Structural diversity in muscle fibres of chicken breast
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Chicken breast muscle is usually considered to be a relatively homogeneous white muscle and has therefore been widely used for studies of muscle proteins. In a previous study, however, we have found different M-region structures in different fibres from this muscle. Because of this result, we have now carried out a combined histochemical and ultrastructural survey of this muscle. In particular, we have made use of large transverse cryo-sections that include most of the muscle cross-section.
Although the white region is fairly homogeneous in fibre content according to normal histochemical criteria (mAT-Pase), we have found that there is a gradation of fibre structure across the muscle. The bulk of the muscle stains conventionally for Type-II fibres according to mATPase tests (the “white” part) but, in the small “red” part of the muscle, there are also Type-I fibres together with the Type-II fibres. Superimposed on this division into Type-I and Type-II fibres are variations in fibre size, oxidative and glycolytic staining properties, and variations of Z-band width and M-band structure; there is no strict correlation among any of these parameters. The apparently uniform staining across most of the muscle when tested for myofibrillar ATPase may be a misleading indicator of fibre properties.
Key wordsStriated skeletal muscle Fibre types Muscle cells Myofibril Chicken
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- Dubowitz V, Brooke MH (1973) Muscle Biopsy: A modern approach. W.B. Saunders Company Ltd, LondonGoogle Scholar
- Gauthier GF, Lowey S (1977) Polymorphism of myosin among skeletal muscle fiber types. J Cell Biol 74:760–779Google Scholar
- Grove BK, Kurer V, Lehner C, Doetchman TC, Perriard TC, Eppenberger HM (1984) A new 185000-dalton skeletal muscle protein detected by monoclonal antibodies. J Cell Biol 98:518–524Google Scholar
- Guth L (1973) Fact and artifact in the histochemical procedure for myofibrillar ATPase. Exp Neurol 41:440–450Google Scholar
- Henriksson-Larsén K, Lexell J, Sjöström M (1983) Distribution of different fibre types in human skeletal muscles. I. Method for the preparation and analysis of cross-sections of whole tibialis anterior. Histochem J 15:167–178Google Scholar
- Lexell J, Henriksson-Larsén K, Sjöström M (1983) Distribution of different fibre types in human skeletal muscles. 2. A study of cross-sections of whole m. vastus lateralis. Acta Physiol Scand 117:115–122Google Scholar
- Pette D, Vrbova G (1985) Neural control of phenotype expression in mammalian muscle fibres. Muscle Nerve 8:676–689Google Scholar
- Salmons S, Henriksson J (1981) The adaptive response of skeletal muscle to increased use. Muscle Nerve 4:94–105Google Scholar
- Sjöström M, Squire JM (1977) Fine structure of the A-band in cryo-sections. The structure of the A-band of human skeletal muscle fibres from ultrathin cryo-sections negatively stained. J Mol Biol 109:49–68Google Scholar
- Sjöström M, Ängquist KA, Bylund AC, Fridén J, Gustavsson L, Scherstén T (1982a) Morphometric analysis of human muscle fiber types. Muscle Nerve 5:538–553Google Scholar
- Sjöström M, Kidman S, Henriksson-Larsén K, Ängquist KA (1982b) Z and M-band appearance in different histochemically defined types of human skeletal muscle fibers. J Histochem Cytochem 30:1–11Google Scholar
- Squire JM (1981) The structural basis of muscular contraction. Plenum Press, New YorkGoogle Scholar
- Woodhead JL, Lowey S (1983) An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments. J Mol Biol 168:831–846Google Scholar