Abstract
The basic mechanism underlying the contraction–relaxation cycle of vertebrate muscles is a Ca2+ exchange between the sarcoplasmic reticulum and the myofibrils. Relaxation is achieved by retrieval of Ca2+ from the myofibrils and transfer to the sarcoplasmic reticulum. However, it is uncertain whether the rate of Ca2+ uptake by the sarcoplasmic reticulum can account for the known speed of relaxation1,2. In fast contracting muscles the Ca2+-binding protein parvalbumin is postulated to facilitate relaxation3–8. Using immunohistochemical techniques, we show here that parvalbumin is located exclusively in type II (fast-twitch) mammalian skeletal muscle fibres which can be further subdivided into five subgroups displaying distinct staining intensities. As the active state decays more rapidly in fast than in slow muscles9,10, our results support the contention that parvalbumin may be concerned with rapid muscle relaxation3–8 and in addition suggest a range of relaxation properties in muscle fibres belonging to the same histochemical fibre type.
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Celio, M., Heizmann, C. Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres. Nature 297, 504–506 (1982). https://doi.org/10.1038/297504a0
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DOI: https://doi.org/10.1038/297504a0
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