Sensitizing multidrug-resistant leukemia cells to common cytostatics by an aluminium-salen complex that has high-apoptotic effects in leukemia, lymphoma and mamma carcinoma cells

BioMetals ◽  
2021 ◽  
Vol 34 (2) ◽  
pp. 211-220
Author(s):  
Sina M. Hopff ◽  
Liliane A. Onambele ◽  
Marc Brandenburg ◽  
Albrecht Berkessel ◽  
Aram Prokop
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.


2002 ◽  
Vol 85 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Thierry Simonart ◽  
Johan R. Boelaert ◽  
Roger Mosselmans ◽  
Graciela Andrei ◽  
Jean-Christophe Noel ◽  
...  

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