Composition of intermediate filament subunit proteins in embryonic, neonatal and postnatal porcine skeletal muscle.

Abstract

The intermediate (10-nm) filament subunit proteins (desmin and vimentin) in samples obtained from embryonic, neonatal, and postnatal porcine skeletal muscle were examined by two-dimensional electrophoresis (isoelectric focusing/sodium dodecylsulfate polyacrylamide gel electrophoresis). The skeletal muscle samples were taken from pig embryos at 45, 73 and 102 d of gestation; from neonatal pigs and from postnatal pigs at 1, 6 and 30 mo of age. Three fractions (namely, whole homogenized muscle, purified myofibrils and myofibrillar-protein-extracted residues) were prepared from each skeletal muscle sample for analysis. Vimentin was the major (approximately 75% vimentin: 25% desmin) 10-nm filament protein present in skeletal muscle samples obtained from the 45-d-old pig embryos. The relative proportion of vimentin decreased progressively during embryogenesis. At birth, the vimentin comprised approximately 15%, and desmin, 85%, of the 10-nm filament protein. The proportional amount of vimentin continued to decline postnatally, with the 10-nm filament protein of samples from the 30-mo-old animals consisting of less than approximately 5% vimentin and over 95% desmin. These results show a developmental stage-dependent pattern in the expression of vimentin and desmin intermediate filament subunit proteins in mammalian skeletal muscle. In the adult mammal, desmin is the significant 10-nm filament protein present.