Summary
A comparative study was performed on the fibre populations in tibialis anterior muscles of mouse, rat, guinea pig, rabbit, cat and dog using the two different methods of histochemical staining for myofibrillar ATPase after acid (Brooke and Kaiser 1970) or alkaline preincubations (Guth and Samaha 1970). For all species a complete correspondence existed between type I (Brooke and Kaiser 1970) and β fibres (Samaha et al. 1970). Gross correspondence (>85%) existed between IIA and IIB (Brooke and Kaiser 1970) and αβ and α fibres (Samaha et al. 1970) respectively in mouse, guinea pig, rabbit, cat and dog. In the case of mouse and dog, this high degree of correspondence was based on the assumption that mouse tibialis anterior contains no type I and the dog no type IIB fibres. For the rat, a pronounced overlap existed between IIA fibres on the one hand and αβ and α fibres on the other hand as well as between IIB fibres and αβ and α fibres. These observations lead to the conclusion that the two classification schemes are not interchangeable for all species and that the two terminologies should be used only in relation with the methods from which they were derived.
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References
Brooke MH, Kaiser KK (1969) Some comments on the histochemical characterization of muscle adenosine triphosphatase. J Histochem Cytochem 17:431–432
Brooke MH, Kaiser KK (1970) Muscle fiber types: How many and what kind? Arch Neurol 23:369–379
Guth L, Samaha FJ (1969) Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exp Neurol 25:139–152
Guth L, Samaha FJ (1970) Procedure for the histochemical demonstration of actomyosin ATPase. Exp Neurol 28:365–367
Guth L, Yellin H (1971) The dynamic nature at the so-called “Fiber Types” of mammalian skeletal muscle. Exp Neurol 31:277–300
Mabuchi K, Sréter FA (1980) Actomyosin ATPase. II. Fiber typing by histochemical ATPase reaction. Muscle Nerve 3:233–239
Müntener M (1979) Variable pH dependence of the myosin-ATPase in different muscles of the rat. Histochemistry 62:299–304
Nemeth P, Hofer HW, Pette D (1979) Metabolic heterogeneity of muscle fibers classified by myosin ATPase. Histochemistry 63:191–201
Nemeth P, Pette D (1980) The interrelationship of two systems of fiber classification in rat EDL muscle. J Histochem Cytochem 28:193
Nemeth P, Pette D (1981a) The limited correlation of myosin-based and metabolism-based classifications of skeletal muscle fibers. J Histochem Cytochem 29:89–90
Nemeth P, Pette D (1981b) Succinate dehydrogenase activity in fibres classified by myosin ATPase in three hind limb muscles of rat. J Physiol (Lond) 320:73–80
Padykula HA, Herman E (1955) Factors affecting the activity of adenosine triphosphatase and other phosphatases as measured by histochemical techniques. J Histochem Cytochem 3:161–167
Reichmann H, Pette D (1982) A comparative microphotometric study of succinate dehydrogenase activity levels in Type I, IIA and IIB fibres of mammalian and human muscles. Histochemistry 74:27–41
Samaha FJ, Guth L, Albers RW (1970) Phenotypic differences between the actomyosin ATPase of the three fiber types of mammalian skeletal muscle. Exp Neurol 26:120–125
Snow DH, Billeter R, Mascarello F, Carpenè E, Rowlerson A, Jenny E (1982) No classical type IIB fibres in dog skeletal muscle. Histochemistry 75:53–65
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Green, H.J., Reichmann, H. & Pette, D. A comparison of two ATPase based schemes for histochemical muscle fibre typing in various mammals. Histochemistry 76, 21–31 (1982). https://doi.org/10.1007/BF00493282
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DOI: https://doi.org/10.1007/BF00493282