Abstract

The enzymatic and ultrastructural pattern of mitochondrial differentiation was investigated during myogenesis. Succinate cytochrome C reductase (SCR), a mitochondrial enzyme complex, increased in activity in developing chick thigh muscle in vivo and in vitro. SCR increase in vitro occurred subsequent to myoblast fusion and correlated with the period of increasing creatine phosphokinase (CPK) activity. Fusion-arrest and Ca 2+-reversal experiments indicated an apparent coordination between CPK and SCR enzymatic increases and fusion. Analysis of SCR activity in fibroblast cultures suggested that the enzymatic increases observed in differentiating muscle cultures reflected myocyte differentiation, rather than fibroblast contamination or a unique property of the tissue culture environment. Morphological transitions in the myogenic mitochondria were temporally correlated with increased SCR activity. During myogenesis, the mitochondria enlarged in length and volume, exhibited an increase in matrix density, oriented in parallel to the long axis of the myofibrils, and contained increased numbers of parallel cristae. Many mitochondria in fusion-inhibited muscle cultures resembled those found in prefusion myoblasts, although mature mitochondria were observed in some fusion-blocked cells. Quantitative stereological analyses of these mitochondrial changes parallel the biochemical data and suggest that ultrastructural and enzymatic changes in the mitochondria are an integral part of myodifferentiation.

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