Effects of resistance training on myosin function studied by the in vitro motility assay in young and older men

M. Canepari, R. Rossi, M. A. Pellegrino, R. W. Orrell, M. Cobbold, S. Harridge, R. Bottinelli

Research output: Contribution to journalArticle

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Abstract

It is generally believed that the maximum shortening velocity (V o) of a skeletal muscle fiber type does not vary unless a change in myosin heavy chain (MHC) isoform composition occurs. However, recent findings have shown that Vo of a given fiber type can change after training, suggesting the hypothesis that the function of myosin can vary without a change in isoform. The present study addressed the latter hypothesis by studying the function of isolated myosin isoforms by the use of the in vitro motility assay (IVMA) technique. Four young (age 23-29 yr, YO) and four elderly men (age 68-82 yr, EL) underwent a 12-wk progressive resistance training program of the knee extensor muscles and to one pre- and one posttraining biopsy of the vastus lateralis muscle. The significant increase in one-repetition maximum posttraining in both YO and EL indicated that training was effective. After training, MHC isoform composition showed a shift from MHC2X toward MHC2A in YO and no shift in EL. The velocity of sliding (V f) of actin filaments on pure myosin isoforms extracted from single fibers was studied in IVMA. One hundred sixty IVMA samples were prepared from 480 single fibers, and at least 50 filaments were analyzed in each experiment. Whereas no training-induced change was observed in Vf of myosin isoform 1 either in YO or in EL, a significant increase in Vf of myosin isoform 2A after training was observed in both YO (18%) and EL (19%). The results indicate that resistance training can change the velocity of the myosin molecule.

Original languageEnglish
Pages (from-to)2390-2395
Number of pages6
JournalJournal of Applied Physiology
Volume98
Issue number6
DOIs
Publication statusPublished - Jun 2005

Fingerprint

Resistance Training
Myosins
Protein Isoforms
Myosin Heavy Chains
Muscles
Skeletal Muscle Fibers
Quadriceps Muscle
In Vitro Techniques
Actin Cytoskeleton
Knee
Biopsy
Education

Keywords

  • Myosin isoforms
  • Velocity of shortening

ASJC Scopus subject areas

  • Physiology
  • Endocrinology
  • Orthopedics and Sports Medicine
  • Physical Therapy, Sports Therapy and Rehabilitation

Cite this

Effects of resistance training on myosin function studied by the in vitro motility assay in young and older men. / Canepari, M.; Rossi, R.; Pellegrino, M. A.; Orrell, R. W.; Cobbold, M.; Harridge, S.; Bottinelli, R.

In: Journal of Applied Physiology, Vol. 98, No. 6, 06.2005, p. 2390-2395.

Research output: Contribution to journalArticle

Canepari, M. ; Rossi, R. ; Pellegrino, M. A. ; Orrell, R. W. ; Cobbold, M. ; Harridge, S. ; Bottinelli, R. / Effects of resistance training on myosin function studied by the in vitro motility assay in young and older men. In: Journal of Applied Physiology. 2005 ; Vol. 98, No. 6. pp. 2390-2395.
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