666.
11 The Korean society of nephrology. 2001. Clinical nephrology, pp. 593-641, Kwangmoon Publisher, Korea.
12 Dalia, E. G., Shailaja, P. R., Michael, H., Seth, H., Johannes, H., Martin, G., Christian, W., Aadrijana, K., Sasa, F., Rudolf, S., Rufina, S., Akos, H. and Gunther, M. 2014. The urea decomposition product cyanate promotes endothelial dysfunction. Kidney Int. 86, 923-931.   DOI
13 Williams, G. T. 1994. Apoptosis in the immune system. J. Pathol. 173, 1-4.   DOI
14 Yang, D. H. 2006. Dialysis therapy. Available from: URL: http://www.yakup.com/pharminfo/pharminfo2006-10-01.php
15 Yang, E. J. and Chang, J. H. 2011. Potassium cyanate induces apoptosis of humans colorectal cancer cell via mitochondrial pathway. J. Exp. Biomed. Sci. 17, 177-184.
16 Ahn, B. G., Kim, W. S. and Kwon, J. Y. 2006. The effects of propofol and sevoflurane on neuronal apoptosis and Bcl-2 family protein expression after transient forebrain ischemia in the rat. Kor. J. Anesthesioly 51, 614-621.   DOI
17 Arai, T. and Kino, I. 1995. Role of apoptosis in modulation of the growth of human colorectral tubular and villous adenomas. J. Pathol. 176, 37-44.   DOI
18 Graham, S. H. and Chen, J. 2001. Programmed cell death in cerebral ischemia. J. Cereb. Blood Flow Metab. 21, 99-109.   DOI
19 Hengartner, M. O. 2000. The biochemistry of apoptosis. Nature 407, 770-776.   DOI
20 Hwang, E. A. 2004. Apoptosis by cyanate in osteoblast. Ph.D. dissertation, Keimyung University, Daegu, Korea.
21 Kamesaki, H. 1998. Mechanism involved in chemotherapy induced apoptosis and their implications in cancer chemotherapy. Int. J. Hematol. 68, 29-43.   DOI
22 Kim, J. Y., Kim, Y. S., Hong, K. Y., Eo, W. K. and Choi, Y. S. 2007. Apoptosis by cyanate in kidney mesangial cell. Kosin Med. J. 22, 160-169.
23 Kerr, J. F. and Searle, J. 1972. A suggested explanation for the paradoxically slow growth rate of basal cell carcinomas that contain numerous mitotic figures. J. Pathol. 107, 41-44.   DOI