ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2010
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.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 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
- Mechanism of post-tetanic depression of slow muscle fibres.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2024Article
- 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
- The ancient sarcomeric myosins found in specialized muscles.Skeletal muscle · 2019Review
- 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
- Myosin binding protein-C slow is a novel substrate for protein kinase A (PKA) and C (PKC) in skeletal muscle.Journal of proteome research · 2011Article
- 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
- Immunohistochemical analysis of the effects of cross-innervation of murine thyroarytenoid and sternohyoid muscles.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
- 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
- Heterogeneity in the muscle satellite cell population.Seminars in cell & developmental biology · 2010Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We test the hypothesis that cat jaw satellite cells belong to a distinct lineage preprogrammed to express masticatory-specific isoforms of myosin heavy-chain (m-MyHC), myosin-binding protein-C (m-MBP-C), and tropomyosin (m-Tm) during myogenesis in vitro. A monoclonal antibody (MAb) against m-MyHC and MAbs raised here against cat m-MBP-C and m-Tm were used to stain cryostat sections of cat masseter muscle and cultured myotubes derived from satellite cells of cat temporalis and limb muscles, using peroxidase immunohistochemistry. MAbs against m-MBP-C bound purified m-MBP-C in Western blots. MAbs against m-Tm failed to react with m-Tm in Western blots, but reacted with native m-Tm in gel electrophoresis-derived ELISA. In cat masseter sections, MAbs against m-MyHC, m-MBP-C, and m-Tm stained all masticatory fibers, but not the jaw-slow fibers. Cat jaw and limb muscle cultures mature significantly more slowly relative to rodent cultures. However, at 3 weeks, all three MAbs extensively stained temporalis myotubes, whereas they apparently stained isolated myotubes weakly in cat limb and rat jaw cultures. We conclude that satellite cells of masticatory fibers are preprogrammed to express these isoforms during myogenesis in vitro. These results consolidate the notion that masticatory and limb muscle allotypes are distinct.
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