A study of excitation-contraction coupling in frog tonic muscle fibers ofRana temporaria

1972 ◽  
Vol 28 (11) ◽  
pp. 1305-1306 ◽  
Author(s):  
G. A. Nasledov ◽  
J. E. Mandelstam ◽  
T. L. Radzjukewich
Keyword(s):  
Muscle Fibers ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Tonic Muscle ◽  
Ofrana Temporaria

scholarly journals T-tubule disorganization and defective excitation-contraction coupling in muscle fibers lacking myotubularin lipid phosphatase

2009 ◽  
Vol 106 (44) ◽  
pp. 18763-18768 ◽  
Author(s):  
L. Al-Qusairi ◽  
N. Weiss ◽  
A. Toussaint ◽  
C. Berbey ◽  
N. Messaddeq ◽  
...  
Keyword(s):  
Muscle Fibers ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Lipid Phosphatase

Extracellular divalent cations in excitation–contraction coupling: hypertonic solution effects

1982 ◽  
Vol 60 (4) ◽  
pp. 440-445
Author(s):  
Isao Oota ◽  
Isao Kosaka ◽  
Torao Nagai ◽  
Hideyo Yabu
Keyword(s):  
Skeletal Muscle ◽  
Divalent Cations ◽  
Muscle Fibers ◽  
Hypertonic Solution ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Skeletal Muscle Fibers ◽  
Membrane Bound

It is the purpose of this article to point out that the membrane-bound Ca plays an important role in excitation–contraction (E–C) coupling of skeletal muscle fibers and that other divalent cations are unable to substitute for this role of membrane-bound Ca.

Effects of hypertonic solutions on contraction of frog tonic muscle fibers

1984 ◽  
Vol 246 (1) ◽  
pp. C148-C153 ◽  
Author(s):  
R. E. Godt ◽  
A. C. Kirby ◽  
A. M. Gordon
Keyword(s):  
Ionic Strength ◽  
Rana Pipiens ◽  
Muscle Fibers ◽  
Contractile Apparatus ◽  
Cross Sectional ◽  
Coupling Process ◽  
Contraction Coupling ◽  
Tonic Muscle ◽  
High K ◽  
The Media

The influence of solution hypertonicity on contraction was studied in small bundles of tonic muscle fibers from the iliofibularis muscle of the frog Rana pipiens. Muscles were activated with high-K+ solutions that had osmolalities which were increased with tris(hydroxymethyl)aminomethanepropionate. Peak potassium contracture force decreased monotonically with tonicity and was zero in solutions with 2.5 or 3 times the osmolality of control Ringer. Contracture force at all tonicities studied (less than or equal to 3 X Ringer) was increased by increasing Ca2+ in the media 10-fold (to 20 mM) and/or by adding caffeine (10-20 mM). Nevertheless, this potentiated force also was diminished as tonicity increased. Force of single, mechanically skinned tonic fibers taken from these bundles was activated by Ca2+ over the same concentration range as that of twitch fibers. Moreover, maximal Ca2+-activated force, normalized per cross-sectional area, was similar in skinned tonic and twitch fibers. As was shown previously in twitch fibers, maximal Ca2+-activated force was decreased when ionic strength was increased. These data suggest that, as with twitch fibers, increased tonicity depresses contraction of tonic fibers by increasing the intracellular ionic strength, which in turn inhibits the ability of the contractile apparatus to generate force. Unlike twitch fibers, however, disruption of the excitation-contraction coupling process probably plays a more significant role in the action of hypertonicity on tonic fibers.

Effects of K+ on the twitch and tetanic contraction in the sartorius muscle of the frog, Rana pipiens. Implication for fatigue in vivo

1992 ◽  
Vol 70 (9) ◽  
pp. 1236-1246 ◽  
Author(s):  
Jean Marc Renaud ◽  
Peter Light
Keyword(s):  
Action Potential ◽  
Action Potentials ◽  
Muscle Fibers ◽  
Resting Potential ◽  
Sartorius Muscle ◽  
Coupling Mechanism ◽  
Tetanic Force ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
The Mean

The effects of increasing the extracellular K+ concentration on the capacity to generate action potentials and to contract were tested on unfatigued muscle fibers isolated from frog sartorius muscle. The goal of this study was to investigate further the role of K+ in muscle fatigue by testing whether an increased extracellular K+ concentration in unfatigued muscle fibers causes a decrease in force similar to the decrease observed during fatigue. Resting and action potentials were measured with conventional microelectrodes. Twitch and tetanic force was elicited by field stimulation. At pHo (extracellular pH) 7.8 and 3 mmol K+∙L−1 (control), the mean resting potential was −86.6 ± 1.7 mV (mean ± SEM) and the mean overshoot of the action potential was 5.6 ± 2.5 mV. An increased K+ concentration from 3 to 8.0 mmol∙L−1 depolarized the sarcolemma to −72.2 ± 1.4 mV, abolished the overshoot as the peak potential during an action potential was −12.0 ± 3.9 mV, potentiated the twitch force by 48.0 ± 5.7%, but did not affect the tetanic force (maximum force) and the ability to maintain a constant force during the plateau phase of a tetanus. An increase to 10 mmol K+∙L−1 depolarized the sarcolemma to −70.1 ± 1.7 mV and caused large decreases in twitch (31.6 ± 26.1%) and tetanic (74.6 ± 12.1%) force. Between 3 and 9 mmol K+∙L−1, the effects of K+ at pHo 7.2 (a pHo mimicking the change in interstitial pH during fatigue) and 6.4 (a pHo known to inhibit force recovery following fatigue) on resting and action potentials as well as on the twitch and tetanic force were similar to those at pHo 7.8. Above 9 mmol K+∙L−1 significant differences were found in the effect of K+ between pHo 7.8 and 7.2 or 6.4. In general, the decrease in peak action potential and twitch and tetanic force occurred at higher K+ concentrations as the pHo was more acidic. The results obtained in this study do not support the hypothesis that an accumulation of K+ at the surface of the sarcolemma is sufficiently large to suppress force development during fatigue. The possibility that the K+ concentration in the T tubules reaches the critical K+ concentration necessary to cause a failure of the excitation–contraction coupling mechanism is discussed.Key words: excitation–contraction coupling, fatigue, potassium, tetanus, twitch.

Sign in / Sign up

Export Citation Format

Share Document