Phorbol 12-myristate 13-acetate prevents apoptosis in erythroleukemia K562 cells induced by some nucleosides

被引:0
作者
Volkova T.O. [1 ]
Malysheva I.E. [1 ]
Nemova N.N. [1 ]
机构
[1] Petrozavodsk State University, Petrozavodsk, 185640
基金
俄罗斯基础研究基金会;
关键词
Apoptosis; Caspases; Erythroid differentiation; Phorbol; 12-myristate; 13-acetate;
D O I
10.1007/s11174-005-0003-0
中图分类号
学科分类号
摘要
We studied the ability of phorbol 12-myristate 13-acetat to prevent erythroid differentiation and apoptosis in erythroleukemic K562 cells induced by cytidine, thymidine, and guanosine. The exposure of cancer cells to combinations of phorbol 12-myrsitate 13-acetate (100 nM) nucleosides for two days led to a loss of hemoglobin production (marker of erythroid differentiation) in cells and increased expression of monocyte-macrophage lineage associated surface antigen CD14. The treatment of K562 cells with nucleosides only was accompanied by the activation of caspase-3 and caspase-9, rather than caspase-6, increased fluorescence of ethidium bromide and DAPI upon binding to DNA, and apoptosis. Intracellular activation of caspase-6, inhibition of caspase-9, a markedly decreased activity of caspase-3 and of fluorescence of DNA-binding dyes, and inhibition of apoptosis were observed when the cells were treated with phorbol 12-myeristet 13-acetate combined with nucleosides. © 2005 Pleiades Publishing, Inc.
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页码:14 / 20
页数:6
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共 43 条
  • [1] Andersson L.C., Nilsson K., Gahmberg C.G., K562 - A Human Erythroleukemic Cell Line, Int. J. Cancer, 23, pp. 143-147, (1979)
  • [2] Anisimov A.G., Bolotnikov I.A., Treatment of Synchronized K562 Cells with Tetrafluorine Luminate Does Not Modulate Fluorescence of Ethidium Bromide and 4′,6-Diamidino-2- Phenylindola upon Binding to Nucleoside DNA, Tsitologiya, 41, 8, pp. 680-684, (1999)
  • [3] Anisimov A.G., Bolotnikov I.A., Volkova T.O., Influence of Thymidine and Phorbol-12-Myristate-13-Acetate on Erythroid Differentiation of K562 Cells and Their Sensitivity to Nonspecific Lysis by Rat Splenocytes, Byull. Eksp. Biol. Med., 128, 11, pp. 521-524, (1999)
  • [4] Anisimov A.G., Bolotnikov I.A., Volkova T.O., Changes in Sensitivity of K562 Cells to Nonspecific Lysis by Human and Rat Leucocytes in the Presence of Sodium Butyrate, DMSO, and Phorbol-12-Myristate-13-Acetate, Ontogenez, 31, 1, pp. 47-52, (2000)
  • [5] Baliga B.S., Mankad M., Shah A.K., Et al., Mechanism of Differentiation of Human Erythroleukemic Cell Line K562 by Hemin, Cell Prolif., 26, pp. 519-529, (1993)
  • [6] Butler T.M., Ziemiecki A., Friis R.R., Megakaryocytic Differentiation of K562 Cells Is Associated with Changes in the Cytoskeletal Organization and the Pattern of Chromatographically Distinct Forms of Phosphotyrosyl-Specific Protein Phosphatases, Cancer Res., 50, pp. 6323-6329, (1990)
  • [7] Chang T.J., Scher B.M., Waxman S., Et al., Inhibition of Mouse GATA-1 Function by the Glucocorticoid Receptor: Possible Mechanism of Steroid Inhibition of Erythroleukemia Cell Differentiation, Mol. Endocrinol., 7, pp. 528-542, (1993)
  • [8] Delgado M.D., Lerga A., Canelles M., Et al., Differential Regulation of Max and Role of c-Myc during Erythroid and Myelomonocytic Differentiation of K562 Cells, Oncogene, 10, pp. 1659-1665, (1995)
  • [9] Doyle B.T., O'Neill A.J., Newsholme P., Et al., The Loss of IAP Expression during HL-60 Cell Differentiation Is Caspase-Independent, J. Leukoc. Biol., 71, pp. 247-254, (2002)
  • [10] Edashige K., Utsumi T., Sato E.F., Et al., Requirement of Protein Association with Membranes for Phosphorylation by Protein Kinase C, Arch. Biochem. Biophvs., 296, pp. 296-301, (1992)