Opposite changes in myosin heavy chain composition of human masseter and biceps brachii muscles during aging.

The myosin heavy chain (MyHC) content in functionally different parts of the human masseter muscle of six elderly and five young adult subjects (mean age 74 and 22 years, respectively) was determined, using gel electrophoresis. The MyHC composition of the old masseter was also studied by enzyme- and immunohistochemical methods and compared with previous data for young adults. For comparison, the biceps brachii muscle of the same subjects was also analysed. The old masseter contained smaller amounts of slow and larger amounts of fast and fetal MyHCs. These differences were region-dependent and were more pronounced in the superficial portion. There was also a larger proportion of "hybrid" fibres, containing two to four MyHC isoforms (42%), compared with the young adult masseter (23%). No such differences were observed between old and young biceps. In contrast to the masseter, the old biceps contained more slow MyHC and less fast MyHC. This investigation demonstrates that the aging process in human skeletal muscle is accompanied by a modification in the muscle phenotype which is both muscle and region specific; a transformation towards a fast and fetal phenotype concomitant with an increased number of fibres with a mixture of different MyHC isoforms in the masseter; and an opposite shift towards a slower phenotype in the biceps brachii. The results might reflect differences between jaw and limb muscles in genetic programs and adaptive responses to changed functional demands following aging.