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Med Sci Sports Exerc. 2010 Jan;42(1):86-95. doi: 10.1249/MSS.0b013e3181ac7afa.

Changes in calpain activity, muscle structure, and function after eccentric exercise.

Author information

1
Norwegian School of Sport Sciences, Oslo, Norway. truls.raastad@nih.no

Abstract

PURPOSE:

The aim of this study was to investigate changes in muscle function, muscle structure, and calpain activity after high-force eccentric exercise.

METHODS:

Eleven healthy males performed 300 maximal voluntary eccentric actions with knee extensors in one leg. Maximal force-generating capacity was measured before exercise and regularly during the next 7 d. Biopsies from musculus vastus lateralis were taken in both control and exercised legs 0.5, 4, 8, 24, 96, and 168 h after exercise for evaluation of myofibrillar structure, extracellular matrix proteins, and calpain activity.

RESULTS:

In the exercised leg, peak torque was reduced by 47 +/- 5% during exercise and was still 22 +/- 5% lower than baseline 4 d after the exercise. Calpain activity was three times higher in the exercised leg compared with the control leg 30 min after exercise. Myofibrillar disruptions were observed in 36 +/- 6% of all fibers in exercised muscle and in 2 +/- 1% of fibers in control muscle. The individual reductions in peak torque correlated with the proportion of fibers with myofibrillar disruptions (r = 0.89). The increase in calpain activity was not correlated to the proportion of fibers with myofibrillar disruptions. Nevertheless, the characteristics of the myofibrillar disruptions mimicked calpain-mediated degradation of myofibrils. Tenascin-C and the N-terminal propeptide of procollagen type III showed increased staining intensity on cross-sections 4-7 d after the exercise.

CONCLUSIONS:

Myofibrillar disruptions seem to be a main cause for the long-lasting reduction in force-generating capacity after high-force eccentric exercise. The increase in calpain activity, but the lack of a relationship between calpain activity and the amount of muscle damage, suggests multiple roles of calpain in the damage and repair process.

PMID:
20010126
DOI:
10.1249/MSS.0b013e3181ac7afa
[Indexed for MEDLINE]

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