Functional significance of myosin transitions in single fibers of developing soleus muscle
- 1 May 1988
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Cell Physiology
- Vol. 254 (5) , C605-C613
- https://doi.org/10.1152/ajpcell.1988.254.5.c605
Abstract
The maximal velocity of shortening and myosin heavy chain (MHC) composition of single, chemically skinned fibers from neonatal and adult rat soleus muscles were examined to determine the relationship between these parameters during slow muscle development in the rat. In addition, the MHC composition of bundles of fibers from soleus muscles at the same ages was studied. The MHC compositions were examined using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The results from the bundles of fibers indicate that from 3 days to 5 mo postnatal, the rat soleus contains predominantly MHCs that migrate in the vicinity of the MHC from adult slow muscle. From 14 days to 2 mo postnatal, there are also significant amounts of additional MHCs that comigrate on SDS gels with those characteristic of adult rat fast muscle. All the fibers studied at 3 and 7 days postnatal and at 5 mo and the majority of fibers from 14 days to 2 mo postnatal had relatively low shortening velocities. A few fibers from the latter group had significantly higher velocities. The faster fibers at each age had greater amounts of the MHCs that comigrate with the adult fast-type MHC on SDS gels. Thus the velocity of shortening of single fibers from the rat soleus muscle appears to be related to MHC composition during postnatal development.This publication has 36 references indexed in Scilit:
- Slow myosin in developing rat skeletal muscle.The Journal of cell biology, 1987
- Fibre type composition of single motor units during synapse elimination in neonatal rat soleus muscleNature, 1984
- A sensitive SDS-page method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosinBiochemical and Biophysical Research Communications, 1983
- A note on the elimination of polyneuronal innervation of skeletal muscles in neonatal ratsActa Physiologica Scandinavica, 1983
- Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog.The Journal of general physiology, 1982
- Skeletal muscle fibers of newborn rats are coupled by gap junctionsDevelopmental Biology, 1982
- Three myosin heavy-chain isozymes appear sequentially in rat muscle developmentNature, 1981
- Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cellsJournal of Molecular Biology, 1978
- Myogenic and neurogenic contributions to the development of fast and slow twitch muscles in ratDevelopmental Biology, 1978
- Adaptive transformation of rat soleus motor units during growthJournal of the Neurological Sciences, 1976