ArticleJournal of muscle research and cell motility2002
Human single masseter muscle fibers contain unique combinations of myosin and myosin binding protein C isoforms.
Article in Journal of muscle research and cell motility, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- Desmin is not ubiquitously expressed in head and neck muscle fibers.Journal of anatomy · 2026Article
- Developmental, Physiological and Phylogenetic Perspectives on the Expression and Regulation of Myosin Heavy Chains in Craniofacial Muscles.International journal of molecular sciences · 2024Review
- Nonspeech Oral Movements and Oral Motor Disorders: A Narrative Review.American journal of speech-language pathology · 2015Review
- Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.Muscle & nerve · 2014Article
- Myosin heavy chain composition of the human genioglossus muscle.Journal of speech, language, and hearing research : JSLHR · 2012Article
- Human masseter muscle fiber type properties, skeletal malocclusions, and muscle growth factor expression.Journal of oral and maxillofacial surgery : official journal of the American Association of Oral and Maxillofacial Surgeons · 2012Article
- Expression of masticatory-specific isoforms of myosin heavy-chain, myosin-binding protein-C and tropomyosin in muscle fibers and satellite cell cultures of cat masticatory muscle.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
- Myosin heavy-chain composition of the human hyoglossus muscle.Dysphagia · 2010Article
- The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1.The Journal of experimental biology · 2010Article
- Sarcomeric myosin expression in the tongue body of humans, macaques and rats.Cells, tissues, organs · 2010Article
- Altered contractility of skeletal muscle in mice deficient in titin's M-band region.Journal of molecular biology · 2009Article
- Myofibrillar protein and gene expression in acute quadriplegic myopathy.Journal of the neurological sciences · 2009Article
- Immunohistochemical characterization of slow and fast myosin heavy chain composition of muscle fibres in the styloglossus muscle of the human and macaque (Macaca rhesus).Archives of oral biology · 2007Article
- Impact of post-synaptic block of neuromuscular transmission, muscle unloading and mechanical ventilation on skeletal muscle protein and mRNA expression.Pflugers Archiv : European journal of physiology · 2006Article
- Human single masseter muscle fibers contain unique combinations of myosin and myosin binding protein C isoforms.Journal of muscle research and cell motility · 2002Article
- Influence of Botulinumtoxin A on the Expression of Adult MyHC Isoforms in the Masticatory Muscles in Dystrophin-Deficient Mice (Mdx-Mice).BioMed research internationalArticle
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
Abstract
Striated craniofacial and limb muscles differ in their embryological origin, regulatory program during myogenesis, and innervation. In an attempt to explore the effects of these differences on the striated muscle phenotype in humans, the expression of myosin and myosin-associated thick filament proteins were studied at the single fiber level both in the human jaw-closing masseter muscle and in two limb muscles (biceps brachii and quadriceps femoris muscles). In the masseter, unique combinations of myosin heavy chain (MyHC) and myosin binding protein C (MyBP-C) isoforms were observed at the single fiber level. Compared to the limb muscles, the MyHC isoform expression was more complex in the masseter while the opposite was observed for MyBP-C. In limb muscles, a coordinated expression of three MyHC and three MyBP-C isoforms were observed, i.e., single fibers contained one or two MyHC isoforms, and up to three MyBP-C isoforms. Also, the relative content of the different MyBP-C isoforms correlated with the MyHC isoform expression. In the masseter, on the other hand, up to five different MyHC isoforms could be observed in the same fiber, but only one MyBP-C isoform was identified irrespective MyHC isoform expression. This MyBP-C isoform had a migration rate similar to the slow MyBP-C isoform in limb muscle fibers. In conclusion, a unique myofibrillar protein isoform expression was observed in the human masseter muscle fibers, suggesting significant differences in structural and functional properties between muscle fibers from human masseter and limb muscles.
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