Summary
In studies of the myosin crossbridge interaction with actin in vertebrate muscles, the muscles of bony fish have the unique advantage for ultrastructural work that the A-band has a simple ‘crystalline’ lattice of myosin filaments. However, the anatomy and physiology of these fish muscles is relatively poorly understood compared with the rabbit, chicken or frog muscles conventionally used for crossbridge studies. Here the fibre types in fish fin muscles have been characterized to allow sensible selection of single fish fibres for ultrastructural studies. The fibre type compositions of the fin muscles of mullet, plaice, sole and turbot were examined by histochemistry and immunohistochemistry using polyclonal antibodies raised against various myosin isoforms: fish slow, fish fast, mammalian fast (type IIA) and chicken tonic myosins. In the mullet, fin muscles were composed of variable proportions of fast and slow fibres. In the three flatfish, the fin muscle showed a zonal arrangement with slow fibres, binding anti-slow myosin antibody, next to the skin (α region). The bulk of the muscle, distal to the skin, was a typical fast muscle both histochemically and in its reaction with antibodies (δ region). Between these two regions there may be one (sole) or two (turbot, plaice) intermediate zones (β and γ regions) comparable to the pink/intermediate layer of myotomal muscle. In the plaice fin muscle, two kinds of slow fibre could be distinguished immunohistochemically.
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Chayen, N.E., Rowlerson, A.M. & Squire, J.M. Fish muscle structure: fibre types in flatfish and mullet fin muscles using histochemistry and antimyosin antibody labelling. J Muscle Res Cell Motil 14, 533–542 (1993). https://doi.org/10.1007/BF00297216
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DOI: https://doi.org/10.1007/BF00297216