Myosin heavy-chain composition of the human hyoglossus muscle

Dysphagia. 2010 Jun;25(2):81-93. doi: 10.1007/s00455-009-9227-y. Epub 2009 Jun 13.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aged, 80 and over
  • Deglutition
  • Deglutition Disorders
  • Electrophoresis
  • Female
  • Humans
  • Immunoblotting
  • Immunohistochemistry
  • Male
  • Middle Aged
  • Muscle Fibers, Skeletal / physiology
  • Muscle, Skeletal / physiology*
  • Myosin Heavy Chains / physiology*
  • Phenotype
  • Tongue / physiology*

Substances

  • Myosin Heavy Chains