scholarly journals Occurrence and role of tightly bound adenine nucleotides in sarcoplasmic reticulum of rabbit skeletal muscle.

1979 ◽  
Vol 76 (8) ◽  
pp. 3622-3626 ◽  
Author(s):  
A. A. Aderem ◽  
D. B. McIntosh ◽  
M. C. Berman
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Adenine Nucleotides ◽  
Rabbit Skeletal Muscle

scholarly journals Calcium-Binding Properties of Sarcoplasmic Reticulum As Influenced by ATP, Caffeine, Quinine, and Local Anesthetics

1968 ◽  
Vol 52 (4) ◽  
pp. 622-642 ◽  
Author(s):  
Arselio P. Carvalho
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Binding Sites ◽  
Local Anesthetics ◽  
Calcium Binding ◽  
Rabbit Skeletal Muscle ◽  
Cellular Membranes ◽  
Binding Properties ◽  
45Ca Fluxes

Calcium retained at binding sites of the sarcoplasmic reticulum membranes isolated from rabbit skeletal muscle requires 10-5 - 10-4 M ATP to exchange with 45Ca added to the medium. The ATP requirement for Ca exchangeability was observed with respect to the "intrinsic" Ca of the reticulum membranes and the fraction of Ca that is "actively" bound in the presence of ATP. Furthermore, a concentration of free Ca in the medium higher than 10-8 M is required for ATP to promote Ca exchangeability. This exchangeability is not influenced by caffeine, quinine, procaine, and tetracaine, and Ca that is either nonexchangeable (in the absence of ATP) or exchangeable (in the presence of ATP) is released by 1–5 mM quinine or tetracaine, but neither caffeine (6 mM) nor procaine (2–5 mM) has this effect. Quinine or tetracaine also releases Ca and Mg bound passively to the reticulum membranes. A possible role of ATP in maintaining the integrity of cellular membranes is discussed, and the effects of caffeine, quinine, and of local anesthetics on the binding of Ca by the isolated reticulum are related to the effects of these agents on 45Ca fluxes and on the twitch output observed in whole muscles.

scholarly journals Calcium-Binding Properties of Sarcoplasmic Reticulum As Influenced by ATP, Caffeine, Quinine, and Local Anesthetics

1968 ◽  
Vol 52 (3) ◽  
pp. 622-642 ◽  
Author(s):  
Arselio P. Carvalho
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Binding Sites ◽  
Local Anesthetics ◽  
Calcium Binding ◽  
Rabbit Skeletal Muscle ◽  
Cellular Membranes ◽  
Binding Properties ◽  
45Ca Fluxes

Calcium retained at binding sites of the sarcoplasmic reticulum membranes isolated from rabbit skeletal muscle requires 10-5 – 10-4 M ATP to exchange with 45Ca added to the medium. The ATP requirement for Ca exchangeability was observed with respect to the "intrinsic" Ca of the reticulum membranes and the fraction of Ca that is "actively" bound in the presence of ATP. Furthermore, a concentration of free Ca in the medium higher than 10-8 M is required for ATP to promote Ca exchangeability. This exchangeability is not influenced by caffeine, quinine, procaine, and tetracaine, and Ca that is either nonexchangeable (in the absence of ATP) or exchangeable (in the presence of ATP) is released by 1–5 mM quinine or tetracaine, but neither caffeine (6 mM) nor procaine (2–5 mM) has this effect. Quinine or tetracaine also releases Ca and Mg bound passively to the reticulum membranes. A possible role of ATP in maintaining the integrity of cellular membranes is discussed, and the effects of caffeine, quinine, and of local anesthetics on the binding of Ca by the isolated reticulum are related to the effects of these agents on 45Ca fluxes and on the twitch output observed in whole muscles.

scholarly journals The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle

1979 ◽  
Vol 100 (2) ◽  
pp. 329-337 ◽  
Author(s):  
Shirish SHENOLIKAR ◽  
Patricia T. W. COHEN ◽  
Philip COHEN ◽  
Angus C. NAIRN ◽  
S. Victor PERRY
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Phosphorylase Kinase

Role of intracellular calcium and metabolites in low-frequency fatigue of mouse skeletal muscle

1997 ◽  
Vol 272 (2) ◽  
pp. C550-C559 ◽  
Author(s):  
E. R. Chin ◽  
C. D. Balnave ◽  
D. G. Allen
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Low Frequency ◽  
Single Muscle ◽  
Low Frequencies ◽  
Time Integral ◽  
Metabolic Component ◽  
Dependent Component ◽  
Low Frequency Fatigue

We have examined the extent to which prolonged reductions in low-frequency force (i.e., low-frequency fatigue) result from increases in intracellular free Ca2+ concentration ([Ca2+]i) and alterations in muscle metabolites. Force and [Ca2+]i were measured in mammalian single muscle fibers in response to short, intermediate, and long series of tetani that elevated the [Ca2+]i-time integral to 5, 17, and 29 microM x s, respectively. Only the intermediate and long series resulted in prolonged (>60 x min) reductions in Ca2+ release and low-frequency fatigue. When fibers recovered from the long series of tetani without glucose, Ca2+ release was reduced to a greater extent and force was reduced at high and low frequencies. These findings indicate that the decrease in sarcoplasmic reticulum Ca2+ release associated with fatigue has at least two components: 1) a metabolic component, which, in the presence of glucose, recovers within 1 h, and 2) a component dependent on the elevation of the [Ca2+]i-time integral, which recovers more slowly. It is this Ca2+-dependent component that is primarily responsible for low-frequency fatigue.

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