Calcium and magnesium contents and volume of the terminal cisternae in caffeine-treated skeletal muscle.

Yoshioka, Toshitada; Somlyo, Andrew P.

doi:10.1083/jcb.99.2.558

Cited by 39 publications

(21 citation statements)

References 80 publications

(155 reference statements)

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“…Structural changes in the sarcomere of the detergenttreated muscle during caffeine-RCC included overstretching and supercontracture of the sarcomeres. These changes are similar to those seen in contractures by caffeine (EISENBERG and EISENBERG, 1982;Y0SHI0KA and SOMLYO, 1984), quinine (YOsHIOKA et al, 1984b), and potassium (EISENBERG and EISENBERG, 1982). It seems that the sarcomeres do not contract all at once, despite the very short time course of the tension development.…”

Section: Discussionsupporting

confidence: 65%

The effects of detergent on the contractility and ultrastructure of frog skeletal muscle.

et al. 1986

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The contractility of detergent-treated frog skeletal muscle and its ultrastructure were studied. Triton X-100 and Brij-58 were used as nonionic surface active substances. The concentrations of the detergent solutions were adjusted so that the trains of the twitch tensions would continue for about 10 min. The duration of the twitch tensions was about 10 min when the muscles were soaked in 0.1 mM (0.006%) Triton or in 2.5 mM (0.280%) Brij solution. The twitch tensions did not recover upon returning the muscles to the normal Ringer solution after treatment of the detergents. Rapid cooling of muscle that had been soaked in a 1.0 mM caffeine Ringer solution for 10 min provoked a marked contracture (RCC) in 0.1-0.2 mM Triton-treated preparation. No such contracture was obtained in 1.0-2.5 mM Brij-treated preparation. In ultrastructural findings of the Triton-treated muscle, some structural changes were observed in the transverse tubule and the junctional gap, but not in the terminal cisternae. Brij-treated muscle showed damage of each of these membranes, including the terminal cisternae. These findings suggest that the two detergents have different surface activities on the internal membrane system of the skeletal muscle. The biological activities of the membrane remained even after the treatment of Triton with a suitable concentration.

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Section: Discussionsupporting

confidence: 65%

The effects of detergent on the contractility and ultrastructure of frog skeletal muscle.

et al. 1986

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“…4) (Su & Hasselbach, 1984) ST fibres is more highly loaded with Ca2' at rest (Sitsapesan & Williams, 1995 (Yoshioka & Somlyo, 1984).…”

Section: Sensitivity Of the Ca2+ Content Techniquementioning

confidence: 99%

Total and sarcoplasmic reticulum calcium contents of skinned fibres from rat skeletal muscle.

Fryer

Stephenson

1996

The Journal of Physiology

179

306

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1. The Ca2+ content of single mammalian skeletal muscle fibres was determined using a novel technique. Mechanically skinned fibres were equilibrated with varying amounts of the Ca2+ buffer BAPTA and were then lysed in a detergent-paraffin oil emulsion. The subsequent myofilament force response was used to estimate the additional amount of Ca2+ bound to BAPTA following lysis of intracellular membranes. 2. The total endogenous Ca2± content (corrected for endogenous Ca2+ buffering) of fast-twitch (FT) and slow-twitch (ST) fibres at a myoplasmic pCa (-log [Ca2+]) of 7-15 was 1 32 + 0-02 and 1P35 + 0-08 mm per fibre volume, respectively. The sarcoplasmic reticulum (SR) component of these estimates was calculated as 1P01 and 1P14 mm, respectively, which normalized to SR volume corresponds to resting SR Ca2P contents of 11 and 21 mm, respectively.3. Equilibration of 'resting' fibres with low myoplasmic [Ca2+] (pCa 7 67-9 00) elicited a timedependent decrease in Ca2P content in both fibre types. Equilibration of resting fibres with higher myoplasmic [Ca2+] (pCa 5 96-6 32) had no effect on the Ca2P content of ST fibres but increased the Ca2+ content of FT fibres. The maximum steady-state total Ca2P content (3-85 mM) was achieved in FT fibres after 3 min equilibration at pCa 5-96. Equilibration at higher myoplasmic [Ca2+] was less effective, probably due to Ca2+-induced Ca2+ release from the SR. 4. Exposure of fibres to either caffeine (30 mm, pCa -8, 2 min) or low myoplasmic [Mg2+] (0 05 mm, pCa -9, 1 min) released approximately 85 % of the resting SR Ca2P content. The ability of caffeine to release SR Ca2+ was dependent on the myoplasmic Ca2P buffering conditions.5. The results demonstrate that the SR of ST fibres is saturated with Ca2P at resting myoplasmic [Ca2+] while the SR of FT fibres is only about one-third saturated with Ca2P under equivalent conditions. These differences suggest that the rate of SR Ca2P uptake in FT fibres is predominantly controlled by myoplasmic [Ca2+] while that of ST fibres is more likely to be limited by the [Ca2+] within the SR lumen.The time course of the contraction-relaxation cycle of skeletal muscle is greatly influenced by the function of the sarcoplasmic reticulum (SR), which acts to both release and to re-sequester intracellular calcium ions. Some aspects of SR function in mammalian skeletal muscle have been ascertained from the simultaneous measurement of the myoplasmic free calcium ion concentration ([Ca2+]i) and force output of intact fibres (Fryer & Neering, 1986;Westerblad & Allen, 1991 ([Ca2K]SR), which is a key determinant of: (i) the rate of Ca2+ loss through SR Ca2+ release channels (Feher & Briggs, 1982;Sitsapesan & Williams, 1995), and (ii) the activity of the SR Ca2+ pump (Inesi & De Meis, 1989 (Fryer & Stephenson, 1993a,b;. METHODSSkinned muscle fibre preparation Skinned fibres were prepared using methods previously decribed in detail (Fink, Stephenson & Williams, 1986). Male Long-Evans hooded rats (Rattus norvegicus; 5-12 months old) were killed by dieth...

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“…In caffeine contracture, fibres are sometimes easily damaged. This might be caused by local contractions (Yoshioka & Somlyo, 1984), which are due to slower activation by caffeine, and do not appear during electrical stimulation. However, the change of temperature is much faster than the diffusion of caffeine in the cell, and thus the activation in rapid cooling contracture is faster than that of caffeine contracture.…”

Section: Effects Of [Ca2+]0 On Rapid Cooling Contracturementioning

confidence: 99%

Change in intracellular calcium ion concentration induced by caffeine and rapid cooling in frog skeletal muscle fibres.

Konishi¹,

Kurihara²,

Sakai³

1985

The Journal of Physiology

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SUMMARY1. In a single skeletal muscle fibre treated with concentrations of caffeine below threshold for caffeine contracture, rapid lowering of the temperature of the bathing solution from 18 0C to below 5 TC induced a contracture (rapid cooling contracture).2. Intracellular Ca2+ concentration ([Ca2+]i) was recorded during rapid cooling contracture using aequorin. Low concentrations of caffeine often caused a slight elevation of the light signal in resting muscle without detectable tension.3. During rapid cooling contracture, the change in light signal occurred in three phases. The first phase was a transient change of [Ca2+]i accompanying slight tension.During the second phase, the light signal slowly increased as cooling produced maximum tension development. The third phase was an additional light signal induced after the second phase, even though the tension was saturated. 4. The second and third phases were more sensitive to low concentrations of procaine (02-0)5 mM) than the first phase. Synchronous oscillations of light and tension were often observed during the second phase. The light signal during rapid cooling contracture was only slightly affected by long incubation in Ca-free or Ca-rich solutions.5. These results are interpreted as follows. A low concentration of caffeine elevates cytoplasmic resting Ca2+ level without tension development. The oscillations of light and tension often observed in the second phase might represent a cyclic release of Ca2+ from the sarcoplasmic reticulum (s.r.). The third phase is considered to be due to a massive Ca2+ release by a Ca-induced Ca-release mechanism which might be similar to that in skinned fibres. The second phase is probably essential for generation of rapid cooling contracture tension and the third phase represents an excess Ca2+ for tension development.

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Calcium and magnesium contents and volume of the terminal cisternae in caffeine-treated skeletal muscle.

Cited by 39 publications

References 80 publications

The effects of detergent on the contractility and ultrastructure of frog skeletal muscle.

The effects of detergent on the contractility and ultrastructure of frog skeletal muscle.

Total and sarcoplasmic reticulum calcium contents of skinned fibres from rat skeletal muscle.

Change in intracellular calcium ion concentration induced by caffeine and rapid cooling in frog skeletal muscle fibres.

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