Functional differences in type-I fibres from two slow skeletal muscles of rabbit

Abstract

The present study addressed the question of whether the slow fibres of mammalian skeletal muscle, containing the myosin heavy chain MHCI (type-I fibres), are a functionally homogeneous population. We compared various properties of Ca(2+)-activated, skinned, type-I fibres from the soleus and semitendinosus muscles of a rabbit. Soleus type-I fibres showed significantly faster kinetics of stretch activation, measured as the time-to-peak of the stretch-induced, delayed force increase, t(3), than semitendinosus fibres (1239+/-438 ms, n=136, vs. 1600+/-409 ms, n=208 respectively) (means+/-SD, 22 degrees C). Similarly, the speed of unloaded shortening at 15 degrees C was faster in soleus than in semitendinosus fibres [0.79+/-0.16 fibre lengths (FL) s(-1), n=44, vs. 0.65+/-0.15 FL s(-1), n=35 respectively]. The kinetics of stretch activation were more temperature sensitive in semitendinosus than in soleus fibres. Finally, the generation of steady-state isometric force was more sensitive to Ca(2+) in semitendinosus than in soleus fibres: [pCa(50) (-log [Ca(2+)] for half-maximal activation) at 22 degrees C: 6.29+/-0.15, n=28, vs. 6.19+/-0.10, n=18 respectively]. These results suggest strongly that there is no functional homogeneity within type-I fibres of different muscles. The observed differences might reflect the existence of more than one functionally different slow myosin heavy chain isoforms or other modifications of contractile proteins.