Patients with spasticity typically present with an increased muscle tone that is at least partly caused by an exaggerated stretch reflex. However, intrinsic changes in the skeletal muscles, such as altered mechanical properties of the extracellular matrix or the cytoskeleton, have been reported in response to spasticity and could contribute to hypertonia, although the underlying mechanisms are poorly understood. Here we examined the vastus lateralis muscles from spinal cord-injured patients with spasticity (n = 7) for their passive mechanical properties at three different levels of structural organization, in comparison to healthy controls (n = 7). We also assessed spasticity-related alterations in muscle protein expression and muscle ultrastructure. At the whole-muscle level in vivo, we observed increased passive tension (PT) in some spasticity patients particularly at long muscle lengths, unrelated to stretch reflex activation. At the single-fibre level, elevated PT was found in cells expressing fast myosin heavy chain (MyHC) isoforms, especially MyHC-IIx, but not in those expressing slow MyHC. Type IIx fibres were present in higher than normal proportions in spastic muscles, whereas type I fibres were proportionately reduced. At the level of the isolated myofibril, however, there were no differences in PT between patients and controls. The molecular size of the giant protein titin, a main contributor to PT, was unchanged in spasticity, as was the titin : MyHC ratio and the relative desmin content. Electron microscopy revealed extensive ultrastructural changes in spastic muscles, especially expanded connective tissue, but also decreased mitochondrial volume fraction and appearance of intracellular amorphous material. Results strongly suggest that the global passive muscle stiffening in spasticity patients is caused to some degree by elevated PT of the skeletal muscles themselves. We conclude that this increased PT component arises not only from extracellular matrix remodelling, but also from structural and functional adaptations inside the muscle cells, which alter their passive mechanical properties in response to spasticity in a fibre type-dependent manner.

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In an attempt to explore the relationship between force production during voluntary contractions at different speeds of isokinetic movement and the myofibrillar protein isoform expression in humans, an improved isokinetic dynamometer that corrects for gravitation, controls for acceleration and deceleration, and identifies a maximum voluntary activation was used. Muscle torque recordings were compared at the same muscle length (knee angle) and the torque was calculated as the average torque at each angle over a large knee angle range (75 degrees -25 degrees ) to reduce the influence of small torque oscillation on the calculated torque. Muscle torque at fast (240 degrees s(-1)) versus slow (30 degrees s(-1)) speeds of movement, torque normalized to muscle cross-sectional area (specific tension), and absolute torque at fast speeds of movement were measured in 34 young healthy male and female short-, middle-, and long-distance runners. The relationship between the different measures of muscle function and the expression of myosin heavy chain (MyHC) isoforms using enzyme-histochemical and electrophoretic protein separation techniques were investigated. A significant correlation between the 240 degrees s(-1) vs 30 degrees s(-1) torque ratio and the relative area of the type II fibers and type II MyHC isoforms were observed in both the men (r=0.74; P<0.001) and the women (r=0.81; P<0.05). Thus, the present results confirm a significant relationship between in vivo human muscle function and the MyHC isoform expression in the contracting muscle.

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