Dantrolene sodium increases calcium binding by human recombinant cardiac calsequestrin and calcium loading by sheep cardiac sarcoplasmic reticulum

2019 ◽  
Vol 226 (3) ◽  
pp. e13261
Author(s):  
Christine Margaret Loescher ◽  
Lynne Michelle Gibson ◽  
Dimitrie George Stephenson
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Dantrolene Sodium ◽  
Calcium Loading

Calcium-binding rate and capacity of cardiac sarcoplasmic reticulum

1981 ◽  
Vol 13 (9) ◽  
pp. 785-796 ◽  
Author(s):  
D.O. Levitsky ◽  
D.S. Benevolensky ◽  
T.S. Levchenko ◽  
V.N. Smirnov ◽  
E.I. Chazov
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Binding Rate

scholarly journals The Influence of Hydrogen Ion Concentration on Calcium Binding and Release by Skeletal Muscle Sarcoplasmic Reticulum

1972 ◽  
Vol 59 (1) ◽  
pp. 22-32 ◽  
Author(s):  
Yoshiaki Nakamaru ◽  
Arnold Schwartz
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Calcium Release ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Ph Change ◽  
Release Process ◽  
Hydrogen Ion Concentration ◽  
Calcium Loading

Calcium release and binding produced by alterations in pH were investigated in isolated sarcoplasmic reticulum (SR) from skeletal muscle. When the pH was abruptly increased from 6.46 to 7.82, after calcium loading for 30 sec, 80–90 nanomoles (nmole) of calcium/mg protein were released. When the pH was abruptly decreased from 7.56 to 6.46, after calcium loading for 30 sec, 25–30 nmole of calcium/mg protein were rebound. The calcium release process was shown to be a function of pH change: 57 nmole of calcium were released per 1 pH unit change per mg protein. The amount of adenosine triphosphate (ATP) bound to the SR was not altered by the pH changes. The release phenomenon was not due to alteration of ATP concentration by the increased pH. Native actomyosin was combined with SR in order to study the effectiveness of calcium release from the SR by pH change in inducing super-precipitation of actomyosin. It was found that SR, in an amount high enough to inhibit superprecipitation at pH 6.5, did not prevent the process when the pH was suddenly increased to 7.3, indicating that the affinity of SR for calcium depends specifically on pH. These data suggest the possible participation of hydrogen ion concentration in excitation-contraction coupling.

A study of calcium binding and uptake by isolated cardiac sarcoplasmic reticulum: The use of a new ionophore (X537A)

1972 ◽  
Vol 48 (4) ◽  
pp. 847-853 ◽  
Author(s):  
Mark L. Entman ◽  
Paul C. Gillette ◽  
Earl T. Wallick ◽  
Burton C. Pressman ◽  
Arnold Schwartz
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Cardiac Sarcoplasmic Reticulum

scholarly journals Ion Effects on Calcium Accumulation by Cardiac Sarcoplasmic Reticulum

1967 ◽  
Vol 50 (8) ◽  
pp. 2085-2095 ◽  
Author(s):  
Roger F. Palmer ◽  
Virginia A. Posey
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Sodium Ion ◽  
Monovalent Cations ◽  
Sodium Influx ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Free System ◽  
Rapid Release ◽  
Active Calcium ◽  
Ion Effects

The effects of monovalent cations on the active calcium-accumulating ability of cardiac sarcoplasmic reticulum were assessed. Grana prepared in an ion-free system accumulated calcium when ATP and Mg++ were present. Sodium ion and to a lesser extent lithium but not K+ reduced the amount of calcium taken up. The reduction of calcium binding by Na+ is not due to inhibition of uptake but to a rapid release of the radiocalcium bound. The amount of calcium released by sodium does not appear to be enough to explain contraction on the basis of sodium influx into muscle, but may be significant in the regulation of tension.

Sign in / Sign up

Export Citation Format

Share Document