Histochemical methods are routinely used to delineate skeletal muscle fiber types. In the present investigation, this qualitative determination of fiber type composition was compared to the electrophoretically determined myosin heavy chain (MHC) content from a large number of human muscle biopsy samples. Biopsies were taken from the vastus lateralis muscle at the beginning and every 2 weeks during 8 weeks of highi-ntensity resistance training from men (n = 13) and woman (n = 8). Muscle was also extracted from nontraining men (n = 7) and women (n = 5) at the same periods. Six muscle fiber types (I, IC, IIAC, IIA, IIAB, and IIB) were determined using basic myofibrillar adenosine triphosphatase histochemistry. Cross-sectional areas were determined for the three major fiber types (I, IIA, and IIB) and used to calculate the percentage area of these types. Electrophoretic techniques were used to separate and quantify the percentage MHC content in these same biopsy samples, and these data were then used to compare with the percentage fiber type area. Correlation analyses suggest a relationship between the histochemically assessed percentage fiber type area and the electrophoretically assessed MHC content in human limb musculature. However, because of possible histochemical misclassification of some fibers (especially in trained muscle) both techniques may be essential in yielding important information about fiber type composition and possible fiber type transformations.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
This is the net price. Taxes to be calculated in checkout.
Adams GR, Hather BM, Baldwin KM, Dudley GA (1993) Skeletal muscle myosin heavy chain composition and resistance training. J Appl Physiol 74:911–915
Andersen P, Henriksson J (1977) Training induced changes in the subgroups of human type 11 skeletal muscle fibers. Acta Physiol Scand 99:123–125
Bär A, Pette D (1988) Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett 235:153–155
Bergström J (1962) Muscle electrolytes in man. Scand J Clin Lab Invest 14 [Suppl 68]: 1–110
Biral D, Betto R, Danieli-Betto D, Salviati G (1988) Myosin heavy chain composition of single fibres from normal human muscle. Biochem J 250:307–308
Brooke MH, Kaiser KK (1970) Three “myosin ATPase” systems: the nature of their pH lability and sulfhydryl dependence. J Histochem Cytochem 18:670–672
Carraro U, Catani C (1983) A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosin. Biochem Biophys Res Commun 116:793–802
Chesley A, MacDougall JD, Tarnopolsky MA, Atkinson SA, Smith K (1992) Changes in human muscle protein synthesis after resistance exercise. J Appl Physiol 73:1383–1388
Evans WJ, Pinney SD, Young VR (1982) Suction applied to a muscle biopsy maximizes sample size. Med Sci Sports 14:101–102
Hather BM, Tesch PA, Buchanan P, Didley GA (1991) Influence of eccentric actions on skeletal muscle adaptations to resistance training. Acta Physiol Scand 143:177–185
Jansson E, Kaijser L (1977) Muscle adaptation to extreme endurance training in man. Acta Physiol Scand 100:315–324
Moritani T, deVries HA (1979) Neural factors versus hypertrophy in the time course of muscle strength gain. Am J Phys Med Rehabil 58:115–130
Perrie WT, Bumford SJ (1984) Correlation of myosin heavy chains with ATPase staining of skeletal- and cardiac-muscle fibres. Biochem Soc Trans 12:825–826
Perrie WT, Bumford SJ (1986) Electrophoretic separation of myosin isoenzymes. Implications for the histochemical demonstration of fibre types in biopsy specimens of human skeletal muscle. J Neurol Sci 73:89–96
Schantz P, Billeter R, Henriksson J, Jansson E (1982) Traininginduced increase in myofibrillar ATPase intermediate fibres in human skeletal muscle. Muscle Nerve 5:628–636
Staron RS (1991) Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers. Histochemistry 96:21–24
Staron RS, Hikida RS (1992) Histochemical, biochemical, and ultrastructural analyses of single human muscle fibers with special reference to the C fiber population. J Histochem Cytochem 40:563–568
Staron RS, Hikida RS, Hagerman FC (1983) Reevaluation of human muscle fast-twitch subtypes: evidence for a continuum. Histochemistry 78:33–39
Staron RS, Malicky ES, Leonardi MJ, Falkel JE, Hageman FC, Dudley GA (1990) Muscle hypertrophy and fast fiber type conversions in heavy resistance-trained women. Eur J Appl Physiol 60:71–79
Staron RS, Leonardi MJ, Karapondo D, Malicky ES, Falkel JE, Hagerman FC, Hikida RS (1991) Strength and skeletal muscle adaptations in heavy resitance-trained women after detraining and retraining. J Appl Physiol 70:631–640
Staron RS, Hikida RS, Murray TF, Nelson MM, Johnson P, Hagerman F (1992) Assessment of skeletal muscle damage in successive biopsies from strength-trained and untrained men and women. Eur J Appl Physiol 65:258–264
About this article
Cite this article
Fry, A.C., Allemeier, C.A. & Staron, R.S. Correlation between percentage fiber type area and myosin heavy chain content in human skeletal muscle. Europ. J. Appl. Physiol. 68, 246–251 (1994). https://doi.org/10.1007/BF00376773
- Fiber types
- Myosin heavy chains
- Resistance training