Journal
DYSPHAGIA
Volume 25, Issue 2, Pages 81-93Publisher
SPRINGER
DOI: 10.1007/s00455-009-9227-y
Keywords
Tongue; Myosin heavy chain; Muscle; Immunohistochemistry; Deglutition; Deglutition disorders
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Funding
- National Institute on Deafness and Other Communication Disorders [DC005017]
- NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS [R01DC005017, R56DC005017] Funding Source: NIH RePORTER
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The human tongue muscle hyoglossus (HG) is active in oromotor behaviors encompassing a wide range of tongue movement speeds. Here we test the hypothesis that the human HG is composed of uncommon myosin heavy-chain (MHC) isoforms MHCembryonic, MHCneonatal, and MHCslow tonic as has been reported for other head and neck muscles active during kinematically diverse behaviors. Following reaction of human HG with antibodies specific for MHCI, MHCIIA, MHCII, MHCembryonic, MHCextraocular, MHCneonatal, and MHCslow tonic, only antibodies to MHCI, MHCIIA, and MHCII label more than occasional muscle fibers. These antibodies describe five phenotypes with prevalence MHCIIA > MHCI > MHCI-IIX > MHCI-IIA > MHCIIX. In MHC composition, the human HG is thus similar to human appendicular muscles and many human head and neck muscles but different from human masseter and extraocular muscles which contain five or more MHC isoforms.
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