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Updated: Jun 22, 2026

MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a
Published on: August 23, 2024
Myosin heavy-chain composition of the human hyoglossus muscle
Alan J Sokoloff1, Megan Daugherty, Haiyan Li
1Department of Physiology, Emory University School of Medicine, 615 Michael Street, Atlanta, GA 30322, USA. Sokoloff@physio.emory.edu
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.
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