Oxidative metabolism of cultured human skeletal muscle cells in comparison with biopsy material.

Human muscle cell cultures were examined for capacities to oxidize several substrates, and for activities of some enzymes related to intermediate metabolism. The results indicate that mitochondrial activities attained appreciable degrees of maturity. The specific activity of creatine kinase increased during myoblast fusion. In contrast, parameters of oxidative metabolism (palmitate and pyruvate oxidation, and cytochrome c oxidase and citrate synthase) did not significantly change throughout myogenesis and thereafter. In differentiated cells (myotubes) the oxidation capacities were pyruvate greater than 2-oxoglutarate greater than malate (+ acetylcarnitine) greater than malate (+ pyruvate), as in muscle biopsies. With regard to protein the cultured human muscle cells showed higher activities than the original biopsies (= 100%) with respect to citrate synthase (179%), but lower values for cytochrome c oxidase (50%) and creatine kinase (7%). Palmitate oxidation capacities were the same in both systems. The presence of antimycin and rotenon inhibited to a comparable extent the palmitate oxidation in cultured muscle and biopsies.