Structural Insight into the Ion-Exchange Mechanism of the Sodium/Calcium Exchanger

Science ◽  
2012 ◽  
Vol 335 (6069) ◽  
pp. 686-690 ◽  
Author(s):  
J. Liao ◽  
H. Li ◽  
W. Zeng ◽  
D. B. Sauer ◽  
R. Belmares ◽  
...  
2020 ◽  
Vol 132 (20) ◽  
pp. 7862-7866 ◽  
Author(s):  
Shivani Sharma ◽  
Aamod V. Desai ◽  
Biplab Joarder ◽  
Sujit K. Ghosh

1993 ◽  
Vol 265 (4) ◽  
pp. C1118-C1127 ◽  
Author(s):  
R. Espinosa-Tanguma ◽  
J. DeSantiago ◽  
H. Rasgado-Flores

To gain insight into the mechanism by which the protease alpha-chymotrypsin (alpha-chym) activates the Na-Ca exchanger in muscle cells we studied 1) the ability of this enzyme to remove the intracellular "catalytic" Ca2+ requirement for activation of all the modes of exchange mediated by the Na-Ca exchanger (i.e., Nao-Cai, Nai-Cao, Nao-Nai, and Cao-Cai, where the subscripts o and i represent extracellular and intracellular, respectively), and 2) the ability of certain monovalent cations to stimulate Cao-Cai exchange after activation of the exchanger by alpha-chym. Barnacle muscle cells were used as models because these cells are so large that they can be internally perfused and voltage clamped. The results show that alpha-chym produces a highly activated Na-Ca exchanger able to operate in all its modes of exchange independently of catalytic Cai. The concentration-dependent effect of alpha-chym was biphasic; maximal activation occurred at 0.5 mg alpha-chym/ml perfusate for 20 min of perfusion at a perfusion rate of 2.5 microliters/min. The results are discussed in terms of the possible effects of alpha-chym on the kinetic modulation of the exchanger.


2016 ◽  
Vol 23 (6) ◽  
pp. 590-599 ◽  
Author(s):  
Jun Liao ◽  
Fabrizio Marinelli ◽  
Changkeun Lee ◽  
Yihe Huang ◽  
José D Faraldo-Gómez ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document