scholarly journals Impaired calcium-calmodulin-dependent inactivation of Cav1.2 contributes to loss of sarcoplasmic reticulum calcium release refractoriness in mice lacking calsequestrin 2

2015 ◽  
Vol 82 ◽  
pp. 75-83 ◽  
Author(s):  
Dmytro O. Kryshtal ◽  
Oleksiy Gryshchenko ◽  
Nieves Gomez-Hurtado ◽  
Bjorn C. Knollmann
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Calcium Calmodulin Dependent ◽  
Dependent Inactivation ◽  
Sarcoplasmic Reticulum Calcium

Two sites of action for LCB29 (idrocilamide) in depressing mechanical tension of rat soleus muscle fibers?

1993 ◽  
Vol 71 (12) ◽  
pp. 889-895
Author(s):  
Aklesso Mouzou ◽  
Alexandre Bouron ◽  
Joel Guillemain ◽  
Daniel Guerrier ◽  
Guy Raymond
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Soleus Muscle ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Voltage Sensor ◽  
Dependent Inactivation ◽  
Voltage Dependent ◽  
Rat Soleus Muscle ◽  
Sarcoplasmic Reticulum Calcium ◽  
Caffeine Contractures

The effects of 50 μM LCB29 (idrocilamide) were tested on depolarization-induced and caffeine contractures of rat soleus muscle fibers. When applied intracellularly by free diffusion in cut-end voltage-clamped fibers, LCB29 decreased tension amplitude by about 25%. The same amount of inhibition by LCB29 was observed on contractures induced by 6 mM caffeine. The drug did not affect the repriming of caffeine contractures, indicating that internal recycling of calcium was not affected. The voltage-dependent inactivation of tension was facilitated by external application of LCB29. This effect was calcium dependent, so that the greater the external calcium concentration, the greater the drug effectiveness. The spontaneous relaxation of K+ contractures was also accelerated by LCB29. It is concluded that LCB29 acts intracellularly by decreasing sarcoplasmic reticulum calcium release and externally by facilitating the voltage-dependent inactivation of the voltage sensor for excitation–contraction coupling.Key words: myorelaxants, skeletal muscle, sarcoplasmic reticulum calcium release, voltage sensor.

scholarly journals Cardiac Sarcoplasmic Reticulum Calcium Release and Load Are Enhanced by Subcellular cAMP Elevations in PI3Kγ-Deficient Mice

2005 ◽  
Vol 96 (10) ◽  
pp. 1079-1086 ◽  
Author(s):  
Benoit-Gilles Kerfant ◽  
Dominica Gidrewicz ◽  
Hui Sun ◽  
Gavin Y. Oudit ◽  
Josef M. Penninger ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Sarcoplasmic Reticulum Calcium ◽  
Deficient Mice

scholarly journals Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor

2016 ◽  
Vol 173 (15) ◽  
pp. 2446-2459 ◽  
Author(s):  
Mark L Bannister ◽  
Anita Alvarez‐Laviada ◽  
N Lowri Thomas ◽  
Sammy A Mason ◽  
Sharon Coleman ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Direct Action ◽  
Sarcoplasmic Reticulum Calcium ◽  
Cardiac Ryanodine Receptor

Sarcoplasmic Reticulum Calcium Release Channels in Ventricles of Older Adult Hamsters

2006 ◽  
Vol 25 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Peter A. Nicholl ◽  
Susan E. Howlett
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Older Adult ◽  
Binding Sites ◽  
Calcium Release ◽  
Ryanodine Receptors ◽  
Calcium Release Channels ◽  
Site Density ◽  
Age Related ◽  
Sarcoplasmic Reticulum Calcium ◽  
Age Related Changes

ABSTRACTWhether the density of sarcoplasmic reticulum (SR) calcium release channels / ryanodine receptors in the heart declines with age is not clear. We investigated age-related changes in the density of «3H»-ryanodine receptors in crude ventricular homogenates, which contained all ligand binding sites in heart and in isolated junctional SR membranes. Experiments utilized young (120 days) and older adult (300 days) hamsters. «3H»-ryanodine binding site density did not change with age in crude homogenate preparations, although total heart protein concentration increased significantly with age. In contrast, the density of «3H»-ryanodine binding sites decreased markedly in heavy SR membranes purified from older hearts. These results show that demonstration of age-related changes in cardiac ryanodine receptor density depends upon the preparation used. Furthermore, the increase in total ventricular protein with age suggests that normalization of data by membrane protein should be used with caution in studies of aging heart.

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