Mismatch between myosin heavy chain mRNA and protein distribution in human skeletal muscle fibers.

Abstract

The distribution of myosin heavy chain (MHC) isoforms was analyzed at the protein and mRNA levels in human skeletal muscle biopsies from young normal adult subjects. Using ATPase histochemical reactions, antibodies to fast- and slow-type MHCs, and in situ hybridization with probes specific for MHC-beta/slow, MHC-2A, and MHC-2X, we confirmed our previous results showing that most fibers contain either a single mRNA and isoprotein or a mixed 1/2A or 2A/2X phenotype with coexistence of two mRNAs and isoproteins. However, we also found a minor proportion of fibers showing a mismatch in the relative proportion of mRNA and protein, e.g., fibers containing MHC-2A mRNA but not the corresponding protein or fibers containing MHC-2A protein but not the corresponding transcript. These fibers were more frequent in biopsies obtained after a training or detraining period than before the training period. We propose that these fibers represent transitional fibers and that the relative content of each mRNA and isoprotein gives a clue as to the direction of change in MHC gene expression.