Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.

Whalen, Robert G.; Schwartz, Ketty; Bouveret, P.; Sell, Susan M.; Gros, François

doi:10.1073/pnas.76.10.5197

Cited by 169 publications

(79 citation statements)

References 40 publications

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“…This pattern is characterized by high levels of the enzyme lactase (EC 3.2.1.108) in early life followed by the subsequent acceleration of sucrase (EC 3.2.1.48) expression (Henning, 1986). Similarly, in the skeletal musculature of altricial mammals, different myosin isoforms are expressed as development proceeds (Whalen et al 1979). In both cases, development involves the appearance of new enzymes accompanied by a progressive fall in the concentration of proteins characteristic of the immature state.…”

Section: P J Reeds a N D Othersmentioning

confidence: 99%

Postnatal growth of gut and muscle: competitors or collaborators

et al. 1993

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Although growth and functional maturation are essentially continuous from conception to the attainment of sexual maturity, birth and weaning are particularly critical milestones in life. Birth is associated with a change in the route of nutrient delivery to the organism and weaning requires the attainment of full locomotor function as the organism is called upon to actively seek its own food. Weaning is associated also with major changes in the composition of the diet, changes which in their turn demand intestinal adaptation. Given this, the tissues responsible for the assimilation of nutrients and the tissues responsible for mobility must grow and develop rapidly during the immediate postnatal period. Table 1 summarizes information on the growth rates of the body, intestinal tract, liver, and the leg muscles of the infant rat. Although the rat, as an altricial species, represents one extreme of the interspecific spectrum of chemical and functional maturation at birth, the information illustrates two general points. First, that as a reflection of the chemical maturation of the body, the rate of accretion of body protein exceeds that of the body mass as a whole. Second, that gut and muscle grow during the sucking period with rate constants that are significantly greater than that of body protein as a whole. We have included values for the liver to show that organs that have been of major physiological significance to the fetus tend to grow during the suckling period at a slower rate than that of the body protein mass as a whole.

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Section: P J Reeds a N D Othersmentioning

confidence: 99%

Postnatal growth of gut and muscle: competitors or collaborators

et al. 1993

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“…Both are specific isoforms of proteins that are transiently expressed during normal muscle development and regeneration (23,24). Their up-regulation in VE deficiency may reflect regenerative processes in the muscle, as myofibre regeneration recapitulates much of the developmental program.…”

Section: Muscle Structurementioning

confidence: 99%

Differential gene expression in skeletal muscle of rats with Vitamin E deficiency

Nier

Weinberg

Rimbach

et al. 2006

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryVitamin E (VE) deficiency is accompanied by myopathy in various animal species including man. Although gene expression profiles related to degenerative and regenerative processes in different kinds of myopathies have been studied, no global expression profile for skeletal muscle subject to VE deficiency has previously been reported. In the present study, Affymetrix GeneChip 1 technology was used to obtain such a profile. Two groups of male rats were fed with either a diet deficient in VE or a control diet. Differential gene expression was monitored at five timepoints over 430 days, with all animals individually profiled. Out of *7000 genes represented on the Genechip, 56 were found to be upregulated in response to VE deficiency in at least four consecutive time-points from as early as 91 days of deficiency. Up-regulated genes included muscle structure and extra cellular matrix genes, as well as anti-oxidative, anti-inflammatory and anti-fibrotic genes. Our data show that molecular transcription might provide a very early marker to detect oncoming degenerative conditions in VE deficiency. They provide further insight into possible molecular mechanisms underlying VE deficiency in skeletal muscle, and reveal the activation of an intensive protection program that can explain the long maintenance of muscle structure during deficiency.

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“…Under normal conditions avian and rat embryo muscle cultures synthesize an embryo-specific MHC (32,33) and predominantly myosin light chains characteristic of fast muscle, fast light-chains 1 and 2 (FLC L , FLC2) (34). We therefore measured the myosin isozymes present in normal and in high K' cultures.…”

Section: Growth In High Potassium Does Not Alter Myosin Isozyme Patternsmentioning

confidence: 99%

Increased K+ inhibits spontaneous contractions reduces myosin accumulation in cultured chick myotubes.

Bandman¹,

Strohman²

1982

The Journal of Cell Biology

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Increasing the K+ from 5.4 mM to 12 mM in the culture medium of developing chick myotubes causes an immediate cessation of spontaneous contractions and leads to an inhibition of myosin accumulation. The synthesis of myosin continues at the same rate in 12 mM K+ as in 5.4 mM K+ as measured by [3H]leucine incorporation into myosin corrected for differences in pool specific activity. Total protein synthesis and total protein accumulation are unaffected by growth in 12 mM K+. In addition, growth in 12 mM K+ did not alter the type of myosin heavy-chain isoform expression nor did it alter the pattern of myosin light-chain synthesis. However, the rate of myosin turnover increased threefold in cultures grown in 12 mM K+ compared to cultures grown in 5.4 mM K+, while total protein turnover was only marginally increased. We conclude that suppressed electrical or contractile activity of myotubes leads to an increased rate of myofibrillar protein turnover and that spontaneous mechanical and or electrical activity is required for continued myotube maturation in culture.

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Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.

Cited by 169 publications

References 40 publications

Postnatal growth of gut and muscle: competitors or collaborators

Postnatal growth of gut and muscle: competitors or collaborators

Differential gene expression in skeletal muscle of rats with Vitamin E deficiency

Increased K+ inhibits spontaneous contractions reduces myosin accumulation in cultured chick myotubes.

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