Selective loss of a plasma membrane protein associated with contraction of skeletal muscle

Narahara, H. T.; Green, John D.

doi:10.1016/0005-2736(83)90318-8

Cited by 5 publications

(4 citation statements)

References 21 publications

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“…It has been shown in vitro that incubating skeletal muscle with calpain produces changes identical to those reported in vivo following exercise (for references, see Belcastro 1993). Other studies have shown that calpain is capable of degrading proteins in skeletal muscle plasma membranes ( Zaidi & Narahara 1989), and that tetanic contractions in isolated frog sartorius muscle lead to a loss of a plasma membrane protein ( Narahara & Green 1983). It is important that calpain I has been found to be activated at Ca 2+ concentrations as low as 1 μ M ( Belcastro 1993) or 5 μ M ( Dayton et al .…”

Section: Ca2+‐induced Cell Damage As a Vicious Cyclementioning

confidence: 99%

Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage

Gissel

Clausen

2001

Acta Physiologica Scandinavica

102

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Excessive exercise may lead to skeletal muscle cell damage with degradation of cellular components and leakage of intracellular enzymes. Calcium has repeatedly been proposed to be involved in these processes. Studies have shown that the resting level of cytoplasmic Ca2+ increases up to threefold during long-term low-frequency stimulation. We have shown that electrical stimulation produces a marked increase in Ca2+ uptake and Ca2+ content in rat skeletal muscle, both in vivo and in vitro. Continuous stimulation for 240 min at 1 Hz results in an increased release (18-fold) of lactate dehydrogenase (LDH) from extensor digitorum longus (EDL) muscle. This was associated with an increased total Ca2+ content (185%), was augmented at high [Ca2+]o and suppressed at low [Ca2+]o. The release of LDH may reflect partial loss of sarcolemmal integrity as a result of degradation of membrane components by Ca2+-activated enzymes (e.g. calpain or phospholipase A2). After cessation of stimulation the increased release of LDH continues for at least 120 min. This is associated with an up to sevenfold increase in 45Ca uptake. The increased permeability to Ca2+ may further activate calpain and phospholipase A2 and accelerate the loss of membrane integrity. Stimulation-induced uptake of Ca2+ and release of LDH is most pronounced in EDL (mainly composed of fast-twitch fibres at variance with soleus which is mainly composed of slow-twitch fibres). This may account for the observation that prolonged exercise leads to preferential damage to fast-twitch fibres. We hypothesize that excessive exercise may lead to an intracellular accumulation of Ca2+ and increased cytoplasmic Ca2+ causing activation of self-accelerating degradative pathways leading to muscle damage.

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Section: Ca2+‐induced Cell Damage As a Vicious Cyclementioning

confidence: 99%

Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage

Gissel

Clausen

2001

Acta Physiologica Scandinavica

102

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“…Loss of a plasma membrane protein with the electrophoretic characteristics of band c was seen when isolated frog sartorius muscles were induced to contract tetanically, or when the influx of Ca 2+ was enhanced by incubating sartorius muscles in a high-K + Ringer's solution [38]. In resting muscle cells, the concentration of free Ca 2+ has been found to range from 0.1 to 0.3/,M, while in cells that have been induced to contract, transient increases to levels of 5-10/~M have been reported [6,26].…”

Section: Discussionmentioning

confidence: 98%

“…Previous studies [38] showed that induction of tetanic contractions in frog skeletal muscles caused loss of proteins in the plasma membrane, demonstrable by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The most prominent loss occurred in a membrane protein band having a molecular mass of approximately 96 kDa.…”

Section: Introductionmentioning

confidence: 99%

Degradation of skeletal muscle plasma membrane proteins by calpain

Zaidi

Narahara

1989

J. Membrain Biol.

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Observations described here provide the first demonstration that calpain (Ca2+-dependent cysteine protease) can degrade proteins of skeletal muscle plasma membranes. Frog muscle plasma membrane vesicles were incubated with calpain preparations and alterations of protein composition were revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Calpain II (activated by millimolar concentrations of Ca2+) was isolated from frog skeletal muscle, but the activity of calpain I (activated by micromolar concentrations of Ca2+) was lost during attempts at fractionation. Calpain I obtained from skeletal muscle and erythrocytes of rats was tested instead, and exerted effects similar to those of frog muscle calpain on the membrane proteins. All of the calpain preparations caused striking losses of a major membrane protein of molecular mass of approximately 97 kDa, designated band c, and diminution of a thinner band of approximately 200 kDa. There were concomitant increases in 83- and 77-kDa polypeptides. These effects were absolutely dependent on the presence of free Ca2+, and were completely blocked by calpastatin, a specific inhibitor of calpain action. Frog muscle calpain differed only in being relatively more active at 0 degree C than were the calpains from rat tissues. Experimental observations suggest that calpain acts at the cytoplasmic surface of the plasma membrane.

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“…Several factors have been found to be released from resting and activated muscle cells (Boyd & Forrester, 1964, 1968Narahara & Green, 1983), but only the material described by Kumbaraci & Nastuk (1982) activates the same type of muscle upon reapplication. In the present paper, the released material was separated into rive major compounds only one of which in turn activated skeletal muscle.…”

Section: Discussionmentioning

confidence: 99%

Isolation of a Ca2+-releasing factor from caffeine-treated skeletal muscle fibres and its effect on Ca2+ release from sarcoplasmic reticulum

Herrmann‐Frank

Meissner

1989

J Muscle Res Cell Motil

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In the presence of 2 mM caffeine, skeletal muscles of the frog exert small irregular oscillations of single sarcomeres. A factor, released from these oscillating muscles, was partially purified, and its activity was tested on skinned fibres and isolated vesicles of the sarcoplasmic reticulum (SR). Purification was achieved in three steps by gel filtration and reversed phase chromatography, and the active compound of the released material was shown probably to be a small peptide. In skinned fibres, the purified factor evoked repetitive contractions and subthreshold sarcomeric oscillations. In 'heavy' SR vesicles passively loaded with 45Ca2+, the factor induced a small but significant increase in the 45Ca2+ efflux rate. At the single channel level, the open probability of the SR Ca2+ release channel increased when the factor was added to the cytoplasmic side of the channel. The results reveal that the released factor potentiates Ca2+ release from the SR by increasing the open time of the Ca2+ release channel.

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Selective loss of a plasma membrane protein associated with contraction of skeletal muscle

Cited by 5 publications

References 21 publications

Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage

Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage

Degradation of skeletal muscle plasma membrane proteins by calpain

Isolation of a Ca2+-releasing factor from caffeine-treated skeletal muscle fibres and its effect on Ca2+ release from sarcoplasmic reticulum

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Selective loss of a plasma membrane protein associated with contraction of skeletal muscle

Cited by 5 publications

References 21 publications

Excitation‐induced Ca2+ influx and skeletal muscle cell damage

Excitation‐induced Ca2+ influx and skeletal muscle cell damage

Degradation of skeletal muscle plasma membrane proteins by calpain

Isolation of a Ca2+-releasing factor from caffeine-treated skeletal muscle fibres and its effect on Ca2+ release from sarcoplasmic reticulum

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Product

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Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage

Excitation‐induced Ca²⁺ influx and skeletal muscle cell damage