Binding of calcium ions to cell membrane isolated from bullfrog skeletal muscle

Koketsu, K.; Kitamura, Ryozo; Tanaka, Ryo

doi:10.1152/ajplegacy.1964.207.2.509

Cited by 53 publications

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“…The results reported here are in agreement with the findings of othe: authors who have studied the interaction of calcium ions, either witt fragments of natural biological membranes [5,20] or with artificial phos pholipid membranes [23][24][25]28]. In both cases, the interaction has beeI shown to be pH dependent.…”

Section: Discussionsupporting

confidence: 92%

“…To explain the effect of calcium on these membranes, it has been suggested that calcium ions are adsorbed on the external edge of the membranes [11]. There are several types of experimental evidence which appear to support this suggestion.For example, it has been shown that isolated fragments of muscle fiber membranes can bind calcium ions and that the binding is pH dependent [5,20]. This behavior is rather similar to that of phospholipid monolayers [23][24][25]28].…”

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confidence: 95%

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Effect of calcium deprivation on frog skeletal muscles at different pH values

Argibay

Caputo

1971

J. Membrain Biol.

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Whole sartorius muscles from the frog were exposed to calcium-free solutions at different pH values. The depolarizations caused by these solutions were measured 1 hr after the solution change. When the pH was 7.2, the mean depolarization was 8 mV. At pH values of 5.1 and 8.5, the mean depolarizations were 1 and 17 mV, respectively. Similar experiments were carried out with solutions in which the main anion was sulfate instead of chloride. In these cases, the depolarization values caused by calcium deprivation at pH values of 7.2, 5.5, and 8.5 were 11, 4, and 20 mV, respectively.

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Section: Discussionsupporting

confidence: 92%

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confidence: 95%

Effect of calcium deprivation on frog skeletal muscles at different pH values

Argibay

Caputo

1971

J. Membrain Biol.

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“…Subsequent experiments were performed on SLF subfractions isolated by discontinuous gradient centrifugation. Table 1 shows the effects of various ions and ouabain, to distinguish the several known muscle ATPases (1)(2)(3)(4)(5)(6)19 4. We next compared the ionic stimulation of ATPase activities of SLF band 1 and a fraction thought to represent sarcoplasmic reticulum (Table 2). The sarcoplasmic vesicular fraction is stimulated by Mg++ alone and to a lesser extent, by Ca++.…”

Section: Resultsmentioning

confidence: 99%

“…For the purposes of this paper, the sarcolemma is defined as a multilayered envelope covering the muscle cell, including, as its inner sheath, the trilaminar plasmalemma (true plasma membrane) external to which is a basement membrane, also composed of several layers. Attempts have been made to isolate "purified" skeletal muscle sarcolemma, with varying degrees of success (1)(2)(3)(4)(5)(6). We have used a modification of a method used to prepare amphibian muscle membrane (3) for our work on a mammalian sarcolemma.…”

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confidence: 99%

In Vitro Analysis of the General Properties and Junctional Receptor Characteristics of Skeletal Muscle Membranes. Isolation, Purification, and Partial Characterization of Sarcolemmal Fragments

Festoff¹,

Engel²

1974

Proc. Natl. Acad. Sci. U.S.A.

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Muscle membranes were partially purified from rat leg muscles. Externally oriented membrane functions were used to monitor and characterize the resulting membrane fractions. Na+K+mstimulated Mg++-adenosinetriphosphatase, acetylcholinesterase, and cholinergic receptor activities are present and enriched in the density-gradient subfractions of crude sarcolemma when compared with the first pellet. The physical separation of the cholinesterase and receptor activities on the gradient subfractions is demonstrated.Receptor activity, determined by specific la6I-labeled alpha-bungarotoxin binding, appears in fractions with densities similar to other plasma membranes (D4 1.1015-1.1520). Acetylcholinesterase, on the other hand, is preferentially distributed in lighter density fractions (D4" 1.0507-1.0780) and parallels the gradient distribution of the ATPase. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a high-molecular-weight glycoprotein sediments with the higher density fractions only.The data suggest a molecular dissection of the layers of the sarcolemma. The receptor is tentatively felt to be an integral component of the junctional plasma membrane. Acetylcholinesterase is felt to be superficially located on the ectolamina of the junctional sarcolemma, and may be woven within the matrix of the intersynaptic basement membrane.Muscle membranes possess properties found in the membranes of all living cells as well as those unique to excitable tissues. Muscle, however, has not been extensively used as a model system for evaluatingnew concepts and methodology of membrane molecular biology. Its relative resistance to cell disruption, extensive connective tissue network, and the multiple layers of the sarcolemma may partially account for this. For the purposes of this paper, the sarcolemma is defined as a multilayered envelope covering the muscle cell, including, as its inner sheath, the trilaminar plasmalemma (true plasma membrane) external to which is a basement membrane, also composed of several layers. Attempts have been made to isolate "purified" skeletal muscle sarcolemma, with varying degrees of success (1-6). We have used a modification of a method used to prepare amphibian muscle membrane (3) for our work on a mammalian sarcolemma.

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“…In recent investigations the Ca + + binding sites of the sarcolemma were characterized [17,22,38]. In the present study we have investigated the effect of ruthenium red on the Ca ++ binding and on ATPase activity of sarcolemma.…”

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confidence: 94%

Interaction of ruthenium red with isolated sarcolemma

Madeira

Antunes-Madeira

1974

J. Membrain Biol.

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Summary. The stain ruthenium red binds very strongly to isolated sarcolemma and the maximal binding is about 125 nmoles/mg protein, decreasing slightly in lipid-extracted membranes. The binding is half maximal when the free stain concentration is about 1.0 ~tM, for both intact and lipid-depleted material. The nucleotide, ATP, reduces markedly the binding and the apparent affinity of the membranes for the stain. Minute concentrations of ruthenium red (10 laM) inhibit by 80 to 90% the Ca+ +-binding by sarcolemma. The inhibition does not depend on the Ca + + concentration and is similar in both intact and lipid-extracted preparations. Ruthenium red inhibits the ATPase activity of sarcolemma. The inhibition is decreased by increasing the ATP concentration in the medium.The primary events of excitation-contraction coupling in muscle occur at the plasma membrane in the sarcolemma [27,28]. Much work has been done to clarify the mechanism which links the electrical activity of the plasma membrane to the contractile machinery inside the cell [15,29,30,35,37], but the detailed events have not yet been elucidated.The sarcoplasmic reticulum is the main muscular structure in skeletal muscle which regulates the intracellular Ca + § concentration [11,12], and therefore, the contractile activity [43,44]. However, in some types of muscle, which are relatively poor in sarcoplasmic reticulum, other structures may work as Ca + § regulators, such as mitochondria [5,16] and, possibly, sarcolemma [1]. A fraction of Ca + + involved in the contraction-relaxation cycle may enter or leave the muscle cell through sarcolemma [24,27,32].Furthermore, we must necessarily consider an energetic efflux of Ca ++ through the sarcolemma to maintain a constant intracellular concentration of Ca + + since the concentration of free Ca + + in the extraceUular medium is much greater than that inside the muscle cell [23,25,32]. Although sarcoplasmic reticulum [6,11,12,44] and possibly mitochondria [5,16,18] may account for most Ca + + sequestration during relaxation of the muscle cell, there is a constant invasion of the cell by an inward net diffusion of

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Binding of calcium ions to cell membrane isolated from bullfrog skeletal muscle

Cited by 53 publications

References 0 publications

Effect of calcium deprivation on frog skeletal muscles at different pH values

Effect of calcium deprivation on frog skeletal muscles at different pH values

In Vitro Analysis of the General Properties and Junctional Receptor Characteristics of Skeletal Muscle Membranes. Isolation, Purification, and Partial Characterization of Sarcolemmal Fragments

Interaction of ruthenium red with isolated sarcolemma

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