Myosin isoforms in neonatal rat extensor digitorum longus, diaphragm, and soleus muscles
- 1 August 1990
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Lung Cellular and Molecular Physiology
- Vol. 259 (2), L116-L122
- https://doi.org/10.1152/ajplung.1990.259.2.l116
Abstract
The postnatal elimination of embryonic and neonatal myosin isoforms in the rat extensor digitorum longus, diaphragm, and soleus muscles was compared using electrophoresis and immunohistochemical techniques. Electrophoresis of native myosin showed that neonatal bands were present in all three muscles on day 4 but were absent from the day 21 extensor digitorum longus muscle that exhibited its adult electrophoretic pattern. Mature electrophoretic banding patterns were present on days 60 and 125 in the diaphragm and soleus muscles, respectively. Immunohistochemical analysis indicated that embryonic myosin heavy chain was present in all day 4 samples but absent by day 21. Quantitative evaluation determined that the rate of elimination of neonatal myosin heavy chain (MHCneo) was faster in the extensor digitorum longus muscle than in the diaphragm, with the soleus muscle having the slowest rate of elimination of this isoform. Embryonic myosin light chain was detected by two-dimensional electrophoresis through day 8 in each of the muscles. These data indicate that postnatal elimination of MHCneo is tissue specific and time dependent but not governed by either activity level or rostral-caudal position.This publication has 18 references indexed in Scilit:
- Histochemical and physiological characteristics of the rat diaphragmJournal of Applied Physiology, 1985
- Muscle fiber type composition of the rat hindlimbJournal of Anatomy, 1984
- Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscleDevelopmental Biology, 1984
- Myosin transitions in developing fast and slow muscles of the rat hindlimbDifferentiation, 1984
- Muscle fiber type differentiation and satellite cell populations in normally grown and neonatally denervated muscles in the ratActa Neuropathologica, 1984
- Development of histochemical and functional properties of baboon respiratory musclesJournal of Applied Physiology, 1983
- Type IIB to IIA fiber transformation in intermittently stimulated rabbit musclesAmerican Journal of Physiology-Cell Physiology, 1982
- Three myosin heavy-chain isozymes appear sequentially in rat muscle developmentNature, 1981
- A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gelsAnalytical Biochemistry, 1980
- Postnatal differentiation and growth of skeletal muscle fibres in normal and undernourished ratsJournal of the Neurological Sciences, 1978