Mammalian skeletal muscle shows an enormous variability in its functional features such as rate of force production, resistance to fatigue, and energy metabolism, with a wide spectrum from slow aerobic to fast anaerobic physiology. In addition, skeletal muscle exhibits high plasticity that is based on the potential of the muscle fibers to undergo changes of their cytoarchitecture and composition of specific muscle protein isoforms. Adaptive changes of the muscle fibers occur in response to a variety of stimuli such as, e.g., growth and differentition factors, hormones, nerve signals, or exercise. Additionally, the muscle fibers are arranged in compartments that often function as largely independent muscular subunits. All muscle fibers use Ca(2+) as their main regulatory and signaling molecule. Therefore, contractile properties of muscle fibers are dependent on the variable expression of proteins involved in Ca(2+) signaling and handling. Molecular diversity of the main proteins in the Ca(2+) signaling apparatus (the calcium cycle) largely determines the contraction and relaxation properties of a muscle fiber. The Ca(2+) signaling apparatus includes 1) the ryanodine receptor that is the sarcoplasmic reticulum Ca(2+) release channel, 2) the troponin protein complex that mediates the Ca(2+) effect to the myofibrillar structures leading to contraction, 3) the Ca(2+) pump responsible for Ca(2+) reuptake into the sarcoplasmic reticulum, and 4) calsequestrin, the Ca(2+) storage protein in the sarcoplasmic reticulum. In addition, a multitude of Ca(2+)-binding proteins is present in muscle tissue including parvalbumin, calmodulin, S100 proteins, annexins, sorcin, myosin light chains, beta-actinin, calcineurin, and calpain. These Ca(2+)-binding proteins may either exert an important role in Ca(2+)-triggered muscle contraction under certain conditions or modulate other muscle activities such as protein metabolism, differentiation, and growth. Recently, several Ca(2+) signaling and handling molecules have been shown to be altered in muscle diseases. Functional alterations of Ca(2+) handling seem to be responsible for the pathophysiological conditions seen in dystrophinopathies, Brody's disease, and malignant hyperthermia. These also underline the importance of the affected molecules for correct muscle performance.

Many studies have documented an association between chronic low back pain (LBP) and deficits in back muscle strength and endurance. The sub-optimal performance is believed to be the result of alterations in the size and structure of the muscle, although the long-standing issue of whether the observed changes precede or are a consequence of the pain remains unresolved. If consequent to the problem, and predominantly related to disuse of the muscles, then it may be expected that a relationship between muscle structure and symptom duration would exist. Lumbar paraspinal muscle samples were obtained from 59 chronic LBP patients using the percutaneous biopsy technique. The samples were subject to routine histochemical analysis for the examination of muscle fibre type characteristics and cytochemical architectural changes. In 55 of the patients, the gross cross-sectional areas of magnetic resonance images of the trunk muscles were also measured. Multivariate analysis showed that symptom duration was the strongest predictor of the individual proportions of the fast-fatigable type IIX fibres; with age and gender included in the model, nearly 30% of the variance in fibre type distribution could be accounted for. Duration of pain had no influence on fibre size. Gross muscle cross-sectional area correlated directly with lean body mass and inversely with age, but showed no relationship with symptom duration. Pathological changes in the internal fibre structure were more frequently encountered in older patients, and were independent of symptom duration. The results suggest that, over the long term, fibre type transformations rather than alterations in fibre size are the predominant changes to be found in the muscles of chronic LBP patients. The direction of change supports the results of many previous studies that have demonstrated corresponding differences in the fatigability of the muscles. There is a strong case for the early implementation of active measures to attempt to offset the development of these changes in back pain patients.