Excitation contraction coupling in skeletal muscle: Evidence for a role of slow Ca2+ channels using Ca2+ channel activators and inhibitors in the dihydropyridine series

1985 ◽  
Vol 129 (3) ◽  
pp. 904-909 ◽  
Author(s):  
M. Ildefonse ◽  
V. Jacquemond ◽  
O. Rougier ◽  
J.F. Renaud ◽  
M. Fosset ◽  
...  
1982 ◽  
Vol 60 (4) ◽  
pp. 440-445
Author(s):  
Isao Oota ◽  
Isao Kosaka ◽  
Torao Nagai ◽  
Hideyo Yabu

It is the purpose of this article to point out that the membrane-bound Ca plays an important role in excitation–contraction (E–C) coupling of skeletal muscle fibers and that other divalent cations are unable to substitute for this role of membrane-bound Ca.


2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Katarina Stroffekova

Ca2+-dependent modulation via calmodulin, with consensus CaM-binding IQ motif playing a key role, has been documented for most high-voltage-activated Ca2+channels. The skeletal muscle Cav1.1 also exhibits Ca2+-/CaM-dependent modulation. Here, whole-cell Ca2+current, Ca2+transient, and maximal, immobilization-resistant charge movement(Qmax)recordings were obtained from cultured mouse myotubes, to test a role of IQ motif in function of Cav1.1. The effect of introducing mutation (IQ to AA) of IQ motif into Cav1.1 was examined. In dysgenic myotubes expressing YFP-Cav1.1AA, neither Ca2+currents nor evoked Ca2+transients were detectable. The loss of Ca2+current and excitation-contraction coupling did not appear to be a consequence of defective trafficking to the sarcolemma. TheQmaxin dysgenic myotubes expressing YFP-Cav1.1AAwas similar to that of normal myotubes. These findings suggest that the IQ motif of the Cav1.1 may be an unrecognized site of structural and functional coupling between DHPR and RyR.


2011 ◽  
Vol 100 (3) ◽  
pp. 592a
Author(s):  
Matthew J. Betzenhauser ◽  
Daniel C. Andersson ◽  
Steven Reiken ◽  
Andrew R. Marks

FEBS Letters ◽  
1986 ◽  
Vol 197 (1-2) ◽  
pp. 1-4 ◽  
Author(s):  
Pompeo Volpe ◽  
Francesco Di Virgilio ◽  
Tullio Pozzan ◽  
Giovanni Salviati

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