Free-energy carriers in human cultured muscle cells.

Creatine phosphate (CrP), adenosine triphosphate (ATP), creatine kinase (CK), adenylate kinase (AK), protein, and DNA were quantified in human muscle cell cultures undergoing transition from dividing myoblasts to multinucleate myotubes. CrP is negligible in cultures grown in commonly applied media but increases rapidly when sufficient exogeneous creatine is available. The rise in CrP content precedes the rapid increase of CK and cessation of DNA synthesis found during cell fusion. The addition of creatine has no significant effect on the CK and protein content and on the fusion of the human muscle cells. ATP, AK, and protein increase gradually during proliferation and differentiation. When expressed per milligram of protein, ATP and AK are in the same range as in human skeletal muscle and are not correlated to the cell fusion. In contrast, CrP and CK per milligram protein are much higher in myotubes than in myoblasts but remain much lower than in muscle. These data indicate that only an early differentiation phase has been reached in the muscle cell cultures.

Uptake of triiodothyronine into cultured human muscle cells.

The uptake of T3 was measured in cultured human muscle cells at 37 degrees C and pH 7.4 in a medium containing albumin and glucose. The initial up]take increased linearly when the total T3 concentration was varied from 10(-9) to 10(-4) M. At prolonged incubation time the uptake decreased to virtually zero in about 30 min. These data indicate a rapid passive transport mechanism of T3 and a fast equilibration of the cellular T3 with the surrounding medium. In agreement with these conclusions the efflux of T3 was rapid and the initial uptake was not altered by pre-incubation in a T3-containing medium.