Abstract
Long-distance runners generally have a remarkably high proportion of slow type I fibers in their lower muscle groups. However, the transformation of type II fast fibers to slow type I fibers as a result of exercise has not been demonstrated clearly. We report the analysis of muscle type composition on m. vastus lateralis from six endurance athletes through the expression of fast, slow, and developmental myosin isoforms, and α-actinin-3 (ACTN3) protein. Only one among the marathon runners presented evident type I fiber predominance, and surprisingly, a second athlete showed a deficiency of ACTN3. The deficiency of ACTN3 in the muscle tissue of endurance athletes confirmed the redundancy of this protein for muscle function, even in muscles that are highly required.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Andersen J. L., Schjerling P., and Saltin B. (2000) Muscle, genes and athletic performance. Sci. Am. 283, 48–55.
Beggs A. H., Byers T. J., Knoll J. H. M., et al. (1992) Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11. J. Biol. Chem. 267, 9281–9288.
Bottinelli R. and Reggiani C. (2000) Human skeletal muscle fibres: molecular and functional diversity. Prog. Biophys. Mol. Biol. 73, 195–262.
Clarkson P. M., Kroll W., and McBride T. C. (1980) Maximal isometric strength and fiber type composition in power and endurance athletes. Eur. J. Appl. Physiol. 44, 35–42.
Coggan A. R., Spina R. J., Rogers M. A., et al. (1990) Histochemical and enzymatic characteristics of skeletal muscle in master athletes. J. Appl. Physiol. 68, 1896–1901.
Costill D. L., Fink W. J., and Pollock M. L. (1976) Muscle fiber composition and enzyme activities of elite distance runners. Med. Sci. Sports 8, 96–100.
Dubowitz V. (1985) Muscle Biopsy: A Practical Approach, 2nd ed., Bailliere Tindall, London.
Ho-Kim M-A., Bedard A., Vincent M., et al. (1991) Dystrophin: a sensitive and reliable immunochemical assay in tissue and cell culture homogenates. Biochem. Biophys. Res. Commun. 181, 1164–1172.
North K. N. and Beggs A. H. (1996) Deficiency of a skeletal muscle isoform of alpha-actinin (alpha-actinin-3) in merosin-positive congenital muscular dystrophy. Neuromuscul. Disord. 6, 229–235.
North K. N., Yang N., Wattanasirichaigoon D., et al. (1999) A common nonsense mutation results in alphaactinin-3 deficiency in the general population. Nat. Genet. 21, 353–354.
Ricoy J. R., Encinas A. R., Cabello A., et al. (1998) Histochemical study of the vastus lateralis muscle types of athletes. J. Physiol. Biochem. 54, 41–47.
Vainzof M., Costa C. S., Marie S. N., et al. (1997) Deficiency of α-actinin-3 (ACTN3) occurs in different forms of muscular dystrophy. Neuropediatrics 28, 223–228.
Vainzof M., Zubrzycka-Gaarn E. E., Rapaport D., et al. (1991) Immunofluorescence dystrophin study in Duchenne dystrophy through the concomitant use of two antibodies directed against the carboxy-terminal and the aminoterminal region of the protein. J. Neurol. Sci. 101, 141–147.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zanoteli, E., Lotuffo, R.M., Oliveira, A.S.B. et al. Deficiency of muscle α-actinin-3 is compatible with high muscle performance. J Mol Neurosci 20, 39–42 (2003). https://doi.org/10.1385/JMN:20:1:39
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1385/JMN:20:1:39