Effect of ONC201 Antitumor Drug on the Number of Mitochondrial Nucleoids in BT474 Breast Cancer Cells in Culture

2021 ◽  
Vol 76 (3) ◽  
pp. 83-89
Author(s):  
A. A. Mishukov ◽  
A. V. Berezhnov ◽  
M. I. Kobyakova ◽  
Ya. V. Evstratova ◽  
E. Yu. Mndlyan ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Antitumor Drug ◽  
Cells In Culture ◽  
Mitochondrial Nucleoids

scholarly journals Whole-cell uptake and nuclear localization of 1,25-dihydroxycholecalciferol by breast cancer cells (T47 D) in culture

1981 ◽  
Vol 200 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Elizabeth Sher ◽  
John A. Eisman ◽  
Jane M. Moseley ◽  
T. John Martin
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Binding Sites ◽  
Breast Cancer Cells ◽  
Nuclear Translocation ◽  
Vitamin D Metabolites ◽  
Intact Cells ◽  
Cells In Culture

Specific high-affinity receptors for 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] have been described recently in broken-cell preparations of several cultured human breast cancer cell lines including the T47 D line. It was necessary to determine whether intact breast cancer cells in culture would bind 1,25-(OH)2D3 specifically and whether the next step in the proposed scheme of action, i.e. nuclear translocation, occurred. The following results were obtained. (1) Specific uptake of 1,25-(OH)2D3 by T47 D cells occurs in intact cells in culture. (2) The rate of uptake is proportional to medium 1,25-(OH)2D3 concentration but is slow compared with that of other steroid hormones, e.g., oestradiol, under identical conditions. Even at 0.5nm-1,25-(OH)2D3 in the medium, at least 4h are required to reach maximum compared with less than 1h for oestradiol binding. (3) Estimation of binding characteristics by Scatchard analysis indicates a single class of binding sites with Kd of 68pm and 11800 binding sites/cell, which are similar results to those obtained with broken-cell preparations. (4) Inclusion of various vitamin D metabolites in the incubation medium decreased specific binding of 1,25-(OH)2D3 by the intact cells in a manner identical with their effects in the broken-cell preparation and with potencies similar to their potency on Ca2+ transport and bone resorption in vivo. Order of potency was 1,25-(OH)2D3>(24R)-1,24,25-trihydroxycholecalciferol »25-hydroxycholecalciferol>(25R)-24,25-dihydroxycholecalciferol »(25R)-25,26-dihydroxycholecalciferol. (5) In the 1,25-(OH)2D3-depleted state, 80% of the 1,25(OH)2D3 receptor is found in the cytosol fraction of the cells even when the subcellular fractionation is performed under low-salt conditions. By contrast after incubation with [3H]1,25-(OH)2D3, 59% of the specific 1,25-(OH)2D3 binding is found in the partially purified nuclei fraction. These data indicate that nuclear translocation of the receptor–hormone complex takes place in the intact T47 D cell. The results also support the hypothesis that the 1,25-(OH)2D3 receptor is functional in this cultured breast cancer cell line, which may provide a useful model for further study of the early biochemical events in 1,25-(OH)2D3 action.

scholarly journals Inverse effects of 20K and 22K human growth hormones on the growth of T-47D human breast cancer cells in culture and in nude mice

IUBMB Life ◽  
1998 ◽  
Vol 46 (4) ◽  
pp. 719-724
Author(s):  
Takahiko Fujikawa ◽  
Hiroshi Kaneko ◽  
Hiroshige Hibasami ◽  
Kesami Sakaguchi ◽  
Khorshed Alam ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Nude Mice ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Human Growth ◽  
Growth Hormones ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Cells In Culture
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