Myosin heavy chain mRNA isoforms in masseter muscle before and after orthognathic surgery

Harzer, Winfried; Worm, Margitta; Gedrange, Tomasz; Schneider, Matthias; Wolf, Peter H.

doi:10.1016/j.tripleo.2007.01.017

Cited by 31 publications

(25 citation statements)

References 20 publications

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“…MHC-M always being expressed wherever MLC1E/A is expressed) is clearly not true. Adult human masseter expresses predominantly the slow isoform of MHC, along with small amounts of developmental (embryonic and neonatal), alpha cardiac, and fast-type (IIA and IID/X) MHC isoforms (Soussi-Yanicostas et al, 1990;Bredman et al, 1991;Pedrosa-Domellöf et al, 1992;Sciote et al, 1994;Stål, 1994;Monemi et al, 1996;Korfage et al, 2000;Yu et al, 2002;Gedrange et al, 2005;Rowlerson et al, 2005;Harzer et al, 2007). Expression patterns of MHC isoforms in mammalian jaw-closing muscles are, in general, more complex than in limb muscles of the same species (reviewed by Hoh, 2002;Sciote et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1

Reiser

Bicer

Patel

et al. 2010

Journal of Experimental Biology

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SUMMARYWe recently reported that masticatory myosin heavy chain (MHC-M) is expressed as the exclusive or predominant MHC isoform in masseter and temporalis muscles of several rodent species, contrary to the prevailing dogma that rodents express almost exclusively MHC isoforms that are typically found in fast limb muscles and not masticatory myosin. We also reported that the same rodent species express the embryonic/atrial isoform of myosin light chain 1 (MLC1E/A) in jaw-closing muscles and not a unique masticatory MLC1 isoform that others have reported as being expressed in jaw-closing muscles of carnivores that express MHC-M. The objective of this study was to test the hypothesis that MLC1E/A is consistently expressed in jaw-closing muscles whenever MHC-M is expressed as the predominant or exclusive MHC isoform. Jaw-closing muscles, fast and slow limb muscles, and cardiac atria and ventricles of 19 species (six Carnivora species, one Primates species, one Chiroptera species, five marsupial species, an alligator and five turtle species) were analyzed using protein gel electrophoresis, immunoblotting, mass spectrometry and RNA sequencing. Gel electrophoresis and immunoblotting indicate that MHC-M is the exclusive or predominant MHC isoform in the jaw-closing muscles of each of the studied species. The results from all of the approaches collectively show that MLC1E/A is exclusively or predominantly expressed in jaw-closing muscles of the same species. We conclude that MLC1E/A is the exclusive or predominant MLC1 isoform that is expressed in jaw-closing muscles of vertebrates that express MHC-M, and that a unique masticatory isoform of MLC1 probably does not exist. Supplementary material available online at

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Section: Discussionmentioning

confidence: 99%

The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1

Reiser

Bicer

Patel

et al. 2010

Journal of Experimental Biology

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“…In a prospective study (Harzer et al, 2007), bilateral biopsies were taken from 30 patients undergoing orthognathic surgery for the correction of either mandibular retrognathia or prognathism. Specific mRNA MyHC analysis was made to quantify the isoforms I, IIa, and IId/x.…”

Section: Discussionmentioning

confidence: 99%

“…The results showed a significant shift in the relative content from type I (46% before, 37% after) to type IIa (29% before, 42% after) but without significant differences between retrognathia and prognathism. This shift correlated with the increase in the number of occlusal contacts, and was considered necessary to stabilise the treatment result and prevent relapse (Gedrange et al, 2006;Harzer et al, 2007). Type I and II MyHC mRNA are the main components of the mRNA content of the muscle.…”

Section: Discussionmentioning

confidence: 99%

Developmental myosin heavy chain mRNA in masseter after orthognathic surgery: A preliminary study

Oukhai

Maricic

Schneider

et al. 2011

Journal of Cranio-Maxillofacial Surgery

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“…In a follow-up study in a similar population of 30 subjects, type I myosin mRNA decreased at 6 months, while type II myosin increased. 47 These changes occurred as the number of occlusal tooth contacts increased. This association indicates that the establishment of normal masticatory function coincides with changes in myosin gene expression.…”

Section: Muscle Growth Regulatorsmentioning

confidence: 99%

Human Masseter Muscle Fiber Type Properties, Skeletal Malocclusions, and Muscle Growth Factor Expression

Sciote

Horton

Rowlerson

et al. 2012

Journal of Oral and Maxillofacial Surgery

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Purpose We identified masseter muscle fiber type property differences in subjects with dentofacial deformities. Patients and Methods Samples of masseter muscle were collected from 139 young adults during mandibular osteotomy procedures to assess mean fiber areas and percent tissue occupancies for the 4 fiber types that comprise the muscle. Subjects were classified into 1 of 6 malocclusion groups based on the presence of a skeletal Class II or III sagittal dimension malocclusion and either a skeletal open, deep, or normal bite vertical dimension malocclusion. In a subpopulation, relative quantities of the muscle growth factors IGF-I and GDF-8 gene expression were quantified by real-time polymerase chain reaction. Results Fiber properties were not different in the sagittal malocclusion groups, but were very different in the vertical malocclusion groups (P ≤ .0004). There were significant mean fiber area differences for type II (P ≤ .0004) and type neonatal—atrial (P = .001) fiber types and for fiber percent occupancy differences for both type I–II hybrid fibers and type II fibers (P ≤ .0004). Growth factor expression differed by gender for IGF-I (P = .02) and GDF-8 (P < .01). The ratio of IGF-I:GDF-8 expression associates with type I and II mean fiber areas. Conclusion Fiber type properties are very closely associated with variations in vertical growth of the face, with statistical significance for overall comparisons at P ≤ .0004. An increase in masseter muscle type II fiber mean fiber areas and percent tissue occupancies is inversely related to increases in vertical facial dimension.

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Myosin heavy chain mRNA isoforms in masseter muscle before and after orthognathic surgery

Cited by 31 publications

References 20 publications

The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1

The myosin light chain 1 isoform associated with masticatory myosin heavy chain in mammals and reptiles is embryonic/atrial MLC1

Developmental myosin heavy chain mRNA in masseter after orthognathic surgery: A preliminary study

Human Masseter Muscle Fiber Type Properties, Skeletal Malocclusions, and Muscle Growth Factor Expression

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