A 23-pS Ca2+-activated K+ channel in MCF-7 human breast carcinoma cells: an apparent correlation of channel incidence with the rate of cell proliferation

1991 ◽  
Vol 417 (6) ◽  
pp. 562-570 ◽  
Author(s):  
E. A. Wegman ◽  
J. A. Young ◽  
D. I. Cook
1994 ◽  
Vol 302 (3) ◽  
pp. 649-654 ◽  
Author(s):  
Z Kiss ◽  
M Tomono ◽  
W B Anderson

The phospholipase D (PLD)-mediated synthesis of phosphatidylethanol (PtdEtOH) and the hydrolysis of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) were examined in drug-sensitive and multidrug-resistant lines of MCF-7 human breast carcinoma cells. In drug-sensitive (MCF-7/WT) cells, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) failed to enhance either the synthesis of PtdEtOH or the hydrolysis of either phospholipid. In the drug-resistant (MCF-7/MDR) cells, 100 nM PMA greatly enhanced both the synthesis of PtdEtOH (approximately 21-fold) and the hydrolysis of PtdEtn (approximately 29-fold), but had no effect on the hydrolysis of PtdCho. The PLD activators sphingosine and H2O2 were found to elicit only a slight (1.28-1.4-fold) stimulatory effect on PtdCho hydrolysis in both the MCF-7/WT and MCF-7/MDR cell types, and had only a small effect on PtdEtn hydrolysis in the MCF-7/WT cells as well. However, these agents significantly (approximately 2.6-3.5-fold) stimulated PtdEtn hydrolysis in the MCF-7/MDR cells. These data indicate that MCF-7/MDR cells contain a PtdEtn-specific PLD activity which can be selectively stimulated by PMA, sphingosine and H2O2.


1989 ◽  
Vol 62 (744) ◽  
pp. 1079-1083 ◽  
Author(s):  
David E. Wazer ◽  
Oscar F. Tercilla ◽  
Peck-Sun Lin ◽  
Rupert Schmidt-Ullrich

Life Sciences ◽  
2007 ◽  
Vol 80 (23) ◽  
pp. 2161-2169 ◽  
Author(s):  
Yanqiu Xia ◽  
Liji Jin ◽  
Bin Zhang ◽  
Hongyu Xue ◽  
Qiujuan Li ◽  
...  

2017 ◽  
Vol 14 (2) ◽  
pp. 2207-2217 ◽  
Author(s):  
Chu Lee ◽  
Wonjoo Chun ◽  
Rongjie Zhao ◽  
Young Dae Kim ◽  
Myung Mo Nam ◽  
...  

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