Thyroidal and neural control of myosin transitions during development of rat fast and slow muscles

Gambke, Brigitte; Lyons, Gary E.; Haselgrove, John C.; Kelly, Alan M.; Rubinstein, Neal A.

doi:10.1016/0014-5793(83)80524-9

Cited by 181 publications

(124 citation statements)

References 7 publications

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“…On the other hand, the role of innervation might not be so determinant, since it has been shown that the muscle denervation of a seven-day-old rat does not prevent the synthesis of the adult fast myosins [38]; the appearance of these myosins is however delayed after muscle denervation at birth and innervation is required for the synthesis of the slow myosin [8].…”

Section: Discussionmentioning

confidence: 99%

Specific programs of myosin expression in the postnatal development of rat muscles

d’Albis

Couteaux

Janmot

et al. 1989

European Journal of Biochemistry

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The expression of myosin during postnatal development was studied in a dozen muscles of the rat. All muscles displayed the usual sequential transitions from embryonic to neonatal and to adult isomyosins. However, we observed that these transitions did not take place uniformly. Thus, half-transition times for the appearance of the adult intermediate and fast myosin extended from seven days for diaphragm, the most precocious muscle of all those examined, to 23 days for male rat masseter. Besides the large differences between their half-transition times, we noticed that the transition curves displayed different slopes, covering different periods. Differences between muscles mainly affected the neonatal-to-adult transition rather than the embryonic-to-neonatal transition, since the embryonic-type myosin disappeared from all muscles examined except for one, at about the Same time, by the end of the first week after birth. In addition, the appearance of slow myosin varied for each muscle and did not follow curves parallel to those for intermediate and fast myosins. These results indicate that each muscle of the rat is subjected to a specific program of myosin isoform transitions during postnatal development.

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Section: Discussionmentioning

confidence: 99%

Specific programs of myosin expression in the postnatal development of rat muscles

d’Albis

Couteaux

Janmot

et al. 1989

European Journal of Biochemistry

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“…Neonatal-type myosins have been observed [23] to persist in another peculiar musculature, the extrinsic ocular muscles of rat, which (perhaps not coincidentally) are also as the masseter muscle innervated by cranial nerves. While the postnatal transitions of fast-type myosins have been shown to be under the influence of thyroid hormone secretion but not under the influence of the nerve [22, 231, it appears that the masseter muscle may be also regulated by additional factors.…”

Section: Discussionmentioning

confidence: 99%

Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle

1986

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Adult rat, mouse, and guinea-pig masseter muscles display distinct myosin electrophoretic patterns. The rat muscle contains four main forms which by reference to the myosins of the IIB tensor fasciae latae, of the IIA mylohyoid, and of the red and white portions of the sternomastoid muscles, correspond respectively to the intermediate-type and to the three fast-type isoforms. The mouse masseter muscle contains only three main myosins, the intermediate-type and two fast-type isoforms. The guinea-pig muscle also displays only three bands, whose assignment is, however, less straightforward than in the murine species; their electrophoretic mobilities are not strictly the same as those of their homologous forms in rat and mouse. Comparison with the myosins of the tensor fasciae latae and of the sternomastoid muscles of guinea-pig allows their identification as intermediate and fast-type myosins.In addition to these typical adult-type forms, adult murine masseter muscles are observed to contain between zero and 30% of neonatal-type myosins. The comparison of the developmental transitions of myosins in the rat masseter with those in the skeletal muscles of the same animal indicates a delay in the appearance of the adult as well as in the disappearance of the neonatal-type myosins in the masseter muscle.Both the variability in myosin types with the animal species and the atypical presence of neonatal forms in the murine adults suggest that myosin expression in the masseter muscle is subjected to unusual regulations.A number of available observations tend to imply that fast-twitch muscles undergo similar transitions from neonatal to adult myosin in the first weeks following birth and that the same muscles from various mammals contain the same types of skeletal myosins in the adult state. Although these statements will probably need adjustments when more results are described, they seem to be true on the whole for the trunk and limb muscles. They may, however, not extend to other types of skeletal muscles with different innervation and distinct embryologic origin. These include the muscles of mastication, for instance the masseter muscle, which is of branchiomeric origin and is innervated by cranial nerves [l].Histochemical studies have indeed pointed out the striking differences in the properties of this muscle depending on the species [2]. The masseter of beef, which masticates slowly, has only slow-type I fibers, while the corresponding muscle of rat and mouse, which eat rapidly, presents type I and type IIA fibers. The masseter of guinea-pig displays only type IIA fibers, that of rabbit a mixture of I, IIA and IIB fibers, and those of predators such as cat and dog have type I1 M fibers. This variability from one mammal to another is uncommon and represents an interesting example of muscle adaptation to specific functional requirements.

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“…These data are consistent with a role for N-CAM controlling the innervation potential of myofibres and suggest that N-CAM down-regulation may be a functional signal in the shift from polyneuronal innervation to monosynaptic input. However, there is only a very general association between the timing of withdrawal of polyneuronal innervation and N-CAM levels and other parallels such as a shift from a hypothyroid state at birth to a neonatal euthyroid state [16] can also be made. In addition, the neonatal down-regulation of N-CAM mediated by activity is difficult to reconcile with studies on chick embryos that show a synchronous downregulation of N-CAM in primary and secondary myofibres that are innervated at different times and in human muscle diseases such as myotonic dystrophy, where there are high levels of sarcolemmal N-CAM and no evidence of impairment of neuromuscular transmission (Walsh, unpublished).…”

Section: Discussionmentioning

confidence: 99%

“…The plasticity of gene expression in skeletal muscle is well documented and a variety of physiological and hormonal stimuli have been found to be important controlling mechanisms [12]. To analyse the plasticity of N-CAM expression in skeletal muscle we analysed the effects of thyroid hormones, a model system that has been extensively used to study isoform transitions in myosin heavy chain (MHC) genes [13][14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Thyroid hormones regulate expression of the neural cell adhesion molecule in adult skeletal muscle

1987

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Adult rat skeletal muscle does not express detectable levels of neural cell adhesion molecule (N‐CAM) and membrane activity mediated by nerve appears to repress the N‐CAM gene. N‐CAM expression in skeletal muscle can however be reinduced by hypothyroidism. Thyroidectomised rats re‐express N‐CAM mRNAs of 5.2 and 2.9 kb and Western blot analysis showed protein bands of 125 and 155 kDa. Immunofluorescence analysis also showed high levels of N‐CAM in the sarcolemma. These changes in N‐CAM expression could be reversed by treatment of hypothyroid rats with thyroxine. Thus thyroid hormones as well as neural influences appear to control N‐CAM expression in skeletal muscle.

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Thyroidal and neural control of myosin transitions during development of rat fast and slow muscles

Cited by 181 publications

References 7 publications

Specific programs of myosin expression in the postnatal development of rat muscles

Specific programs of myosin expression in the postnatal development of rat muscles

Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle

Thyroid hormones regulate expression of the neural cell adhesion molecule in adult skeletal muscle

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