Imaging calcium entering the cytosol through a single opening of plasma membrane ion channels: SCCaFTs—fundamental calcium events

Cell Calcium ◽  
2004 ◽  
Vol 35 (6) ◽  
pp. 523-533 ◽  
Author(s):  
Hui Zou ◽  
Lawrence M Lifshitz ◽  
Richard A Tuft ◽  
Kevin E Fogarty ◽  
Joshua J Singer
Author(s):  
A. Koivisto ◽  
T. Ringer ◽  
U. Ruß ◽  
J. Nedergaard ◽  
D. Siemen

1992 ◽  
pp. 225-236
Author(s):  
B. R. Terry ◽  
S. D. Tyerman ◽  
G. P. Findlay

2016 ◽  
Vol 23 (11) ◽  
pp. R517-R525 ◽  
Author(s):  
Iman Azimi ◽  
Gregory R Monteith

A variety of studies have suggested that epithelial to mesenchymal transition (EMT) may be important in the progression of cancer in patients through metastasis and/or therapeutic resistance. A number of pathways have been investigated in EMT in cancer cells. Recently, changes in plasma membrane ion channel expression as a consequence of EMT have been reported. Other studies have identified specific ion channels able to regulate aspects of EMT induction. The utility of plasma membrane ion channels as targets for pharmacological modulation make them attractive for therapeutic approaches to target EMT. In this review, we provide an overview of some of the key plasma membrane ion channel types and highlight some of the studies that are beginning to define changes in plasma membrane ion channels as a consequence of EMT and also their possible roles in EMT induction.


eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Florian Ullrich ◽  
Sandy Blin ◽  
Katina Lazarow ◽  
Tony Daubitz ◽  
Jens Peter von Kries ◽  
...  

Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR’s pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR’s role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed.


1992 ◽  
Vol 99 (1) ◽  
pp. 96-102 ◽  
Author(s):  
E. P. Spalding ◽  
C. L. Slayman ◽  
M. H. M. Goldsmith ◽  
D. Gradmann ◽  
A. Bertl

Author(s):  
Koen M. O. Galenkamp ◽  
Cosimo Commisso

Cancer cells exhibit increased glycolytic flux and adenosine triphosphate (ATP) hydrolysis. These processes increase the acidic burden on the cells through the production of lactate and protons. Nonetheless, cancer cells can maintain an alkaline intracellular pH (pHi) relative to untransformed cells, which sets the stage for optimal functioning of glycolytic enzymes, evasion of cell death, and increased proliferation and motility. Upregulation of plasma membrane transporters allows for H+ and lactate efflux; however, recent evidence suggests that the acidification of organelles can contribute to maintenance of an alkaline cytosol in cancer cells by siphoning off protons, thereby supporting tumor growth. The Golgi is such an acidic organelle, with resting pH ranging from 6.0 to 6.7. Here, we posit that the Golgi represents a “proton sink” in cancer and delineate the proton channels involved in Golgi acidification and the ion channels that influence this process. Furthermore, we discuss ion channel regulators that can affect Golgi pH and Golgi-dependent processes that may contribute to pHi homeostasis in cancer.


Sign in / Sign up

Export Citation Format

Share Document