scholarly journals Calcium-gated calcium channels in sarcoplasmic reticulum of rabbit skinned skeletal muscle fibers.

1986 ◽  
Vol 87 (2) ◽  
pp. 289-303 ◽  
Author(s):  
P Volpe ◽  
G Salviati ◽  
A Chu
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Isometric Force ◽  
Muscle Fibers ◽  
Ruthenium Red ◽  
Scattering Method ◽  
Tension Development ◽  
Maximal Force ◽  
Skeletal Muscle Fibers ◽  
Ca2 Channels

The action of ruthenium red (RR) on Ca2+ loading by and Ca2+ release from the sarcoplasmic reticulum (SR) of chemically skinned skeletal muscle fibers of the rabbit was investigated. Ca2+ loading, in the presence of the precipitating anion pyrophosphate, was monitored by a light-scattering method. Ca2+ release was indirectly measured by following tension development evoked by caffeine. Stimulation of the Ca2+ loading rate by 5 microM RR was dependent on free Ca2+, being maximal at pCa 5.56. Isometric force development induced by 5 mM caffeine was reversibly antagonized by RR. IC50 for the rate of tension rise was 0.5 microM; that for the extent of tension was 4 microM. RR slightly shifted the steady state isometric force/pCa curve toward lower pCa values. At 5 microM RR, the pCa required for half-maximal force was 0.2 log units lower than that of the control, and maximal force was depressed by approximately 16%. These results suggest that RR inhibited Ca2+ release from the SR and stimulated Ca2+ loading into the SR by closing Ca2+-gated Ca2+ channels. Previous studies on isolated SR have indicated the selective presence of such channels in junctional terminal cisternae.

Differential Effects of Sevoflurane, Isoflurane, and Halothane on Ca (2+) Release from the Sarcoplasmic Reticulum of Skeletal Muscle 

1999 ◽  
Vol 91 (1) ◽  
pp. 179-186 ◽  
Author(s):  
Gudrun Kunst ◽  
Bernhard M. Graf ◽  
Rupert Schreiner ◽  
Eike Martin ◽  
Rainer H. A. Fink
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibers ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Maximal Force ◽  
Skinned Muscle ◽  
Skeletal Muscle Fibers ◽  
Force Relation ◽  
The Individual

Background Although malignant hyperthermia after application of sevoflurane has been reported, little is known about its action on intracellular calcium homeostasis of skeletal muscle. The authors compared the effect of sevoflurane with that of isoflurane and halothane on Ca2+ release of mammalian sarcoplasmic reticulum and applied a novel method to quantify Ca2+ turnover in permeabilized skeletal muscle fibers. Methods Liquid sevoflurane, isoflurane, and halothane at 0.6 mM, 3.5 mM, and 7.6 mm were diluted either in weakly calcium buffered solutions with no added Ca2+ (to monitor Ca2+ release) or in strongly Ca2+ buffered solutions with [Ca2+] values between 3 nM and 24.9 microm for [Ca+]-force relations. Measurements were taken on single saponin skinned muscle fiber preparations of BALB/c mice. Individual [Ca2+]force relations were characterized by the Ca2+ concentration at half-maximal force that indicates the sensitivity of the contractile proteins and by the steepness. Each force transient was transformed directly into a Ca2+ transient with respect to the individual [Ca2+]-force relation of the fiber. Results At 0.6 mM, single force transients induced by sevoflurane were lower compared with equimolar concentrations of isoflurane and halothane (P < 0.05). Similarly, calculated peak Ca2+ transients of sevoflurane were lower than those induced by equimolar halothane (P < 0.05). The Ca2+ concentrations at half maximal force were decreased after the addition of sevoflurane, isoflurane, and halothane in a concentration-dependent manner (P < 0.05). Conclusion Whereas sevoflurane, isoflurane, and halothane similarly increase the Ca2+ sensitivity of the contractile apparatus in skeletal muscle fibers, 0.6 mM sevoflurane induces smaller Ca2+ releases from the sarcoplasmic reticulum than does equimolar halothane.

Injury to skeletal muscle fibers of mice following lengthening contractions

1985 ◽  
Vol 59 (1) ◽  
pp. 119-126 ◽  
Author(s):  
K. K. McCully ◽  
J. A. Faulkner
Keyword(s):  
Skeletal Muscle ◽  
Isometric Force ◽  
Muscle Fibers ◽  
Lengthening Contractions ◽  
Control Value ◽  
Skeletal Muscle Fibers ◽  
Maximum Isometric Force ◽  
Distal Tendon ◽  
Shortening Contractions

We tested the hypothesis that lengthening contractions result in greater injury to skeletal muscle fibers than isometric or shortening contractions. Mice were anesthetized with pentobarbital sodium and secured to a platform maintained at 37 degrees C. The distal tendon of the extensor digitorum longus muscle was attached to a servomotor. A protocol consisting of isometric, shortening, or lengthening contractions was performed. After the contraction protocol the distal tendon was reattached, incisions were closed, and the mice were allowed to recover. The muscles were removed after 1–30 days, and maximum isometric force (Po) was measured in vitro at 37 degrees C. Three days after isometric and shortening contractions and sham operations, histological appearance was not different from control and Po was 80% of the control value. Three days after lengthening contractions, histological sections showed that 37 +/- 4% of muscle fibers degenerated and Po was 22 +/- 3% of the control value. Muscle regeneration, first seen at 4 days, was nearly complete by 30 days, when Po was 84 +/- 3% of the control value. We conclude that, with the protocol used, lengthening, but not isometric or shortening contractions, caused significant injury to muscle fibers.

beta-Adrenergic modulation of Ba2+ currents and K+ contractures in frog slow skeletal muscle fibers

1997 ◽  
Vol 272 (1) ◽  
pp. C77-C81 ◽  
Author(s):  
M. Huerta ◽  
X. Trujillo ◽  
C. Vasquez
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Isometric Tension ◽  
External Application ◽  
Beta Adrenergic ◽  
Cyclic Monophosphate ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Adrenergic Modulation ◽  
Ca2 Channels

beta-Adrenergic modulation of the Ba2+ current (IBa) and K+ contracture in slow skeletal muscle fibers of the frog (Rana pipiens) were investigated in intact fibers with the three-microelectrode voltage-clamp technique and isometric tension measurements. Application of epinephrine (10(-6) to 10(-5) M) to the bath increased the amplitude of IBa. This increase was blocked by the beta-antagonist propranolol (3 microM), and a similar increase was observed with the beta-specific agonist isoproterenol (1 microM). Thus the epinephrine effect was mediated mainly by beta-adrenergic receptors. External application of permeable 8-bromoadenosine 3',5'-cyclic monophosphate (0.5 mM) increased the amplitude of both IBa and K+ contractures. The present results suggest that beta-adrenergic modulation of IBa in slow skeletal muscle fibers could reflect a modulation of Ca2+ channels via adenosine 3',5'-cyclic monophosphate (cAMP). cAMP (0.5 mM) also potentiated the K(+)-evoked tension in these slow fibers. The physiological contribution made by the modulation of slow skeletal muscle Ca2+ channels to the increase in tension is still not completely understood.

scholarly journals Block of single L-type Ca2+ channels in skeletal muscle fibers by aminoglycoside antibiotics.

1996 ◽  
Vol 107 (3) ◽  
pp. 421-432 ◽  
Author(s):  
C M Haws ◽  
B D Winegar ◽  
J B Lansman
Keyword(s):  
Skeletal Muscle ◽  
Single Channel ◽  
Muscle Fibers ◽  
External Solution ◽  
Bimolecular Reaction ◽  
Aminoglycoside Antibiotics ◽  
Ion Concentration ◽  
Ion Flow ◽  
Skeletal Muscle Fibers ◽  
Ca2 Channels

The activity of single L-type Ca2+ channels was recorded from cell-attached patches on acutely isolated skeletal muscle fibers from the mouse. The experiments were concerned with the mechanism by which aminoglycoside antibiotics inhibit ion flow through the channel. Aminoglycosides produced discrete fluctuations in the single-channel current when added to the external solution. The blocking kinetics could be described as a simple bimolecular reaction between an aminoglycoside molecule and the open channel. The blocking rate was found to be increased when either the membrane potential was made more negative or the concentration of external permeant ion was reduced. Both of these effects are consistent with a blocking site that is located within the channel pore. Other features of block, however, were incompatible with a simple pore blocking mechanism. Hyperpolarization enhanced the rate of unblocking, even though an aminoglycoside molecule must dissociate from its binding site in the channel toward the external solution against the membrane field. Raising the external permeant ion concentration also enhanced the rate of unblocking. This latter finding suggests that aminglycoside affinity is modified by repulsive interactions that arise when the pore is simultaneously occupied by a permeant ion and an aminoglycoside molecule.

Evidence for Na+/Ca2+exchange in intact single skeletal muscle fibers from the mouse

1998 ◽  
Vol 274 (4) ◽  
pp. C940-C946 ◽  
Author(s):  
Christopher D. Balnave ◽  
David G. Allen
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibers ◽  
Exchange Mechanism ◽  
Initial Exposure ◽  
Mouse Skeletal Muscle ◽  
Reverse Mode ◽  
Skeletal Muscle Fibers ◽  
Plateau Level ◽  
Sustained Increase

The myoplasmic free Ca2+concentration ([Ca2+]i) was measured in intact single fibers from mouse skeletal muscle with the fluorescent Ca2+ indicator indo 1. Some fibers were perfused in a solution in which the concentration of Na+ was reduced from 145.4 to 0.4 mM (low-Na+solution) in an attempt to activate reverse-mode Na+/Ca2+exchange (Ca2+ entry in exchange for Na+ leaving the cell). Under normal resting conditions, application of low-Na+ solution only increased [Ca2+]iby 5.8 ± 1.8 nM from a mean resting [Ca2+]iof 42 nM. In other fibers, [Ca2+]iwas elevated by stimulating sarcoplasmic reticulum (SR) Ca2+ release with caffeine (10 mM) and by inhibiting SR Ca2+ uptake with 2,5-di( tert-butyl)-1,4-benzohydroquinone (TBQ; 0.5 μM) in an attempt to activate forward-mode Na+/Ca2+exchange (Ca2+ removal from the cell in exchange for Na+ influx). These two agents caused a large increase in [Ca2+]i, which then declined to a plateau level approximately twice the baseline [Ca2+]iover 20 min. If the cell was allowed to recover between exposures to caffeine and TBQ in a solution in which Ca2+ had been removed, the increase in [Ca2+]iduring the second exposure was very low, suggesting that Ca2+ had left the cell during the initial exposure. Application of caffeine and TBQ to a preparation in low-Na+ solution produced a large, sustained increase in [Ca2+]iof ∼1 μM. However, when cells were exposed to caffeine and TBQ in a low-Na+ solution in which Ca2+ had been removed, a sustained increase in [Ca2+]iwas not observed, although [Ca2+]iremained higher and declined slower than in normal Na+ solution. This suggests that forward-mode Na+/Ca2+exchange contributed to the fall of [Ca2+]iin normal Na+ solution, but when extracellular Na+ was low, a prolonged elevation of [Ca2+]icould activate reverse-mode Na+/Ca2+exchange. The results provide evidence that skeletal muscle fibers possess a Na+/Ca2+exchange mechanism that becomes active in its forward mode when [Ca2+]iis increased to levels similar to that obtained during contraction.

Characteristics of phosphate-induced Ca2+ efflux from the SR in mechanically skinned rat skeletal muscle fibers

2000 ◽  
Vol 278 (1) ◽  
pp. C126-C135 ◽  
Author(s):  
Adrian M. Duke ◽  
Derek S. Steele
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Muscle Fibers ◽  
Cyclopiazonic Acid ◽  
Creatine Phosphate ◽  
Ruthenium Red ◽  
Rat Skeletal Muscle ◽  
Atpase Inhibitor ◽  
Skeletal Muscle Fibers ◽  
Efflux Pathway

The effects of Pi on sarcoplasmic reticulum (SR) Ca2+ regulation were studied in mechanically skinned rat skeletal muscle fibers. Brief application of caffeine was used to assess the SR Ca2+ content, and changes in concentration of Ca2+([Ca2+]) within the cytosol were detected with fura 2 fluorescence. Introduction of Pi (1–40 mM) induced a concentration-dependent Ca2+ efflux from the SR. In solutions lacking creatine phosphate (CP), the amplitude of the Pi-induced Ca2+ transient approximately doubled. A similar potentiation of Pi-induced Ca2+ release occurred after inhibition of creatine kinase (CK) with 2,4-dinitrofluorobenzene. In the presence of ruthenium red or ryanodine, caffeine-induced Ca2+ release was almost abolished, whereas Pi-induced Ca2+ release was unaffected. However, introduction of the SR Ca2+ ATPase inhibitor cyclopiazonic acid effectively abolished Pi-induced Ca2+ release. These data suggest that Pi induces Ca2+ release from the SR by reversal of the SR Ca2+ pump but not via the SR Ca2+ channel under these conditions. If this occurs in intact skeletal muscle during fatigue, activation of a Ca2+efflux pathway by Pi may contribute to the reported decrease in net Ca2+ uptake and increase in resting [Ca2+].

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