Maximum shortening velocity and myosin heavy-chain isoform expression in human masseter muscle fibers.

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  • Additional Information
    • Source:
      Publisher: Sage Country of Publication: United States NLM ID: 0354343 Publication Model: Print Cited Medium: Print ISSN: 0022-0345 (Print) Linking ISSN: 00220345 NLM ISO Abbreviation: J Dent Res Subsets: MEDLINE
    • Publication Information:
      Publication: Thousand Oaks, CA : Sage
      Original Publication: Chicago, American Dental Assn. [etc.]
    • Subject Terms:
      Masseter Muscle/*chemistry ; Muscle Contraction/*physiology ; Myosin Heavy Chains/*physiology ; Myosin Type I/*physiology ; Skeletal Muscle Myosins/*physiology; Adolescent ; Adult ; Electrophoresis, Polyacrylamide Gel ; Female ; Humans ; Least-Squares Analysis ; Male ; Masseter Muscle/metabolism ; Masseter Muscle/physiology ; Middle Aged ; Muscle Fibers, Slow-Twitch/chemistry ; Muscle Fibers, Slow-Twitch/physiology ; Myosin Heavy Chains/analysis ; Myosin Type I/analysis ; Phenotype ; Protein Isoforms/biosynthesis ; Protein Isoforms/physiology ; Skeletal Muscle Myosins/analysis
    • Abstract:
      While human masseter muscle is known to have unusual co-expression of myosin heavy-chain proteins, cellular kinetics of individual fibers has not yet been tested. Here we examine if myosin heavy-chain protein content is closely correlated to fiber-shortening speed, as previously reported in other human muscles, or if these proteins do not correlate well to shortening speeds, as has been demonstrated previously in rat muscle. Slack-test recordings of single, skinned human masseter fibers at 15 degrees C revealed maximum shortening velocities generally slower and much more variable than those recorded in human limb muscle. The slowest fiber recorded had a maximum shortening velocity (V0) value of 0.027 muscle lengths x s(-1), several times slower than the slowest type I fibers previously measured in humans. By contrast, human limb muscle controls produced V0 measurements comparable with previously published results. Analysis by gel electrophoresis found 63% of masseter fibers to contain pure type I MyHC and the remainder to co-express mostly type I in various combinations with IIA and IIX isoforms. V0 in masseter fibers forms a continuum in which no clear relationship to MyHC isoform content is apparent.
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    • Grant Information:
      R01 DC005058 United States DC NIDCD NIH HHS; DE 11709 United States DE NIDCR NIH HHS
    • Accession Number:
      0 (Protein Isoforms)
      EC 3.6.1.- (Myosin Type I)
      EC 3.6.1.- (Skeletal Muscle Myosins)
      EC 3.6.4.1 (Myosin Heavy Chains)
    • Publication Date:
      Date Created: 20020403 Date Completed: 20020417 Latest Revision: 20181113
    • Publication Date:
      20231215
    • Accession Number:
      PMC4141476
    • Accession Number:
      10.1177/00220345010800091401
    • Accession Number:
      11926245