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Iowa State University, Ames 50011
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.
1 Journal paper no. J. 12298 of the Iowa Agr. and Home Econ. Exp. Sta., Ames, Projects 2361 and 2127. This research was supported in part by grants from the Amer. Heart Assoc., Iowa Affiliate, the Muscular Dystrophy Assoc., and the Natl. Instit. of Health (HL-15679).
2 We gratefully acknowledge the advice and help of Drs. Marvin H. Stromer, Ted W. Huiatt and Michael K. Hartzer.
3 Muscle Biol. Group, Depts. of Anim. Sci., Biochem. and Biophys., and Food Technol., cooperating.
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