ArticleJournal of muscle research and cell motility1995
New method for the accurate characterization of single human skeletal muscle fibres demonstrates a relation between mATPase and MyHC expression in pure and hybrid fibre types.
Article in Journal of muscle research and cell motility, 1995. 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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Who cites it
24 citing papers in PubMed, 111 citations in OpenAlex.
- Inverse relationship between exercise economy and oxidative capacity in muscle.European journal of applied physiology · 2005Trial
- Metabolically assessed muscle fibre recruitment in brief isometric contractions at different intensities.European journal of applied physiology · 2004Trial
- Myosin heavy chain isoform expression and high energy phosphate content in human muscle fibres at rest and post-exercise.The Journal of physiology · 1996Trial
- Quantitative and simultaneous measurement of oxygen consumption rates in rat brain and skeletal muscle usingMagnetic resonance in medicine · 2021Article
- Muscle fiber size in healthy children and adults in relation to sex and fiber types.Muscle & nerve · 2021Article
- Myosin Heavy Chain Expression Can Vary over the Length of Jaw and Leg Muscles.Cells, tissues, organs · 2016Article
- A continuum of myofibers in adult rabbit extraocular muscle: force, shortening velocity, and patterns of myosin heavy chain colocalization.Journal of applied physiology (Bethesda, Md. : 1985) · 2011Article
- Adaptation of rat jaw muscle fibers in postnatal development with a different food consistency: an immunohistochemical and electromyographic study.Journal of anatomy · 2010Article
- Functional characteristics of the rat jaw muscles: daily muscle activity and fiber type composition.Journal of anatomy · 2009Article
- Regional differences in fiber characteristics in the rat temporalis muscle.Journal of anatomy · 2008Article
- Protein metabolism in slow- and fast-twitch skeletal muscle during turpentine-induced inflammation.International journal of experimental pathology · 2008Article
- Heterogeneity of fiber characteristics in the rat masseter and digastric muscles.Journal of anatomy · 2007Article
- Postnatal transitions in myosin heavy chain isoforms of the rabbit superficial masseter and digastric muscle.Journal of anatomy · 2006Article
- Adaptive changes of Myosin isoforms in response to long-term strength and power training in middle-aged men.Journal of sports science & medicine · 2006Article
- Validation of a simple, rapid, and economical technique for distinguishing type 1 and 2 fibres in fixed and frozen skeletal muscle.Journal of clinical pathology · 2002Article
- Unloaded shortening velocity and myosin heavy chain variations in human laryngeal muscle fibers.The Annals of otology, rhinology, and laryngology · 2002Article
- Abundant expression of myosin heavy-chain IIB RNA in a subset of human masseter muscle fibres.Archives of oral biology · 2001Article
- Immunolabelling, histochemistry and in situ hybridisation in human skeletal muscle fibres to detect myosin heavy chain expression at the protein and mRNA level.Journal of anatomy · 2001Article
- Distribution of fast myosin heavy chain-based muscle fibres in the gluteus medius of untrained horses: mismatch between antigenic and ATPase determinants.Journal of anatomy · 1999Article
- The interplay of central and peripheral factors in limiting maximal O2 consumption in man after prolonged bed rest.The Journal of physiology · 1997Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study we have developed a method which, by combining histochemical, immunohistochemical, electrophoretic and immunoblotting analyses on a single fibre, enables a sensitive characterization of human skeletal muscle fibres dissected from freeze-dried biopsy samples. For histochemical (and immunohistochemical) analysis fibre fragments (500 microns) of individual fibres were mounted in an embedding medium to allow cryostat sections of normalized thickness to be reproducibly obtained. The specificity of the myofibrillar Ca2+ ATPase (mATPase) staining profiles in gelatin-embedded single fibre sections was tested by immunohistochemical reactions with anti-myosin heavy chain (MyHC) monoclonal antibodies specific to human MyHC I, IIA, IIB and IIA + IIB and by gel electrophoresis. The combined methodologies demonstrated the specificity of the mATPase staining patterns which correlated to the expression of distinct MyHC isoforms. In addition the results provide evidence that many fibres co-expressed different MyHC isoforms in variable relative amounts, forming a continuum. Staining intensities for mATPase, converted into optical density values by image analysis revealed that a relationship between mATPase and MyHC expression holds for hybrid fibres even when displaying one MyHC type with overwhelming dominance. The results also revealed that three MyHC isoforms I, IIA and IIB can be co-expressed on a single muscle fibre. In such a case mATPase alone, with the current protocols, does not allow an accurate characterization of the specific MyHC-based fibre type(s). Although some hybrid fibres may have displayed a non-uniform expression of myosins along their lengths, most fibres from the IIA/B group (type) remained very stable with respect to the relative amounts of the MyHCs expressed. Finally, a second slow MyHC isoform was recognized on immunoblots of a mixed muscle sample.
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