Calcium-dependent regulation of protein synthesis and degradation in muscle

Kameyama, T; Etlinger, Joseph D.

doi:10.1038/279344a0

Cited by 153 publications

(78 citation statements)

References 28 publications

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“…Synthesis of skeletal-muscle proteins increased in the presence of the Ca2+ ionophore A23187 (Kameyama & Etlinger, 1979;Roufa et al, 1981). Synthesis in incubated muscles was unaffected by 2 mM-EGTA (without added Ca2+), and was not increased by the ionophore in the presence of the chelator (Kameyama & Etlinger, 1979).…”

Section: Discussionmentioning

confidence: 93%

“…These relationships are of interest in light of the observation that the Ca2+ antagonist verapamil (10-1OOpM) decreased the incorporation of radioactive proline into collagenase-digestible and non-collagen proteins by foetal-rat calvaria (Dietrich & Duffield, 1979). Synthesis of skeletal-muscle proteins increased in the presence of the Ca2+ ionophore A23187 (Kameyama & Etlinger, 1979;Roufa et al, 1981). Synthesis in incubated muscles was unaffected by 2 mM-EGTA (without added Ca2+), and was not increased by the ionophore in the presence of the chelator (Kameyama & Etlinger, 1979).…”

Section: Discussionmentioning

confidence: 99%

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Reversible inhibition of protein synthesis in lung by halothane

Rannels¹,

Christopherson²,

Watkins³

1983

Biochemical Journal

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Alterations in the synthesis and degradation of proteins were investigated in intact lungs exposed to the volatile anaesthetic halothane. In rat lungs perfused in situ with Krebs-Henseleit bicarbonate buffer containing 4.5% (w/v) bovine serum albumin, 5.6 mM-glucose, plasma concentrations of 19 amino acids and 69OpM-EU-14C]-phenylalanine and equilibrated with O2/N2/CO2 (4:15 :1), protein synthesis, calculated based on the specific radioactivity of aminoacyl-tRNA, was inhibited by halothane. The anaesthetic did not affect degradation of lung proteins. The inhibition of protein synthesis was rapid in onset, dose-dependent, and quickly reversible. It did not appear to be associated with overall energy depletion, with non-specific changes in cellular permeability, or with decreased availability synthesis.Halothane and other anaesthetic agents are well known to affect a number of metabolic pathways, including those of oxidative, glycolytic and protein metabolism. Halothane exposure produced a doserelated inhibition of glutamate oxidation by mitochondria isolated from rat liver, as well as an inhibition of oxygen uptake in several tissues

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Reversible inhibition of protein synthesis in lung by halothane

Rannels¹,

Christopherson²,

Watkins³

1983

Biochemical Journal

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“…Among the factors known to regulate muscle protein turnover are food intake (9), various hormones (10), and muscle work (11). Recently, in in vitro studies, calcium has also been shown to have a direct effect on muscle protein turnover rates (12,13). Vitamin D administration increases plasma calcium levels, improves force generation by muscle, affects the secretion of other hormones, and is associated with increased food intake (5,(14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

Vitamin D Deficiency, hypocalcemia, and increased skeletal muscle degradation in rats.

Wassner¹,

Li²,

Sperduto³

et al. 1983

J. Clin. Invest.

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A B S T R A C T The myopathy associated with vitamin D deficiency was examined in vitamin D-deficient and vitamin D-supplemented rats. When compared with either vitamin D-supplemented ad lib. or pair-fed rats, weight gain and muscle mass were decreased in vitamin D-deficient hypocalcemic animals. With the exception of a modest decrease in muscle creatine phosphate levels, muscle composition was unchanged by vitamin D deficiency. Muscle protein turnover rates were determined in both in vivo and in vitro studies and demonstrated that myofibrillar protein degradation was increased in vitamin D deficiency. Normal growth rates could be maintained be feeding the rats vitamin D-deficient diets containing 1.6% calcium, which maintained plasma calcium within the normal range. In addition to its role in maintaining plasma calcium, vitamin D-supplemented rats had significantly higher levels of the anabolic hormone insulin. Vitamin D supplementation may affect muscle protein turnover by preventing hypocalcemia, as well as directly stimulating insulin secretion, rather than by a direct effect within skeletal muscle.

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“…Additional reports suggest that muscle atrophy caused by other catabolic conditions, including denervation, burn injury, and muscular dystrophy, is also associated with increased tissue concentrations of calcium (2,3,10,17,64,73). These observations are significant because calcium is an important regulator of muscle protein balance and may link systemic catabolic responses to stimulated protein breakdown in skeletal muscle (16,34,50). The mechanisms regulating calcium entry and cellular levels of calcium in muscle-wasting conditions are not known.…”

mentioning

confidence: 99%

Dexamethasone stimulates store-operated calcium entry and protein degradation in cultured L6 myotubes through a phospholipase A₂-dependent mechanism

Itagaki

Menconi

Antoniu

et al. 2010

American Journal of Physiology-Cell Physiology

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Hasselgren PO. Dexamethasone stimulates store-operated calcium entry and protein degradation in cultured L6 myotubes through a phospholipase A 2-dependent mechanism. Am J Physiol Cell Physiol 298: C1127-C1139, 2010. First published January 27, 2010; doi:10.1152/ajpcell.00309.2009.-Muscle wasting in various catabolic conditions is at least in part regulated by glucocorticoids. Increased calcium levels have been reported in atrophying muscle. Mechanisms regulating calcium homeostasis in muscle wasting, in particular the role of glucocorticoids, are poorly understood. Here we tested the hypothesis that glucocorticoids increase intracellular calcium concentrations in skeletal muscle and stimulate storeoperated calcium entry (SOCE) and that these effects of glucocorticoids may at least in part be responsible for glucocorticoid-induced protein degradation. Treatment of cultured myotubes with dexamethasone, a frequently used in vitro model of muscle wasting, resulted in increased intracellular calcium concentrations determined by fura-2 AM fluorescence measurements. When SOCE was measured by using calcium "add-back" to muscle cells after depletion of intracellular calcium stores, results showed that SOCE was increased 15-25% by dexamethasone and that this response to dexamethasone was inhibited by the store-operated calcium channel blocker BTP2. Dexamethasone treatment stimulated the activity of calcium-independent phospholipase A 2 (iPLA2), and dexamethasone-induced increase in SOCE was reduced by the iPLA 2 inhibitor bromoenol lactone (BEL). In additional experiments, treatment of myotubes with the store-operated calcium channel inhibitor gadolinium ion or BEL reduced dexamethasone-induced increase in protein degradation. Taken together, the results suggest that glucocorticoids increase calcium concentrations in myocytes and stimulate iPLA 2-dependent SOCE and that glucocorticoid-induced muscle protein degradation may at least in part be regulated by increased iPLA 2 activity, SOCE, and cellular calcium levels. glucocorticoids; muscle; wasting MUSCLE WASTING, mainly reflecting stimulated degradation of myofibrillar proteins, is commonly seen in patients with sepsis, severe injury, and cancer (24, 52). Loss of muscle mass also occurs in patients with muscular dystrophy (30, 31). In previous studies, we found evidence (4, 15, 79) that sepsis-induced muscle proteolysis was associated with increased uptake and tissue levels of calcium in skeletal muscle. Additional reports suggest that muscle atrophy caused by other catabolic conditions, including denervation, burn injury, and muscular dystrophy, is also associated with increased tissue concentrations of calcium (2,3,10,17,64,73). These observations are significant because calcium is an important regulator of muscle protein balance and may link systemic catabolic responses to stimulated protein breakdown in skeletal muscle (16,34,50). The mechanisms regulating calcium entry and cellular levels of calcium in muscle-wasting conditions are not known.Glucocorticoids are prom...

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Calcium-dependent regulation of protein synthesis and degradation in muscle

Cited by 153 publications

References 28 publications

Reversible inhibition of protein synthesis in lung by halothane

Reversible inhibition of protein synthesis in lung by halothane

Vitamin D Deficiency, hypocalcemia, and increased skeletal muscle degradation in rats.

Dexamethasone stimulates store-operated calcium entry and protein degradation in cultured L6 myotubes through a phospholipase A₂-dependent mechanism

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Calcium-dependent regulation of protein synthesis and degradation in muscle

Cited by 153 publications

References 28 publications

Reversible inhibition of protein synthesis in lung by halothane

Reversible inhibition of protein synthesis in lung by halothane

Vitamin D Deficiency, hypocalcemia, and increased skeletal muscle degradation in rats.

Dexamethasone stimulates store-operated calcium entry and protein degradation in cultured L6 myotubes through a phospholipase A2-dependent mechanism

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Dexamethasone stimulates store-operated calcium entry and protein degradation in cultured L6 myotubes through a phospholipase A₂-dependent mechanism