ArticleThe Journal of cell biology1988
The expression of slow myosin during mammalian somitogenesis and limb bud differentiation.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 109 citations in OpenAlex.
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Growth of limb muscle is dependent on skeletal-derived Indian hedgehog.Developmental biology · 2011Article
- Protein kinase A represses skeletal myogenesis by targeting myocyte enhancer factor 2D.Molecular and cellular biology · 2008Article
- A 7.1 kbp beta-myosin heavy chain promoter, efficient for green fluorescent protein expression, probably induces lethality when overexpressing a mutated transforming growth factor-beta type II receptor in transgenic mice.Transgenic research · 2005Article
- RNA-protein interactions of the 3' untranslated regions of myosin heavy chain transcripts.Journal of muscle research and cell motility · 2002Article
- Skeletal muscle fibre type specification during embryonic development.Journal of muscle research and cell motility · 2002Review
- Regulation of myosin heavy chain expression during rat skeletal muscle development in vitro.Molecular biology of the cell · 2001Article
- Lack of coordinated changes in metabolic enzymes and myosin heavy chain isoforms in regenerated muscles of trained rats.Journal of muscle research and cell motility · 2000Article
- Both avian and mammalian embryonic myoblasts are intrinsically heterogeneous.Journal of muscle research and cell motility · 1998Article
- Evidence for distinct fast and slow myogenic cell lineages in human foetal skeletal muscle.Journal of muscle research and cell motility · 1998Article
- Notochord induction of zebrafish slow muscle mediated by Sonic hedgehog.Genes & development · 1997Article
- Regenerated rat fast muscle transplanted to the slow muscle bed and innervated by the slow nerve, exhibits an identical myosin heavy chain repertoire to that of the slow muscle.Histochemistry and cell biology · 1996Article
- An immunocytochemical marker for early type I muscle fibers in the developing rat hindlimb.Anatomy and embryology · 1995Article
- Cellular aggregation enhances MyoD-directed skeletal myogenesis in embryonal carcinoma cells.Molecular and cellular biology · 1994Article
- Mammalian myoblasts become fast or slow myocytes within the somitic myotome.Journal of muscle research and cell motility · 1994Article
- Comparison of the foetal development of fibre types in four bovine muscles.Journal of muscle research and cell motility · 1994Article
- Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development.The Journal of cell biology · 1993Article
- Myosin heavy chain composition of single fibres and their origins and distribution in developing fascicles of sheep tibialis cranialis muscles.Journal of muscle research and cell motility · 1992Article
- Neural regulation of differentiation of rat skeletal muscle cell types.Histochemistry · 1992Article
- Expression of MRF4, a myogenic helix-loop-helix protein, produces multiple changes in the myogenic program of BC3H-1 cells.Molecular and cellular biology · 1992Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The developmental pattern of slow myosin expression has been studied in mouse embryos from the somitic stage to the period of secondary fiber formation and in myogenic cells, cultured from the same developmental stages. The results obtained, using a combination of different polyclonal and monoclonal antibodies, indicate that slow myosin is coexpressed in virtually all the cells that express embryonic (fast) myosin in somites and limb buds in vivo as well as in culture. On the contrary fetal or late myoblasts (from 15-d-old embryos) express in culture only embryonic (fast) myosin. At this stage, muscle cells in vivo, as already shown (Crow, M.T., and F.A. Stockdale. 1986. Dev. Biol. 113:238-254; Dhoot, G.K. 1986. Muscle & Nerve. 9:155-164; Draeger, A., A.G. Weeds, and R.B. Fitzsimons. 1987. J. Neurol. Sci. 81:19-43; Miller, J.B., and F.A. Stockdale. 1986. J. Cell Biol. 103:2197-2208), consist of primary myotubes, which express both myosins, and secondary myotubes, which express preferentially embryonic (fast) myosin. Under no circumstance neonatal or adult fast myosins were detected. Western blot analysis confirmed the immunocytochemical data. These results suggest that embryonic myoblasts in mammals are all committed to the mixed embryonic-(fast) slow lineage and, accordingly, all primary fibers express both myosins, whereas fetal myoblasts mostly belong to the embryonic (fast) lineage and likely generate fibers containing only embryonic (fast) myosin. The relationship with current models of avian myogenesis are discussed.
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