Involvement of thiols in the induction of inward current induced by silver in frog skeletal muscle membrane

1993 ◽  
Vol 49 (9) ◽  
pp. 792-794 ◽  
Author(s):  
T. Aoki ◽  
K. Nihonyanagi ◽  
T. Oba
Keyword(s):  
Skeletal Muscle ◽  
Muscle Membrane ◽  
Frog Skeletal Muscle ◽  
Inward Current

The Effect of Lanthanum on Excitation–Contraction Coupling in Frog Skeletal Muscle

1974 ◽  
Vol 52 (6) ◽  
pp. 1126-1135 ◽  
Author(s):  
D. J. Parry ◽  
A. Kover ◽  
G. B. Frank
Keyword(s):  
Skeletal Muscle ◽  
Action Potential ◽  
Muscle Membrane ◽  
Frog Skeletal Muscle ◽  
Tension Development ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Reduced Rate ◽  
Caffeine Contractures

Exposure of frog toe muscles to 1 mM La3+ results in a decrease in amplitude and rate of tension development of potassium contractures and twitches. At this concentration La3+ also inhibits the uptake of calcium, both in the resting condition and during stimulation. Caffeine contractures are unaffected even after a 5-min pre-exposure to La3+. The depolarization induced by various concentrations of K+ is reduced by about 10 mV as is the amplitude of the action potential. The rate of rise of the action potential is reduced by about 40% after 1 min in La3+ Ringer. Neither the decreased amplitude nor the reduced rate of depolarization is considered to be sufficient to explain the inhibition of tension development. It is suggested that La3+ partially uncouples excitation from contraction by preventing the release of a trigger-Ca2+ fraction from some site on the muscle membrane. This fraction normally plays a role in excitation–contraction coupling, although some tension may still be developed in the absence of a trigger-Ca2+ influx.

Membrane domain localization of pH-regulating transporters in frog skeletal muscle membrane vesicles

1996 ◽  
Vol 271 (4) ◽  
pp. C1367-C1379 ◽  
Author(s):  
R. W. Putnam ◽  
P. B. Douglas ◽  
N. A. Ritucci
Keyword(s):  
Skeletal Muscle ◽  
Atpase Activity ◽  
Surface Membrane ◽  
Membrane Vesicles ◽  
Muscle Membrane ◽  
Frog Skeletal Muscle ◽  
Membrane Domain ◽  
Ph Response ◽  
Kinase C ◽  
Inside Out

The distribution of pH-regulating transporters in surface and transverse (T) tubular membrane (TTM) domains of frog skeletal muscle was studied. 2',7'-Bis(carboxyethyl)-5(6)- carboxyfluorescein-loaded giant sarcolemmal vesicles, containing surface membrane, exhibited reversible Na+/H+ exchange. A microsomal vesicle fraction was shown to be enriched in TTM on the basis of high Na(+)-K(+)-ATPase and Mg(2+)-ATPase activity, high ouabain and nitrendipine binding, and low Ca(2+)-ATPase activity. TTM vesicles were well sealed and oriented inside out. Vesicles were loaded with the pH-sensitive dye pyranine. In response to an inwardly directed Na+ gradient, vesicles displayed virtually no alkalinization unless monensin was present. No pH response to an imposed Na+ gradient was seen regardless of the direction of the pH gradient across the vesicles, after phosphorylation of the vesicles with protein kinase C, or when exposed to guanosine 5'-O-(3-thiotriphosphate). In the presence of CO2, addition of Na+ or Cl- had no effect on vesicle pH. These data indicate that the TTM lacks functional pH-regulating transporters [Na+/H+ and (Na+ + HCO3-)/Cl- exchangers], suggesting that pH-regulating transporters are localized only to the surface membrane domain in frog muscle.

High-affinity [3H]PN200-110 and [3H]ryanodine binding to rabbit and frog skeletal muscle

1994 ◽  
Vol 266 (2) ◽  
pp. C462-C466 ◽  
Author(s):  
K. Anderson ◽  
A. H. Cohn ◽  
G. Meissner
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Muscle Membrane ◽  
Scatchard Analysis ◽  
Physical Interaction ◽  
Frog Skeletal Muscle ◽  
Release Channel ◽  
High Affinity ◽  
Voltage Dependent ◽  
Student’S T

In vertebrate skeletal muscle, the voltage-dependent mechanism of sarcoplasmic reticulum (SR) Ca2+ release, commonly referred to as excitation-contraction (E-C) coupling, is mediated by the voltage-sensing dihydropyridine receptor (DHPR), which is believed to affect SR Ca2+ release through a physical interaction with the SR ryanodine receptor (RYR)/Ca2+ release channel. Scatchard analysis of ligand binding of [3H]PN200-110 to the DHPR and [3H]ryanodine to the RYR indicated the presence of high-affinity sites in muscle homogenates, with maximum binding (Bmax) values of 72 +/- 26 and 76 +/- 30 pmol/g wet wt for rabbit skeletal muscle, and 27 +/- 14 and 44 +/- 13 pmol/g wet wt for frog skeletal muscle, respectively. The Bmax values corresponded to a PN200-110-to-ryanodine binding ratio of 0.98 +/- 0.26 and 0.61 +/- 0.24 for rabbit and frog skeletal muscle, respectively, and were found by Student's t test to be significantly different (P < 0.02, n = 7). These results are compared with measurements with isolated rabbit skeletal muscle membrane fractions and discussed in relation to our current understanding of the mechanism of E-C coupling in skeletal muscle.

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