Inhibition of Zn2+-induced potentiation of twitch tension by Ni2+ in frog muscle

1986 ◽  
Vol 64 (5) ◽  
pp. 625-630
Author(s):  
Toshiharu Oba ◽  
Ken Hotta
Keyword(s):  
Action Potential ◽  
Inhibitory Action ◽  
Channel Blocker ◽  
Rana Catesbeiana ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Duration Of Action ◽  
Ringer’S Solution ◽  
Mechanical Threshold ◽  
T Tubules

Effect of Ni2+ on Zn2+-induced potentiation of twitch tension was studied electrophysiologically in the toe muscle fibers of Rana catesbeiana. The major findings of this investigation are as follows. When 2 mM Ni2+ was applied to fibers in a normal Ringer's solution containing 50 μM Zn2+ (Zn2+ solution), the Zn2+-potentiated twitch tension decreased remarkably to about one-third of that before Ni2+ treatment. This concentration of Ni2+ caused a 23% decrease in the duration of action potential which had been prolonged by Zn2+ (6.61–5.09 ms). Ni2+ (2 mM) added to normal Ringer's solution led to increases of about 30 and 42% in twitch tension and in the duration of action potential, respectively. A slight increase in the mechanical threshold was induced by 2 mM Ni2+. The inhibitory action of Ni2+ on the twitch tension in Zn2+ solution was larger than that in the case of tetanus tension. Diltiazem (40 μM), aCa2+ channel blocker, did not inhibit the twitch tension potentiated in Zn2+ solution. These results suggest that the decrease in Zn2+-potentiated twitch tension by Ni2+ may possibly derive from impairment of the propagation of action potential along the T tubules.

Effect of temperature and Zn2+ on isometric contractile properties and electrical phenomena of frog (Rana) and Xenopus skeletal muscle fibers

1984 ◽  
Vol 62 (12) ◽  
pp. 1511-1517 ◽  
Author(s):  
Toshiharu Oba ◽  
Yumiko Takagi ◽  
Ken Hotta
Keyword(s):  
Action Potential ◽  
Rana Catesbeiana ◽  
Muscle Fibers ◽  
Contractile Properties ◽  
Effect Of Temperature ◽  
Duration Of Action ◽  
Time To Peak ◽  
Effects Of Temperature ◽  
Maximum Rate Of Rise ◽  
Tubular Morphology

Effects of temperature and Zn2+ on the isometric contractile properties of toe muscle fibers of Rana catesbeiana and Xenopus laevis were studied. The maximum twitch tension almost doubled when the temperature was lowered from 20 to 4 °C in Rana muscles but not in Xenopus muscles, although the duration of action potential in Xenopus muscle was increased slightly more than that seen in the Rana species. The maximum rate of rise of tension was greater in Xenopus muscle than in the Rana muscle, at 20 °C. The prolongation of the time-to-peak tension following exposure to low temperature (4 °C) was more pronounced in Rana than in Xenopus muscles. These results suggest that the speed of release and reuptake of Ca2+ by the sarcoplasmic reticulum (SR) differs in Rana and Xenopus muscles and that these factors may be related to differences in the SR and the T-tubular morphology. In Rana muscles, Zn2+ prolonged the falling phase of the action potential and potentiated the twitch tension. In Xenopus muscles, Zn2+ marginally prolonged the duration of action potential and the twitch tension was not markedly potentiated. These results indicate that Zn2+ potentiates the twitch tension by prolonging the action potential and that Rana muscles are more sensitive to the effects of Zn2+.

scholarly journals Double Sucrose-Gap Method Applied to Single Muscle Fiber of Xenopus laevis

1974 ◽  
Vol 63 (2) ◽  
pp. 235-256 ◽  
Author(s):  
Shigehiro Nakajima ◽  
Joseph Bastian
Keyword(s):  
Electrical Properties ◽  
Action Potential ◽  
Muscle Fiber ◽  
Time Course ◽  
Muscle Fibers ◽  
Membrane Conductance ◽  
Frog Muscle ◽  
Muscle Twitch ◽  
Sucrose Gap ◽  
Isotonic Shortening

Passive electrical properties (internal conductance, membrane conductance, low frequency capacity, and high frequency capacity obtained from the foot of the action potential) of normal and glycerol-treated muscle of Xenopus were determined with the intracellular microelectrode technique. The results show that the electrical properties of Xenopus muscle are essentially the same as those of frog muscle. Characteristics of the action potential of Xenopus muscle were also similar to those of frog muscle. Twitch tension of glycerol-treated muscle fibers of Xenopus recovered partially when left in normal Ringer for a long time (more than 6 h). Along with the twitch recovery, the membrane capacity increased. Single isolated muscle fibers of Xenopus were subjected to the double sucrose-gap technique. Action potentials under the sucrose gap were not very different from those obtained with the intracellular electrode, except for the sucrose-gap hyperpolarization and a slight tendency toward prolongation of the shape of action potential. Twitch contraction of the artificial node was recorded as a change of force from one end of the fiber under the sucrose gap. From the time-course of the recorded force and the sinusoidal stress-strain relationship at varying frequencies of the resting muscle fiber, the time-course of isotonic shortening of the node was recovered by using Fourier analysis. It was revealed that the recorded twitch force can approximately be regarded as isotonic shortening of the node.

scholarly journals Inhibition of Ca2+-activated large-conductance K+ channel activity alters synaptic AMPA receptor phenotype in mouse cerebellar stellate cells

2011 ◽  
Vol 106 (1) ◽  
pp. 144-152 ◽  
Author(s):  
Yu Liu ◽  
Iaroslav Savtchouk ◽  
Shoana Acharjee ◽  
Siqiong June Liu
Keyword(s):  
Potassium Channels ◽  
Action Potential ◽  
Action Potential Duration ◽  
Action Potentials ◽  
Channel Blocker ◽  
Stellate Cells ◽  
Bk Channels ◽  
Bk Channel ◽  
K Channel ◽  
Duration Of Action

Many fast-spiking inhibitory interneurons, including cerebellar stellate cells, fire brief action potentials and express α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA)-type glutamate receptors (AMPAR) that are permeable to Ca2+ and do not contain the GluR2 subunit. In a recent study, we found that increasing action potential duration promotes GluR2 gene transcription in stellate cells. We have now tested the prediction that activation of potassium channels that control the duration of action potentials can suppress the expression of GluR2-containing AMPARs at stellate cell synapses. We find that large-conductance Ca2+-activated potassium (BK) channels mediate a large proportion of the depolarization-evoked noninactivating potassium current in stellate cells. Pharmacological blockade of BK channels prolonged the action potential duration in postsynaptic stellate cells and altered synaptic AMPAR subtype from GluR2-lacking to GluR2-containing Ca2+-impermeable AMPARs. An L-type channel blocker abolished an increase in Ca2+ entry that was associated with spike broadening and also prevented the BK channel blocker-induced switch in AMPAR phenotype. Thus blocking BK potassium channels prolongs the action potential duration and increases the expression of GluR2-containing receptors at the synapse by enhancing Ca2+ entry in cerebellar stellate cells.

Cellular mechanisms of fatigue in skeletal muscle

1991 ◽  
Vol 261 (4) ◽  
pp. 1-1 ◽  
Author(s):  
H. Westerblad ◽  
J. A. Lee ◽  
J. Läuml;nnergren ◽  
D. G. Allen
Keyword(s):  
Skeletal Muscle ◽  
Action Potential ◽  
Creatine Phosphokinase ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Cellular Mechanisms ◽  
Left Hand ◽  
Hand Column ◽  
Right Hand ◽  
On Line

Pages C195–C209: H. Westerblad, J. A. Lee, J. Lännergren, and D. G. Allen. “Cellular mechanisms of fatigue in skeletal muscle.” Page C198, left-hand column, paragraph 2, sentence beginning on line 15 should read: If the creatine phosphokinase reaction is assumed to be at equilibrium, a calculation of free ADP reveals an increase from ≈30 to 200 μM (27). Page C198, right-hand column, paragraph 3, sentence beginning on line 3 should read: From measurements in frog muscle fibers it has been calculated that for each action potential there would be an increase in the intracellular Na+ concentration ([Na+]i) of ≈7.7 μM and a decrease of the intracellular K+ concentration ([K+]i) of ap4.7 μM (52).

scholarly journals The Influence of Sodium-Free Solutions on the Membrane Potential of Frog Muscle Fibers

1963 ◽  
Vol 47 (1) ◽  
pp. 117-132 ◽  
Author(s):  
L. J. Mullins ◽  
K. Noda
Keyword(s):  
Membrane Potential ◽  
Activity Coefficients ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Sartorius Muscle ◽  
Coupling Ratio ◽  
Nernst Equation ◽  
Ringer’S Solution ◽  
Na Efflux ◽  
Frog Sartorius

The membrane potential of frog sartorius muscle fibers in a Cl- and Na-free Ringer's solution when sucrose replaces NaCl is about the same as that in normal Ringer's solution. The K+ efflux is also about the same in the two solutions but muscles lose K and PO4 in sucrose Ringer's solutions. The membrane potential in sucrose Ringer's solution is equal to that given by the Nernst equation for a K+ electrode, when corrections are made for the activity coefficients for K+ inside and outside the fiber. For a muscle in normal Ringer's solution, the measured membrane potential is within a few millivolts of EK. This finding is incompatible with a 1:1 coupled Na-K pump. It is consistent with either no coupling of Na efflux to K influx, or a coupling ratio of 3 or greater.

scholarly journals Loss of the Plateau of the Cardiac Action Potential in Hypertonic Solutions

1972 ◽  
Vol 59 (6) ◽  
pp. 779-793 ◽  
Author(s):  
Kent Hermsmeyer ◽  
Russell Rulon ◽  
Nick Sperelakis
Keyword(s):  
Guinea Pig ◽  
Action Potential ◽  
Surface Membrane ◽  
Muscle Fibers ◽  
Input Resistance ◽  
Cell Diameter ◽  
Hypertonic Solution ◽  
Myocardial Cells ◽  
Hypertonic Solutions ◽  
T Tubules

The effect of hypertonicity on the electrical properties of vertebrate myocardial cells was studied in ventricular muscle fibers of guinea pig, cat, frog, and chicken. The latter two species do not have a T-tubule system, whereas the former two do. In hypertonic solutions (2 x isotonic) produced by addition of sucrose or excess of NaCl, cell diameter decreased and there was a slight hyperpolarization and decrease in action potential overshoot. In guinea pig and cat, the hypertonic solution caused a decrease in input resistance and the plateau of the action potential to disappear in some of the cells; contractions of the entire ventricle also became depressed. These effects were reversed by returning the muscle fibers to isotonic solution. Addition of 5 mM SrCl2 to the hypertonic solution also caused the plateau component and contraction to reappear. In frog and chick cells, loss of the plateau component and contraction never occurred in hypertonic solution, and input resistance increased. Urea and glycerol hyperosmolarity (2 x) caused no loss of the plateau component or contraction. If the frog and chicken ventricular, and guinea pig atrial myocardial cells (all of which lack T tubules) were to serve as an adequate control for possible effects of hypertonicity on the surface membrane and on contractile proteins, then the results suggest that swelling of the T tubules of mammalian myocardial cells leads to loss of the plateau component.

Mechanical threshold and inactivation in denervated frog muscle

1973 ◽  
Vol 225 (1) ◽  
pp. 171-176 ◽  
Author(s):  
BD Lindley ◽  
AC Kirby ◽  
SC Stuesse ◽  
Picken
Keyword(s):  
Frog Muscle ◽  
Mechanical Threshold ◽  
Denervated Frog Muscle

scholarly journals Globular and asymmetric acetylcholinesterase in frog muscle basal lamina sheaths.

1986 ◽  
Vol 102 (3) ◽  
pp. 762-768 ◽  
Author(s):  
M Nicolet ◽  
M Pinçon-Raymond ◽  
F Rieger
Keyword(s):  
Basal Lamina ◽  
Acetylcholine Receptors ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Motor Endplate ◽  
Molecular Forms ◽  
Nonionic Detergent ◽  
Plasmic Membrane ◽  
Triton X

After denervation in vivo, the frog cutaneus pectoris muscle can be led to degenerate by sectioning the muscle fibers on both sides of the region rich in motor endplate, leaving, 2 wk later, a muscle bridge containing the basal lamina (BL) sheaths of the muscle fibers (28). This preparation still contains various tissue remnants and some acetylcholine receptor-containing membranes. A further mild extraction by Triton X-100, a nonionic detergent, gives a pure BL sheath preparation, devoid of acetylcholine receptors. At the electron microscope level, this latter preparation is essentially composed of the muscle BL with no attached plasmic membrane and cellular component originating from Schwann cells or macrophages. Acetylcholinesterase is still present in high amounts in this BL sheath preparation. In both preparations, five major molecular forms (18, 14, 11, 6, and 3.5 S) can be identified that have either an asymmetric or a globular character. Their relative amount is found to be very similar in the BL and in the motor endplate-rich region of control muscle. Thus, observations show that all acetylcholinesterase forms can be accumulated in frog muscle BL.

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