Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles

Giuseppe D'Antona, Aram Megighian, Susan Bortolotto, Maria Antonietta Pellegrino, Rosario Marchese-Ragona, Alberto Staffieri, Roberto Bottinelli, Carlo Reggiani

Research output: Contribution to journalArticle

Abstract

In the present study we aimed to determine the functional properties and the myosin heavy chain (MHC) isoform composition of single chemically skinned fibres from the vocal muscle of four adult men (age: 55-67 years). Single fibres, dissected from the bioptic samples, were chemically skinned and isometric tension (P0) and maximal shortening velocity (V0) were measured at pCa 4.6. MHC and myosin light chain (MLC) composition of fibre segments and MHC distribution of the biopsy samples were analysed by SDS-poly-acrylamide gel electrophoresis (SDS - PAGE) and densitometry. Four MHC isoforms (1,2A, 2X and a fourth isoform, provisionally called L) and five MLC isoforms (MLC1s, MLC1f, MLC3f, MLC2f, MLC2s) were identified. The major findings of this study were: (1) fast MHC isoforms (in particular MHC-2A) and fast fibres were predominant, (2) one-third of the fibres were mixed or hybrid, i.e. expressed more than one MHC isoform, (3) V0 and P0 values were determined by the MHC isoform composition and mixed fibres showed functional properties which were intermediate between pure fibres; MHC-L was associated with V0 values similar to those of MHC-2A, (4) compared with limb muscles, V0 values of laryngeal fibres were similar to those of limb muscle fibres containing the same MHC isoform whereas P0 values were lower for slow and fast 2X fibres and similar for fibres expressing MHC-2A.

Original languageEnglish
Pages (from-to)187-195
Number of pages9
JournalJournal of Muscle Research and Cell Motility
Volume23
Issue number3
DOIs
Publication statusPublished - 2002

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Laryngeal Muscles
Myosin Heavy Chains
Muscle
Protein Isoforms
Fibers
Chemical analysis
Myosin Light Chains
Extremities
Muscles
Acrylamide
Densitometry
Biopsy
Polyacrylates
Electrophoresis

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Endocrinology
  • Cell Biology

Cite this

D'Antona, G., Megighian, A., Bortolotto, S., Pellegrino, M. A., Marchese-Ragona, R., Staffieri, A., ... Reggiani, C. (2002). Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles. Journal of Muscle Research and Cell Motility, 23(3), 187-195. https://doi.org/10.1023/A:1020963021105

Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles. / D'Antona, Giuseppe; Megighian, Aram; Bortolotto, Susan; Pellegrino, Maria Antonietta; Marchese-Ragona, Rosario; Staffieri, Alberto; Bottinelli, Roberto; Reggiani, Carlo.

In: Journal of Muscle Research and Cell Motility, Vol. 23, No. 3, 2002, p. 187-195.

Research output: Contribution to journalArticle

D'Antona, G, Megighian, A, Bortolotto, S, Pellegrino, MA, Marchese-Ragona, R, Staffieri, A, Bottinelli, R & Reggiani, C 2002, 'Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles', Journal of Muscle Research and Cell Motility, vol. 23, no. 3, pp. 187-195. https://doi.org/10.1023/A:1020963021105
D'Antona, Giuseppe ; Megighian, Aram ; Bortolotto, Susan ; Pellegrino, Maria Antonietta ; Marchese-Ragona, Rosario ; Staffieri, Alberto ; Bottinelli, Roberto ; Reggiani, Carlo. / Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles. In: Journal of Muscle Research and Cell Motility. 2002 ; Vol. 23, No. 3. pp. 187-195.
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