Contractile activity is required for the expression of neonatal myosin heavy chain in embryonic chick pectoral muscle cultures.

Cerny, Lisbeth C.; Bandman, Everett

doi:10.1083/jcb.103.6.2153

Cited by 75 publications

(40 citation statements)

References 60 publications

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“…These findings agree with previous in vitro studies showing that administration of TTX to cultured muscle cells causes centralization of nuclei and disorganization of myofibrils (Tassin et al, 1988;Park-Matsumoto et al, 1992). In chick cultures, TTX inhibits the formation of neonatal MHC, so that only embryonic myosin is expressed (Cerny and Bandman, 1986). DiMario and Stockdale (1997) found that TTX prevented expression of slow MHC in their muscle-spinal cord explant cocultures.…”

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confidence: 82%

Regulation of Myosin Heavy Chain Expression during Rat Skeletal Muscle Development In Vitro

Torgan

Daniels

2001

MBoC

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Signals that determine fast-and slow-twitch phenotypes of skeletal muscle fibers are thought to stem from depolarization, with concomitant contraction and activation of calcium-dependent pathways. We examined the roles of contraction and activation of calcineurin (CN) in regulation of slow and fast myosin heavy chain (MHC) protein expression during muscle fiber formation in vitro. Myotubes formed from embryonic day 21 rat myoblasts contracted spontaneously, and ϳ10% expressed slow MHC after 12 d in culture, as seen by immunofluorescent staining. Transfection with a constitutively active form of calcineurin (CN*) increased slow MHC by 2.5-fold as determined by Western blot. This effect was attenuated 35% by treatment with tetrodotoxin and 90% by administration of the selective inhibitor of CN, cyclosporin A. Conversely, cyclosporin A alone increased fast MHC by twofold. Cotransfection with VIVIT, a peptide that selectively inhibits calcineurin-induced activation of the nuclear factor of activated T-cells, blocked the effect of CN* on slow MHC by 70% but had no effect on fast MHC. The results suggest that contractile activity-dependent expression of slow MHC is mediated largely through the CN-nuclear factor of activated T-cells pathway, whereas suppression of fast MHC expression may be independent of nuclear factor of activated T-cells. INTRODUCTIONSkeletal muscle fibers exhibit a range of phenotypes that are characterized by morphological, biochemical, and functional properties. The phenotypes form a continuum ranging from white, glycolytic, fast-twitch fibers to red, oxidative, slowtwitch fibers. The differences are due to variations in gene expression of numerous proteins and their isoforms, including those of metabolic pathways, excitation-contraction coupling, and the contractile apparatus. Hence the phenotype expressed by an individual fiber has important consequences with respect to the energy demands and functional parameters of that fiber.Although the plasticity of muscle phenotype has been characterized in adult models, little is known about the signals involved in the initial determination of fiber type. Development of vertebrate skeletal muscle is biphasic. Primary (or embryonic) fibers form in the limb before innervation. They express both fast and slow myosin heavy chain (MHC) isoforms, a key determinant of fiber type (ButlerBrowne and Whalen, 1984;Condon et al., 1990a). These fibers serve as a scaffold for the formation of the secondary (or fetal) population of fibers, which compose the bulk of muscle.During development and maturation, secondary fibers in the rat hindlimb first express the embryonic MHC isoform, followed by neonatal and then adult fast or slow isoforms (Whalen et al., 1987;Condon et al., 1990a). The signals that govern secondary fiber development and phenotypic expression are just beginning to be elucidated. In vivo work has shown that formation of the secondary fibers in rats requires contractile activity in that it is blocked by administration of tetrodotoxin (TTX) (Harris, 1981)....

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confidence: 82%

Regulation of Myosin Heavy Chain Expression during Rat Skeletal Muscle Development In Vitro

Torgan

Daniels

2001

MBoC

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“…BA-F8 (IgG2b) was raised against human MyHC and reported to react with slow and cardiac MyHC in humans and mice, and BA-D5 (IgG2b) was raised against human MyHC and reported to detect slow MyHCs in rodent, chicken and zebrafish (Blagden et al, 1997;Schiaffino et al, 1989). Antibody EB165 (IgG1), raised against chicken fast MyHC, was a gift from Dr Everett Bandman (Cerny and Bandman, 1986). The muscle marker 12/101 was a gift from Dr Jeremy Brockes.…”

Section: Immunochemistry and Histologymentioning

confidence: 99%

Hedgehog regulation of superficial slow muscle fibres inXenopusand the evolution of tetrapod trunk myogenesis

et al. 2004

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In tetrapod phylogeny, the dramatic modifications of the trunk have received less attention than the more obvious evolution of limbs. In somites,several waves of muscle precursors are induced by signals from nearby tissues. In both amniotes and fish, the earliest myogenesis requires secreted signals from the ventral midline carried by Hedgehog (Hh) proteins. To determine if this similarity represents evolutionary homology, we have examined myogenesis in Xenopus laevis, the major species from which insight into vertebrate mesoderm patterning has been derived. Xenopus embryos form two distinct kinds of muscle cells analogous to the superficial slow and medial fast muscle fibres of zebrafish. As in zebrafish, Hh signalling is required for XMyf5 expression and generation of a first wave of early superficial slow muscle fibres in tail somites. Thus, Hh-dependent adaxial myogenesis is the likely ancestral condition of teleosts, amphibia and amniotes. Our evidence suggests that midline-derived cells migrate to the lateral somite surface and generate superficial slow muscle. This cell re-orientation contributes to the apparent rotation of Xenopussomites. Xenopus myogenesis in the trunk differs from that in the tail. In the trunk, the first wave of superficial slow fibres is missing,suggesting that significant adaptation of the ancestral myogenic programme occurred during tetrapod trunk evolution. Although notochord is required for early medial XMyf5 expression, Hh signalling fails to drive these cells to slow myogenesis. Later, both trunk and tail somites develop a second wave of Hh-independent slow fibres. These fibres probably derive from an outer cell layer expressing the myogenic determination genes XMyf5, XMyoD and Pax3 in a pattern reminiscent of amniote dermomyotome. Thus, Xenopus somites have characteristics in common with both fish and amniotes that shed light on the evolution of somite differentiation. We propose a model for the evolutionary adaptation of myogenesis in the transition from fish to tetrapod trunk.

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“…Although work has elucidated some of the factors regulating MyHC gene expression, including thyroid hormone (Gustafson et al, 1986;Izumo et al, 1986), innervation (Pette, 2001) and activity (Cerny and Bandman, 1986;Kennedy et al, 1986), exactly how these and other mechanisms interact to regulate a complex series of isoform changes is not known. Thyroid hormone is perhaps the best documented agent that regulates individual fast MyHC isoforms both positively and negatively, depending on the cellular context (Izumo et al, 1986;Morkin et al, 1989).…”

Section: Differentiation and Maturation Of Myotomal Fibersmentioning

confidence: 99%

Regulation of myosin expression during myotome formation

et al. 2003

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The first skeletal muscle fibers to form in vertebrate embryos appear in the somitic myotome. PCR analysis and in situ hybridization with isoform-specific probes reveal differences in the temporal appearance and spatial distribution of fast and slow myosin heavy chainmRNA transcripts within myotomal fibers. Embryonic fast myosin heavy chain was the first isoform expressed, followed rapidly by slow myosin heavy chains 1 and 3, with slow myosin heavy chain 2 appearing several hours later. Neonatal fast myosin heavy chain is not expressed in myotomal fibers. Although transcripts of embryonic fast myosin heavy chain were always distributed throughout the length of myotomal fibers, the mRNA for each slow myosin heavy chain isoform was initially restricted to the centrally located myotomal fiber nuclei. As development proceeded, slow myosin heavy chain transcripts spread throughout the length of myotomal fibers in order of their appearance. Explants of segments from embryos containing neural tube, notochord and somites 7-10, when incubated overnight, become innervated by motor neurons from the neural tube and express all four myosin heavy chain genes. Removal of the neural tube and/or notochord from explants prior to incubation or addition of d-tubocurare to intact explants prevented expression of slow myosin chain 2 but expression of genes encoding the other myosin heavy chain isoforms was unaffected. Thus, expression of slow myosin heavy chain 2 is dependent on functional innervation, whereas expression of embryonic fast and slow myosin heavy chain 1 and 3are innervation independent. Implantation of sonic-hedgehog-soaked beads in vivo increased the accumulation of both fast and slow myosin heavy chain transcripts, as well as overall myotome size and individual fiber size, but had no effect on myotomal fiber phenotype. Transcripts encoding embryonic fast myosin heavy chain first appear ventrolaterally in the myotome, whereas slow myosin heavy chain transcripts first appear in fibers positioned midway between the ventrolateral and dorsomedial lips of the myotome. Therefore, models of epaxial myotome formation must account for the positioning of the oldest fibers in the more ventral-lateral region of the myotome and the youngest fibers in the dorsomedial region.

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Contractile activity is required for the expression of neonatal myosin heavy chain in embryonic chick pectoral muscle cultures.

Cited by 75 publications

References 60 publications

Regulation of Myosin Heavy Chain Expression during Rat Skeletal Muscle Development In Vitro

Regulation of Myosin Heavy Chain Expression during Rat Skeletal Muscle Development In Vitro

Hedgehog regulation of superficial slow muscle fibres inXenopusand the evolution of tetrapod trunk myogenesis

Regulation of myosin expression during myotome formation

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