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The mode of myofibril remodelling in human skeletal muscle affected by DOMS induced by eccentric contractions

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Abstract

Myofibrillar Z-disc streaming and loss of the desmin cytoskeleton are considered the morphological hallmarks of eccentric contraction-induced injury. The latter is contradicted by recent studies where a focal increase of desmin was observed in biopsies taken from human muscles with DOMS. In order to determine the effects of eccentric contraction-induced alterations of the myofibrillar Z-disc, we examined the distribution of α-actinin, the Z-disc portion of titin and the nebulin NB2 region in relation to actin and desmin in DOMS biopsies. In biopsies taken 2–3 days and 7–8 days after exercise, we observed a significantly higher number of fibres showing focal areas lacking staining for α-actinin, titin and nebulin than in biopsies taken from control or 1 h after exercise. None of these proteins were part of Z-disc streamings but instead they were found in distinct patterns in areas characterised by altered staining for desmin and actin. These were preferentially seen in regions with increased numbers of sarcomeres in parallel myofibrils. We propose that these staining patterns represent different stages of sarcomere formation. These findings therefore support our previous suggestion that muscle fibres subjected to eccentric contractions adapt to unaccustomed activity by the addition of new sarcomeres.

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Acknowledgements

We thank Mrs. M. Enerstedt for excellent technical assistance, and G.S. Butler-Browne, M. Gautel and F. Pedrosa-Domellof for valuable comments. This work was supported by grants from the Swedish National Centre for Research in Sports (90/98, 79/99), the Swedish Research Council (12X-03934) and the Medical Faculty of Umeå University.

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Correspondence to Lars-Eric Thornell.

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Yu, JG., Fürst, D.O. & Thornell, LE. The mode of myofibril remodelling in human skeletal muscle affected by DOMS induced by eccentric contractions. Histochem Cell Biol 119, 383–393 (2003). https://doi.org/10.1007/s00418-003-0522-7

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