The effects of temperature on relaxation in frog skeletal muscle: the role of parvalbumin

1988 ◽  
Vol 412 (1-2) ◽  
pp. 195-202 ◽  
Author(s):  
Paul A. Iaizzo
Keyword(s):  
Skeletal Muscle ◽  
Frog Skeletal Muscle ◽  
Effects Of Temperature

Hg2+-induced contracture in mechanically skinned fibers of frog skeletal muscle

1985 ◽  
Vol 63 (9) ◽  
pp. 1070-1074 ◽  
Author(s):  
Takako Aoki ◽  
Toshiharu Oba ◽  
Ken Hotta
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Sulfhydryl Groups ◽  
Skinned Fibers ◽  
Frog Skeletal Muscle ◽  
Semitendinosus Muscle ◽  
Skinned Fiber ◽  
Brij 58 ◽  
Develop Tension

In mechanically skinned fibers of the semitendinosus muscle of bullfrogs, we examined the role of membrane sulfhydryl groups on Ca2+ release from the sarcoplasmic reticulum (SR). Hg2+, a sulfhydryl reagent (20–100 μM), induced a repetitive contracture of skinned fibers, and this contracture did not occur in skinned fibers in which the SR had been disrupted by treatment with a detergent (Brij 58). Procaine (10 mM), Mg2+ (5 mM), or dithiothreitol (1 mM) blocked the Hg2+-induced contracture. Ag+ or p-chloromercuribenzenesulfonic acid produced similar contractures to that induced by Hg2+. We conclude that Hg2+ releases Ca2+ from SR of a skinned fiber by modifying sulfhydryl groups on the SR membrane, and suggest that the Ca2+ released by Hg2+ may trigger a greater release of Ca2+ from SR to develop tension.

scholarly journals The Changes in Ca2+ Sparks Associated with Measured Modifications of Intra-store Ca2+ Concentration in Skeletal Muscle

2006 ◽  
Vol 128 (1) ◽  
pp. 45-54 ◽  
Author(s):  
Bradley S. Launikonis ◽  
Jingsong Zhou ◽  
Demetrio Santiago ◽  
Gustavo Brum ◽  
Eduardo Ríos
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Muscle ◽  
Confocal Imaging ◽  
Frog Skeletal Muscle ◽  
Average Increase ◽  
Global Level ◽  
Event Frequency ◽  
Average Change ◽  
Contractile Activation

In cardiac muscle and amphibian skeletal muscle, the intracellular Ca2+ release that signals contractile activation proceeds by discrete local packets, which result in Ca2+ sparks. The remarkably stereotyped duration of these release events requires a robustly timed termination mechanism. In cardiac muscle the mechanism of spark termination appears to crucially involve depletion of Ca2+ in the lumen of the sarcoplasmic reticulum (SR), but in skeletal muscle, the mechanism is unknown. We used SEER (shifted excitation and emission ratioing of fluorescence) of SR-trapped mag-indo-1 and confocal imaging of fluorescence of cytosolic rhod-2 to image Ca2+ sparks while reversibly changing and measuring [Ca2+] in the SR ([Ca2+]SR) of membrane-permeabilized frog skeletal muscle cells. Sparks were collected in cells immersed in a solution promoting production of events at moderate frequency. Just after permeabilization, event frequency was zero, and in 10 minutes it reached close to a steady value. Controlled interventions modified [Ca2+]SR reversibly between a low value (299 μM on average in 10 experiments) and a high value (433 μM, a 45% average increase). This change increased sparks frequency by 93%, spatial width by 7%, rise time by 10%, and peak amplitude by 38% (provided that it was calculated in absolute terms, rather than normalized by resting fluorescence). The changes in event frequency and amplitude were statistically significant. The “strength” of the effect of [Ca2+]SR on frequency, quantified by decomposition of variance, was <6%. While the average change in [Ca2+]SR was limited, it reached up to 200% in individual fibers, without causing massive Ca2+ release or an increase of >3.5-fold in event frequency. Taken together with existing evidence that depletion is modest during Ca2+ sparks or release elicited by an action potential, the mild effects of [Ca2+]SR reported here do not support a major role of depletion in either the termination of sparks or the strong inactivation that terminates Ca2+ release at the global level in frog skeletal muscle.

Role of Parvalbumin in Skeletal Muscle Relaxation

Physiology ◽  
1996 ◽  
Vol 11 (6) ◽  
pp. 249-255 ◽  
Author(s):  
JA Rall
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Muscle Relaxation ◽  
Calcium Pump ◽  
Frog Skeletal Muscle ◽  
Animal Kingdom ◽  
Calcium Buffer ◽  
High Concentrations ◽  
Sarcoplasmic Reticulum Calcium

Parvalbumin, a soluble intracellular calcium buffer, is present in high concentrations in fast-contracting skeletal muscles across the animal kingdom. In frog skeletal muscle, pharmacological or low-temperature inhibition of the sarcoplasmic reticulum calcium pump reveals that parvalbumin sequesters calcium and promotes relaxation at a rate determined by magnesium dissociation from parvalbumin.

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