High resolution radioautographic study of newly formed protein in striated muscle with emphasis on red and white fibres.

The elaboration and distribution of newly formed proteins in the striated muscle of 21-day-old mice were investigated by quantitative radioautography at intervals between 2 and 240 min after intravenous injection of tritiated leucine. In radioautographs, the localization and the relative label concentration were comparatively estimated for the different components of mitochondria-rich fibres, in particular of red fibres, from the tibialis anterior muscle and of mitochondria-poor fibres from the oesophageal muscle. As early as 2 min after injection, radioactivity was detected over the nucleus, the polysome-rich sarcoplasm, the A and I bands, the Z lines, and the mitochondria in the two fibre types. Label localization did not change with time. The relative label concentration increased similarly in the polysome-rich sarcoplasm and the A and I bands of both fibre types within 30 min after injection, a confirmation that biosynthesis of myofibrillar proteins takes place rapidly. In each case, concentration was higher in the Z lines than in the I bands, and higher in the I bands than in the A bands, thus showing "in vivo" that the rates of synthesis of sarcomere protein components are not uniform. However, the relative label concentration was found to be higher in the Z lines of mitochondria-poor fibres than of mitochondria-rich fibres: this suggests that a higher synthetic rate of Z line protein, and probably of alpha actinin, is characteristic of the first type. Inversely, the concentration was higher in the mitochondria of mitochondria-rich fibres. This lead to the belief that high rate of protein synthesis in these organelles may account for the high rate of label incorporation into this type of fibre.