Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Effect of Cellular Zinc on the Regulation of C2-ceramide Induced Apoptosis in Mammary Epithelial and Macrophage Cell Lines

  • Han, S.E. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Lee, H.G. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Yun, C.H. (International Vaccine Institute) ;
  • Hong, Z.S. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Kim, S.H. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Kang, S.K. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Kim, S.H. (Departments of Biology, Kyung Hee University) ;
  • Cho, J.S. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Ha, S.H. (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University) ;
  • Choi, YunJaie (Department of Animal Science and Biotechnology, School of Agricultural Biotechnology Seoul National University)
  • Received : 2005.02.11
  • Accepted : 2005.07.12
  • Published : 2005.12.01
Download PDF
⟨ Previous Next ⟩

Abstract

Zinc is a trace element that is associated with a stimulation of immune function and regulation of ion balance for livestock production. In this study, the effect of zinc as inhibitor to apoptosis-induced cells was examined in vitro using mammary epithelial cell line, HC11 and macrophage cell line, NCTC3749. Cell viability, measured by MTT assay, indicated that 10 g/ml of zinc had a negative impact on cellular activity and 50 ng/ml was chosen for further testing. Apoptosis was induced in cells treated with C2-ceramide in serum-free media. DNA fragmentation and gene expression of acidic sphingomyelinase (a gene responsible for the progress of apoptosis) were distinctively low in zinc treated cells compared with those in non-treated controls. In conclusion, zinc is involved in the regulation of cell proliferation and apoptosis in mammary epithelial cells and macrophages.

Keywords

References

  1. Aiuchi, T., S. Mihara, M. Nakaya, Y. Masuda, S. Nakajo and K. Nakaya. 1998. Zinc ions prevent processing of caspase-3 during apoptosis induced by geranylgeraniol in HL-60 cells. J. Biochem. 124:300-303.
  2. Chai, F., A. Q. Truong-Tan and L. H. Ho. 1999. Regulation of caspase activation and apoptosis by cellular zinc deprivation: a review. Immunol. Cell Biol. 77:272-278.
  3. Duan, R. D., L. Nyberg and A. Nilsson. 1995. Alkaline sphingomyelinase activity in rat gastrointestinal tract: distribution and characteristics. Biochim. Biophys. Acta. 1259:49-55.
  4. Filipe, P. M., A. C. Fernandes and C. F. Manso. 1995. Effects of zinc on copper-induced and spontaneous lipid peroxidation. Biol. Trace Elem. Res. 47:51-56.
  5. Kerr, J. F. R., J. Searle, B. V. Harmon and C. J. Bishop. 1987. Apoptosis. (Ed. C. S. Potten) Perspectives of Mammalian Cell Death. Oxford University Press Oxford. pp. 93-128.
  6. Kim, S. H., S. C. Kim, Y. J. Kho, S. W. Kwak, H. G. Lee, S. K. You, J. H. Woo and Y. J. Choi. 2004. C2-ceramide as a cell death inducer in HC11 mouse mammary epithelial cells. Cancer Lett. 203:191-7.
  7. Lina, M., M. Corinne, A. Linda and A. Yusuf. 1993. Programmed cell death induced by ceramide. Sci. 259:1769-1771.
  8. Liu, X., H. Zou, C. Slaughter and X. Wang. 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184.
  9. Perry, D. K., M. J. Smyth, H. R. Stennicke, G. S. Salvesen, P. Duriez, G. G. Pirier and Y. A. Hannun. 1997. Zinc is a potent inhibitor of the apoptotic protease caspase-3: a novel target for zinc in the inhibition of apoptosis. J. Biol. Chem. 272:18530-18533.
  10. Shanker, A. H. and A. S. Prasad. 1998. Zinc and immune function: the biological basis of altered resistance to infection. Am. J. Clin. Nutr. 68(suppl):447S-463S.
  11. Spence, M. W., D. M. Byers, F. B. Palmer and H. W. Cook. 1989. A new Zn$^{2+}$-stimulated sphingomyelinase in fetal bovine serum. J. Biol. Chem. 264:5358-5363.
  12. Vaux, D. L. and A. Strasser. 1996. The molecular biology of apoptosis. Proc. Natl. Acad. Sci. USA 93:2239-2244.
  13. Wang, Y. Z., Z. R. Xu, W. X. Lin, H. Q. Huang and Z. Q. Wang. 2004. Developmental gene expression of antimicrobial peptide PR-39 and effect of zinc oxide on gene regulation of PR-39 in piglets. Asian-Aust. J. Anim. Sci. 17(12):1635-1640.
  14. Wolf, C. M. and A. Eastman. 1999. The temporal relationship between protein phosphate, mitochondrial cytochrome C release, and caspase activation in apoptosis. Exp. Cell Res. 247:505-513.
  15. Wyllie, A. H. 1997. Apoptosis: an overview. Br. Med. Bull. 53:451-465.

Cited by

  1. Involvement of Cathepsin D in Apoptosis of Mammary Epithelial Cells vol.19, pp.8, 2005, https://doi.org/10.5713/ajas.2006.1100
  2. Viability and Functions of Alginate-microencapsulated Islets Isolated from Neonatal Pigs vol.20, pp.5, 2005, https://doi.org/10.5713/ajas.2007.795