Voltage-Dependent Anion Channels and Tubulin: Bioenergetic Controllers in Cancer Cells

2017 ◽  
pp. 121-140
Author(s):  
Eduardo N. Maldonado ◽  
David N. DeHart ◽  
John J. Lemasters
Keyword(s):  
Cancer Cells ◽  
Anion Channels ◽  
Voltage Dependent

scholarly journals Voltage-dependent Anion Channels Modulate Mitochondrial Metabolism in Cancer Cells

2013 ◽  
Vol 288 (17) ◽  
pp. 11920-11929 ◽  
Author(s):  
Eduardo N. Maldonado ◽  
Kely L. Sheldon ◽  
David N. DeHart ◽  
Jyoti Patnaik ◽  
Yefim Manevich ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Mitochondrial Metabolism ◽  
Anion Channels ◽  
Voltage Dependent

scholarly journals Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

2007 ◽  
Vol 9 (5) ◽  
pp. 550-555 ◽  
Author(s):  
Christopher P. Baines ◽  
Robert A. Kaiser ◽  
Tatiana Sheiko ◽  
William J. Craigen ◽  
Jeffery D. Molkentin
Keyword(s):  
Cell Death ◽  
Anion Channels ◽  
Voltage Dependent ◽  
Dependent Cell

scholarly journals Voltage-dependent block of endothelial volume-regulated anion channels by calix[4]arenes

1998 ◽  
Vol 275 (3) ◽  
pp. C646-C652 ◽  
Author(s):  
Guy Droogmans ◽  
Jean Prenen ◽  
Jan Eggermont ◽  
Thomas Voets ◽  
Bernd Nilius
Keyword(s):  
Open Channel ◽  
Single Channel ◽  
Anion Channel ◽  
Anion Channels ◽  
Channel Conductance ◽  
Open Channel Block ◽  
Maximum Inhibition ◽  
Voltage Dependent ◽  
A Site ◽  
Maximal Block

We have studied the effects of calix[4]arenes on the volume-regulated anion channel (VRAC) currents in cultured calf pulmonary artery endothelial cells. TS- and TS-TM-calix[4]arenes induced a fast inhibition at positive potentials but were ineffective at negative potentials. Maximal block occurred at potentials between 30 and 50 mV. Lowering extracellular pH enhanced the block and shifted the maximum inhibition to more negative potentials. Current inhibition was also accompanied by an increased current noise. From the analysis of the calix[4]arene-induced noise, we obtained a single-channel conductance of 9.3 ± 2.1 pS ( n = 9) at +30 mV. The voltage- and time-dependent block were described using a model in which calix[4]arenes bind to a site at an electrical distance of 0.25 inside the channel with an affinity of 220 μM at 0 mV. Binding occludes VRAC at moderately positive potentials, but calix[4]arenes permeate the channel at more positive potentials. In conclusion, our data suggest an open-channel block of VRAC by calix[4]arenes that also depends on the protonation of the binding site within the pore.

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