ArticleJournal of muscle research and cell motility2002
Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles.
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 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Morphological Evidence for a Unique Neuromuscular Functional Unit of the Human Vocalis Muscle.International journal of molecular sciences · 2024Article
- Developmental, Physiological and Phylogenetic Perspectives on the Expression and Regulation of Myosin Heavy Chains in Craniofacial Muscles.International journal of molecular sciences · 2024Review
- Male and female syringeal muscles exhibit superfast shortening velocities in zebra finches.The Journal of experimental biology · 2024Article
- Morphometric and Immunohistochemical Characteristics of the Adult Human Soft Palate Muscles.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2022Article
- Structure and function of human muscle fibres and muscle proteome in physically active older men.The Journal of physiology · 2017Article
- The effects of treadmill running on aging laryngeal muscle structure.The Laryngoscope · 2016Article
- Mechanical properties of respiratory muscles.Comprehensive Physiology · 2013Review
- Differential effects of targeted tongue exercise and treadmill running on aging tongue muscle structure and contractile properties.Journal of applied physiology (Bethesda, Md. : 1985) · 2013Article
- Tongue muscle plasticity following hypoglossal nerve stimulation in aged rats.Muscle & nerve · 2013Article
- Myosin heavy chain composition of the human genioglossus muscle.Journal of speech, language, and hearing research : JSLHR · 2012Article
- Human skeletal muscle: transition between fast and slow fibre types.Pflugers Archiv : European journal of physiology · 2011Article
- How to make rapid eye movements "rapid": the role of growth factors for muscle contractile properties.Pflugers Archiv : European journal of physiology · 2011Article
- Myosin heavy-chain composition of the human hyoglossus muscle.Dysphagia · 2010Article
- Immunohistochemical analysis of laryngeal muscles in normal horses and horses with subclinical recurrent laryngeal neuropathy.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009Article
- Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.Pflugers Archiv : European journal of physiology · 2008Article
- 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
- Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles: correlations with myosin subunit composition.Journal of muscle research and cell motility · 2007Article
- Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.The Journal of physiology · 2006Article
- Functional properties of skinned rabbit skeletal and cardiac muscle preparations containing alpha-cardiac myosin heavy chain.Pflugers Archiv : European journal of physiology · 2004Article
- Anatomy and fiber type composition of human interarytenoid muscle.The Annals of otology, rhinology, and laryngology · 2004Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study we aimed to determine the functional properties and the myosin heavy chain (MHC) isoform composition of single chemically skinned fibres from the vocal muscle of four adult men (age: 55-67 years). Single fibres, dissected from the bioptic samples, were chemically skinned and isometric tension (P0) and maximal shortening velocity (V0) were measured at pCa 4.6. MHC and myosin light chain (MLC) composition of fibre segments and MHC distribution of the biopsy samples were analysed by SDS-poly-acrylamide gel electrophoresis (SDS-PAGE) and densitometry. Four MHC isoforms (1, 2A, 2X and a fourth isoform, provisionally called L) and five MLC isoforms (MLC1s, MLC1f, MLC3f, MLC2f, MLC2s) were identified. The major findings of this study were: (1) fast MHC isoforms (in particular MHC-2A) and fast fibres were predominant, (2) one-third of the fibres were mixed or hybrid, i.e. expressed more than one MHC isoform, (3) V0 and P0 values were determined by the MHC isoform composition and mixed fibres showed functional properties which were intermediate between pure fibres; MHC-L was associated with V0 values similar to those of MHC-2A, (4) compared with limb muscles, V0 values of laryngeal fibres were similar to those of limb muscle fibres containing the same MHC isoform whereas P0 values were lower for slow and fast 2X fibres and similar for fibres expressing MHC-2A.
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