scholarly journals Cross-Bridges and Sarcomere Stiffness in Single Intact Frog Muscle Fibers

2010 ◽  
Vol 98 (3) ◽  
pp. 348a
Author(s):  
Giovanni Cecchi ◽  
Barbara Colombini ◽  
Marta Nocella ◽  
Giulia Benelli ◽  
Maria Angela Bagni
Keyword(s):  
Muscle Fibers ◽  
Frog Muscle ◽  
Cross Bridges

Effects of BAPTA on force and Ca2+ transient during isometric contraction of frog muscle fibers

1998 ◽  
Vol 275 (2) ◽  
pp. C375-C381 ◽  
Author(s):  
Y.-B. Sun ◽  
C. Caputo ◽  
K. A. P. Edman
Keyword(s):  
Mechanical Performance ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Clear Correlation ◽  
Bathing Solution ◽  
Control Value ◽  
Contractile System ◽  
Intracellular Ca ◽  
Cross Bridges ◽  
Reduced State

The effects of 1,2-bis(2-aminophenoxy)ethane- N, N, N′, N′-tetraacetic acid (BAPTA) on force and intracellular Ca2+ transient were studied during isometric twitches and tetanuses in single frog muscle fibers. BAPTA was added to the bathing solution in its permeant AM form (50 and 100 μM). There was no clear correlation between the changes in force and the changes in Ca2+ transient. Thus during twitch stimulation BAPTA did not suppress the Ca2+ transient until the force had been reduced to <50% of its control value. At the same time, the peak myoplasmic free Ca2+concentration reached during tetanic stimulation was markedly increased, whereas the force was slightly reduced by BAPTA. The effects of BAPTA were not duplicated by using another Ca2+ chelator, EGTA, indicating that BAPTA may act differently as a Ca2+ chelator. Stiffness measurements suggest that the decrease in mechanical performance in the presence of BAPTA is attributable to a reduced number of active cross bridges. The results could mean that BAPTA, under the conditions used, inhibits the binding of Ca2+ to troponin C resulting in a reduced state of activation of the contractile system.

scholarly journals Weakly attached cross-bridges in relaxed frog muscle fibers

1989 ◽  
Vol 55 (4) ◽  
pp. 605-619 ◽  
Author(s):  
D.W. Jung ◽  
T. Blangé ◽  
H. de Graaf ◽  
B.W. Treijtel
Keyword(s):  
Muscle Fibers ◽  
Frog Muscle ◽  
Cross Bridges

Role of calcium and cross bridges in determining rate of force development in frog muscle fibers

1997 ◽  
Vol 272 (5) ◽  
pp. C1664-C1671 ◽  
Author(s):  
P. A. Wahr ◽  
J. A. Rall
Keyword(s):  
Isometric Force ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Rate Of Force Development ◽  
Force Development ◽  
Double Exponential ◽  
Maximum Activation ◽  
Cross Bridges ◽  
Kinetics Of

The influence of Ca2+ and force-generating cross bridges on the kinetics of force development was examined in skinned frog muscle fibers activated by photolytic release of Ca2+ from caged Ca2+ at 10 degrees C. Isometric force development was fit by a double exponential equation with rates of 44.4 s-1 (kc1) and 6.1 s-1 (kc2); kc1 was not significantly different from the rate of force development observed in intact fibers. Maximum activation by caged Ca2+ from preexisting submaximal force produced rates of contraction similar to those observed with maximum activation from zero force. Decreasing the Ca2+ level to an extent that resulted in 50% of maximum force development produced an approximately sevenfold decrease in kc1 and no change in kc2. Partial extraction of troponin C reduced kc1 only slightly (by 16%), whereas decreasing the number of force-generating cross bridges by vanadate did not decrease kc1. Neither treatment altered kc2. Thus the rate of force development increases dramatically with increases in Ca2+ level.

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.

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.

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