ArticleJournal of muscle research and cell motility1996
Spatial and temporal patterns of myosin heavy chain expression in developing rat extraocular muscle.
Article in Journal of muscle research and cell motility, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 103 citations in OpenAlex.
- One-Month-Old Rabbits Exhibit a Longer Postoperative Remodeling in Extraocular Muscles Compared to 3-Month-Old Rabbits.Investigative ophthalmology & visual science · 2025Article
- Developmental, Physiological and Phylogenetic Perspectives on the Expression and Regulation of Myosin Heavy Chains in Craniofacial Muscles.International journal of molecular sciences · 2024Review
- Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024Article
- The ATPase cycle of human muscle myosin II isoforms: Adaptation of a single mechanochemical cycle for different physiological roles.The Journal of biological chemistry · 2019Article
- Motor neuron vulnerability and resistance in amyotrophic lateral sclerosis.Acta neuropathologica · 2017Review
- Absence of morphological and molecular correlates of sarcopenia in the macaque tongue muscle styloglossus.Experimental gerontology · 2016Article
- Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.Muscle & nerve · 2014Article
- The superfast human extraocular myosin is kinetically distinct from the fast skeletal IIa, IIb, and IId isoforms.The Journal of biological chemistry · 2013Article
- Complex tropomyosin and troponin T isoform expression patterns in orbital and global fibers of adult dog and rat extraocular muscles.Journal of muscle research and cell motility · 2013Article
- Differences in gene expression between strabismic and normal human extraocular muscles.Investigative ophthalmology & visual science · 2012Article
- Myosin heavy chain composition of the human genioglossus muscle.Journal of speech, language, and hearing research : JSLHR · 2012Article
- Pitx2 regulates myosin heavy chain isoform expression and multi-innervation in extraocular muscle.The Journal of physiology · 2011Article
- Postnatal changes in the developing rat extraocular muscles.Investigative ophthalmology & visual science · 2011Article
- Myosin heavy chain expression in mouse extraocular muscle: more complex than expected.Investigative ophthalmology & visual science · 2010Article
- Nonmuscle myosin IIB, a sarcomeric component in the extraocular muscles.Experimental cell research · 2010Article
- Myosin heavy-chain composition of the human hyoglossus muscle.Dysphagia · 2010Article
- Functional diversity among a family of human skeletal muscle myosin motors.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Histochemical and immunohistochemical profile of human and rat ocular medial rectus muscles.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2009Article
- An altered phenotype in a conditional knockout of Pitx2 in extraocular muscle.Investigative ophthalmology & visual science · 2009Article
- Characteristics of muscle fibers reconstituted in the regeneration process of masseter muscle in an mdx mouse model of muscular dystrophy.Journal of muscle research and cell motility · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The present study describes transitions in myosin heavy chain expression in the extraocular muscles of rats between the ages of E17 and adult. The unique phenotype of the extraocular muscle is reflected in its fibre type composition, which is comprised by six distinct profiles, each defined by location (orbital versus global layer) and innervation pattern (single versus multiple terminals). During extraocular muscle myogenesis, developmental myosin heavy chains were expressed in both primary and secondary fibres from embryonic day E17 through the first postnatal week. At this time, the downregulation of developmental myosin heavy chain isoforms began in the global layer in a fibre type-specific manner, reaching completion only after the first postnatal month. By contrast, developmental isoforms were retained in the overwhelming majority of orbital layer fibres into adulthood and expressed differentially along the length of these fibres. Fast myosin heavy chain was detected pre- and postnatally in developing secondary fibres and in all of the singly innervated fibre types and one of the multiply innervated fibre types in the adult. As many as four fast isoforms were detected in maturing extraocular muscle, including the extraocular muscle-specific myosin heavy chain. Slow myosin heavy chain was expressed in primary fibres throughout development and in one of the multiply innervated fibre types in the adult. In contrast, the pure fast-twitch retractor bulbi initially expressed slow myosin heavy chain in fibres destined to switch to the fast myosin heavy chain developmental programme. Based upon spatial and temporal patterns of myosin heavy chain isoform transitions, we suggest that epigenetic influences, rather than purely myogenic stage-specific factors, are critical in determining the unique extraocular muscle phenotype.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.