ArticleThe Journal of experimental biology2010
The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1.
Article in The Journal of experimental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Research into the physiology of myosins - a personal odyssey.European journal of translational myology · 2025Article
- Developmental, Physiological and Phylogenetic Perspectives on the Expression and Regulation of Myosin Heavy Chains in Craniofacial Muscles.International journal of molecular sciences · 2024Review
- Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Review
- Nucleotide and protein sequences for dog masticatory tropomyosin identify a novel Tpm4 gene product.Journal of muscle research and cell motility · 2015Article
- Developmental myosins: expression patterns and functional significance.Skeletal muscle · 2015Article
- Regional variation in IIM myosin heavy chain expression in the temporalis muscle of female and male baboons (Papio anubis).Archives of oral biology · 2013Article
- Chronic low-frequency stimulation transforms cat masticatory muscle fibers into jaw-slow fibers.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011Article
- Regulation of jaw-specific isoforms of myosin-binding protein-C and tropomyosin in regenerating cat temporalis muscle innervated by limb fast and slow motor nerves.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We recently reported that masticatory myosin heavy chain (MHC-M) is expressed as the exclusive or predominant MHC isoform in masseter and temporalis muscles of several rodent species, contrary to the prevailing dogma that rodents express almost exclusively MHC isoforms that are typically found in fast limb muscles and not masticatory myosin. We also reported that the same rodent species express the embryonic/atrial isoform of myosin light chain 1 (MLC1E/A) in jaw-closing muscles and not a unique masticatory MLC1 isoform that others have reported as being expressed in jaw-closing muscles of carnivores that express MHC-M. The objective of this study was to test the hypothesis that MLC1E/A is consistently expressed in jaw-closing muscles whenever MHC-M is expressed as the predominant or exclusive MHC isoform. Jaw-closing muscles, fast and slow limb muscles, and cardiac atria and ventricles of 19 species (six Carnivora species, one Primates species, one Chiroptera species, five marsupial species, an alligator and five turtle species) were analyzed using protein gel electrophoresis, immunoblotting, mass spectrometry and RNA sequencing. Gel electrophoresis and immunoblotting indicate that MHC-M is the exclusive or predominant MHC isoform in the jaw-closing muscles of each of the studied species. The results from all of the approaches collectively show that MLC1E/A is exclusively or predominantly expressed in jaw-closing muscles of the same species. We conclude that MLC1E/A is the exclusive or predominant MLC1 isoform that is expressed in jaw-closing muscles of vertebrates that express MHC-M, and that a unique masticatory isoform of MLC1 probably does not exist.
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Registered trials
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