scholarly journals P371Role of the N- and distal C-terminal domains in Nav1.5 alpha-subunit interaction

2014 ◽  
Vol 103 (suppl 1) ◽  
pp. S68.1-S68 ◽  
Author(s):  
N Neyroud ◽  
A Ziyadeh-Isleem ◽  
J Clatot ◽  
I Deschenes ◽  
A Coulombe ◽  
...  
1992 ◽  
Vol 262 (5) ◽  
pp. F837-F842 ◽  
Author(s):  
E. Imesch ◽  
M. Moosmayer ◽  
B. M. Anner

The presence of circulating inhibitors able to decrease the renal Na-K-adenosinetriphosphatase (ATPase) activity (natriuretic hormones) was postulated some 30 years ago. In the present work, the natriuretic inhibitor HgCl2 was selected as a model compound for the structural characterization of a possible natriuretic pathway for Na-K-ATPase modification. The structural effects of Na-K-ATPase inhibition by HgCl2 were assessed by trypsinolysis of the blocked enzyme in comparison with untreated preparations. The results show that inactivation of Na-K-ATPase by HgCl2 leads to the release of the alpha-subunit from the membrane preferentially in the E2 conformation but also in the E1 conformation. Apparently, HgCl2 weakens the membrane anchoring of the alpha-subunit, presumably by loosening the alpha-beta-subunit interaction. By this mechanism, the sensitivity of the Na-K-ATPase to extracellular drugs, hormones, and antibodies, as well as to intracellular proteases and other regulatory factors, could be altered.


1997 ◽  
Vol 94 (21) ◽  
pp. 11274-11278 ◽  
Author(s):  
K. Murakami ◽  
J. T. Owens ◽  
T. A. Belyaeva ◽  
C. F. Meares ◽  
S. J. W. Busby ◽  
...  

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