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1Department of Zoology, La Trobe University, Victoria; 2Muscle, Ions and Exercise Group, Centre for Ageing, Rehabilitation, Exercise and Sport, School of Human Movement, Recreation and Performance, Victoria University, Melbourne; and 3Department of Nephrology, Royal Melbourne Hospital and Western Hospital, Melbourne, Australia
Submitted 14 December 2006 ; accepted in final form 15 June 2007
The function and normal regulation of calpain-3, a muscle-specific Ca2+-dependent protease, is uncertain, although its absence leads to limb-girdle muscular dystrophy type 2A. This study examined the effect of eccentric exercise on calpain-3 autolytic activation, because such exercise is known to damage sarcomeric structures and to trigger adaptive changes that help prevent such damage on subsequent exercise. Six healthy human subjects performed a 30-min bout of one-legged, eccentric, knee extensor exercise. Torque measurements, vastus lateralis muscle biopsies, and venous blood samples were taken before and up to 7 days following the exercise. Peak isometric muscle torque was depressed immediately and at 3 h postexercise and recovered by 24 h, and serum creatine kinase concentration peaked at 24 h postexercise. The amount of autolyzed calpain-3 was unchanged immediately and 3 h after exercise, but increased markedly (from 
16% to 35% of total) 24 h after the exercise, and returned to preexercise levels within 7 days. In contrast, the eccentric exercise produced little autolytic activation of the ubiquitous Ca2+-activated protease, µ-calpain. Eccentric exercise is the first physiological circumstance shown to result in calpain-3 activation in vivo.
µ-calpain; proteolysis; autolysis; muscle damage
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