The Metabolism of Myosin and the Meromyosins from Rabbit Skeletal Muscle

McManus, I. Rosabelle; Mueller, Helmut

doi:10.1016/s0021-9258(18)96364-7

Cited by 28 publications

(5 citation statements)

References 42 publications

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“…The values of the half-lives of myosin heavy chain and total protein (~15 h and ~22 h, respectively) reported here compare favorably with values obtained by Reporter (14) using skeletal muscle tissue culture of embryonic rat leg (18-21 h and 21 h for myosin and total protein, respectively). However, these values are very different from those reported for myosin from adult skeletal muscle growing in vivo: 20 or 30 days for rat (15) and rabbit (16). A value of 150 days has also been reported for rabbit myosin (17).…”

Section: Discussioncontrasting

confidence: 67%

Specificity of Creatine in the Control of Muscle Protein Synthesis

Ingwall

Morales

Davis

et al. 1974

The Journal of Cell Biology

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This study provides additional evidence that creatine, an end product of contraction unique to muscle, is involved in the control of muscle protein synthesis. Creatine is shown to stimulate selectively the rate of synthesis of two major contractile proteins, actin and myosin heavy chain, in cultures of differentiating skeletal muscle. Creatine affects only the rate of synthesis and not the rate of degradation. Several creatine analogs are as effective as creatine in stimulating muscle protein synthesis, creatinine and amino acids such as arginine and glycine are not. Creatine stimulates myosin heavy chain synthesis twofold in cultures of embryonic muscle grown in either normal or dialyzed media.

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Section: Discussioncontrasting

confidence: 67%

Specificity of Creatine in the Control of Muscle Protein Synthesis

Ingwall

Morales

Davis

et al. 1974

The Journal of Cell Biology

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“…According to previous studies, it might be possible that the ∼20% of type-I fibers in which MYH4 was undetectable at 7 days after denervation represent primary fibers. However, because MyHC proteins have a rather long half-life of ∼30 to 50 days, , it would be interesting to determine the kinetic profiles of MyHC expression in individual fibers from a diverse set of skeletal muscles. This would help to unravel the distribution of primary and secondary fibers and possibly reveal how, depending on their localization, the MyHC profiles of these fibers are altered during catabolic conditions.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, we also observed increased levels of the embryonic myosin MYH3 in denervated type-IIa and -IIb fibers (Figure 3D). 42,43 However, because MyHCs have relatively long half-lives of ∼28 days in rabbits and ∼54 days in rats, 44,45 a slight increase in MYH4 expression in the soleus might not be adequate to induce a marked fiber-type transition at this early time point after denervation. 46,47 Collectively, our quantitative proteomic analyses of single fibers reflected the known fiber-type compositions of the soleus and EDL muscle and enabled the comparison of fiber types with the same MyHC expression profile and metabolic activity during muscular atrophy.…”

Section: Distinct Protein Changes During Denervation-induced Atrophy ...mentioning

confidence: 99%

Single Muscle Fiber Proteomics Reveals Distinct Protein Changes in Slow and Fast Fibers during Muscle Atrophy

et al. 2018

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Skeletal muscles are composed of heterogeneous collections of fibers with different metabolic profiles. With varied neuronal innervation and fiber-type compositions, each muscle fulfils specific functions and responds differently to stimuli and perturbations. We assessed individual fibers by mass spectrometry to dissect protein changes after loss of neuronal innervation due to section of the sciatic nerve in mice. This proteomics approach enabled us to quantify ∼600 proteins per individual soleus and EDL (extensor digitorum longus) muscle fiber. Expression of myosin heavy chain (MyHC) in individual fibers enabled clustering of specific fiber types; comparison of fibers from control and denervated muscles with the same MyHC expression revealed restricted regulation of a total of 240 proteins in type-I, -IIa, or -IIb fibers 7 days after denervation. The levels of several mitochondrial and proteasomal proteins were significantly altered, indicating rapid adaption of metabolic processes after denervation. Furthermore, we observed fiber-type-specific regulation of proteins involved in calcium ion binding and transport, such as troponins, parvalbumin, and ATP2A2, indicating marked remodeling of muscle contractility after denervation. This study provides novel insight into how different muscle fiber types remodel their proteomes during muscular atrophy.

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“…Although several studies (Caldwell and Grosjean, 1971 ;lodice et al ., 1966 ;Parrish and Bailey, 1966 ;Suzuki and Fujimaki, 1968) have shown that proteolytic enzymes can be isolated from muscle tissue, repeated and careful tests have shown that none of these preparations will catalyze degradation of the myofibril (Bodwell and Pearson, 1964 ;Fukazawa and Yasui, 1967 ;Martins and Whitaker, 1968) . Since it is known that myofibrillar proteins have a predictable metabolic turnover time (McManus and Mueller, 1966), the mechanism of myofibrillar protein degradation has remained unknown . It is possible that the Ca 2+-activated sarcoplasmic protein factor we describe in this paper initiates myofibril degradation in vivo by removal of the Z line and that Z-line removal leaves the remaining myofibrillar proteins susceptible to hydrolytic action of lysosomal cathepsins found in the muscle cell (Canonico and Bird, 1970) .…”

Section: Discussionmentioning

confidence: 99%

Ca2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL MUSCLE

Busch

Stromer

Goll

et al. 1972

The Journal of Cell Biology

362

141

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Removal of rabbit psoas strips immediately after death and incubation in a saline solution containing 1 mM Ca 2 + and 5 MM Mg2+ for 9 hr at 37°C and pH 7 .1 causes complete Zline removal but has no ultrastructurally detectable effect on other parts of the myofibril . Z lines remain ultrastructurally intact if I mm 1, 2-bis-(2-dicarboxymethylaminoethoxy)-ethane (EGTA) is substituted for 1 mm Ca 2+ and the other conditions remain unchanged . Z lines are broadened and amorphous but are still present after incubation for 9 hr at 37°C if 1 mm ethylenediaminetetraacetate (EDTA) is substituted for 1 mm Ca 2+ and 5 MM Mg2+ in the saline solution . A protein fraction that causes Z-line removal from myofibrils in the presence of Ca2+ at pH 7 .0 can be isolated by extraction of ground muscle with 4 mat EDTA at pH 7 .0-7 .6 followed by isoelectric precipitation and fractionation between 0 and 40% ammonium sulfate saturation . Z-line removal by this protein fraction requires Ca2 + levels higher than 0

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The Metabolism of Myosin and the Meromyosins from Rabbit Skeletal Muscle

Cited by 28 publications

References 42 publications

Specificity of Creatine in the Control of Muscle Protein Synthesis

Specificity of Creatine in the Control of Muscle Protein Synthesis

Single Muscle Fiber Proteomics Reveals Distinct Protein Changes in Slow and Fast Fibers during Muscle Atrophy

Ca2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL MUSCLE

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