Characterization of C-protein isoforms expressed in developing, denervated, and dystrophic chicken skeletal muscles by two-dimensional gel electrophoresis

C-Proteins in developing, denervated, and dystrophic chicken skeletal muscles were examined by means of two-dimensional (2D) gel electrophoresis in combination with immunoblotting. In this analysis, the electrophoresis system which was devised by Hirabayashi (Anal. Biochem. 117, 443-451, 1981) provided excellent resolution; three C-protein variants, one fast-type (Cf) and two slow-types (CS3 and CS4) with different Mrs and pIs, were distinguished on a 2D gel. In the neonatal breast muscle, both Cf and CS3 were detected, but during postnatal development, CS3 disappeared from this muscle and Cf became only the C-protein isoform in the adult muscle. In posterior latissimus dorsi (PLD) muscle, both Cf and CS3 were similarly detected at the neonatal stage, but CS3 was replaced by CS4 as this muscle developed. When the breast and PLD muscles were denervated or suffered from muscular dystrophy, both CS3 and CS4 were co-expressed in these muscles in addition to Cf. These results definitely show that the C-protein isoform pattern varies during development and degeneration of chicken skeletal muscles, and in addition the dystrophic or denervated muscle differs from the neonatal muscle with regard to C-protein isoform expression. We suggest that chicken skeletal muscle degenerating due to denervation or muscular dystrophy does not simply recapture the nature of the neonatal muscle, but shifts in a somewhat different direction.