Developmental changes in crossbridge properties and myosin isoforms in hamster diaphragm

Am J Respir Crit Care Med. 1997 Sep;156(3 Pt 1):959-67. doi: 10.1164/ajrccm.156.3.9701051.

Abstract

The aim of this study was to determine the effects of maturation on crossbridge properties and myosin isoform composition in hamster diaphragm muscle. Diaphragm strips were obtained at postnatal Days 1 and 8 and in adults (10 to 12 wk). Peak isometric tension and maximum unloaded shortening velocity (Vmax) increased with age (p < 0.001). The single crossbridge force (pi), the total number of crossbridges normalized per cross-sectional area (m x 10(9)/mm2), the turnover rate of myosin ATPase (kcat), and peak mechanical efficiency (Effmax) were calculated from Huxley's equations. The value of m increased significantly from birth to adulthood (p < 0.001), with no changes in pi or Effmax; kcat increased significantly only after the first week postpartum. There was a strong linear relationship between peak isometric tension and m (p < 0.001). Conversely, changes in Vmax were not related to kcat. Myosin electrophoresis showed that neonatal bands and slow myosin isoforms (S) were present at birth. The number of fast adult myosin isoforms increased progressively from birth to adulthood, whereas S increased during the first week postpartum. In conclusion, development changes in diaphragm muscle force and myosin isoform composition were associated with changes in crossbridge number and kinetics, with no changes in the average force per crossbridge or in mechanical efficiency.

MeSH terms

  • Age Factors
  • Animals
  • Animals, Newborn / growth & development*
  • Biomechanical Phenomena
  • Cricetinae
  • Diaphragm / enzymology
  • Diaphragm / growth & development*
  • Electrophoresis
  • Isometric Contraction
  • Linear Models
  • Mesocricetus / growth & development*
  • Muscle Development*
  • Myosins / analysis
  • Myosins / chemistry*

Substances

  • Myosins