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Maximum Shortening Velocity and Myosin Heavy-chain Isoform Expression in Human Masseter Muscle Fibers

Morris, T.J. ; Branden, C.A. ; Horton, M.J. ; Carlson, D.S. ; Sciote, J.J.

Journal of dental research, 2001-09, Vol.80 (9), p.1845-1848 [Periódico revisado por pares]

Los Angeles, CA: SAGE Publications

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Título:
Maximum Shortening Velocity and Myosin Heavy-chain Isoform Expression in Human Masseter Muscle Fibers
Autor: Morris, T.J. ; Branden, C.A. ; Horton, M.J. ; Carlson, D.S. ; Sciote, J.J.
Assuntos: Adolescent ; Adult ; Dentistry ; Electrophoresis, Polyacrylamide Gel ; Female ; Humans ; Least-Squares Analysis ; Male ; Masseter Muscle - chemistry ; Masseter Muscle - metabolism ; Masseter Muscle - physiology ; Middle Aged ; Muscle Contraction - physiology ; Muscle Fibers, Slow-Twitch - chemistry ; Muscle Fibers, Slow-Twitch - physiology ; Myosin Heavy Chains - analysis ; Myosin Heavy Chains - physiology ; Myosin Type I - analysis ; Myosin Type I - physiology ; Phenotype ; Protein Isoforms - biosynthesis ; Protein Isoforms - physiology ; Skeletal Muscle Myosins - analysis ; Skeletal Muscle Myosins - physiology
É parte de: Journal of dental research, 2001-09, Vol.80 (9), p.1845-1848
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: 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°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 ·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. Vo in masseter fibers forms a continuum in which no clear relationship to MyHC isoform content is apparent.
Editor: Los Angeles, CA: SAGE Publications
Idioma: Inglês

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Maximum Shortening Velocity and Myosin Heavy-chain Isoform Expression in Human Masseter Muscle Fibers

Morris, T.J. ; Branden, C.A. ; Horton, M.J. ; Carlson, D.S. ; Sciote, J.J.

Los Angeles, CA: SAGE Publications

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