Metabolic heterogeneity of muscle fibres

Mammalian skeletal muscle is an extremely heterogeneous tissue. Its diversity results from a spectrum of fibres which are metabolically suited to a wide range of functional demands. As judged from enzyme activity analyses of single fibres, the metabolic properties of fibres belonging to the same motor unit are similar or identical. It is likely, therefore, that the phenotype expression of muscle fibres is primarily under neural control. Differences in recruitment patterns of various motor units explain the wide range of metabolic properties as evidenced by pronounced variations in enzyme activities and enzyme activity ratios. There exist large overlaps between the activity spectra of various enzymes of anaerobic and aerobic metabolism in slow- and fast-twitch fibres. Nevertheless, these two major fibre classes can be distinguished by discriminative enzyme activity ratios (e.g. phosphofructokinase/malate dehydrogenase, phosphofructokinase/3-hydroxyacyl-CoA dehydrogenase, fructose-1,6-diphosphatase/phosphofructokinase). Moreover, slow-twitch fibres display an H-type isozyme pattern of lactate dehydrogenase, whereas fast-twitch fibres are characterized by a predominance of LDH-5. No clear-cut differences exist between enzyme activity profiles and LDH isozyme patterns of the IIA and IIB subgroups of fast-twitch fibres. Comparative studies indicate that the metabolic properties of IIA and IIB fibres vary in different animal species. This observation supports the notion that metabolic and myosin-related properties of muscle fibres may be regulated independently. Due to relatively high turnover rates of enzymes of energy metabolism in muscle, changes in functional demands may be met by relatively rapid changes in metabolic properties. In view of these findings it is not surprising that muscle fibres display a spectrum of metabolic properties and represent stages within a dynamic equilibrium.