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HIGHLIGHTED TOPICS
Biomechanics and Mechanotransduction in Cell and Tissues

Aging does not alter the mechanosensitivity of the p38, p70^S6k, and JNK2 signaling pathways in skeletal muscle

¹School of Kinesiology, University of Illinois Chicago, Chicago, Illinois; and ²Pfizer Global Research and Development, Groton, Connecticut

Submitted 11 August 2004 ; accepted in final form 6 September 2004

The capacity for skeletal muscle to recover its mass following periods of unloading (regrowth) has been reported to decline with age. Although the mechanisms responsible for the impaired regrowth are not known, it has been suggested that aged muscles have a diminished capacity to sense and subsequently respond to a given amount of mechanical stimuli (mechanosensitivity). To test this hypothesis, extensor digitorum longus muscles from young (2–3 mo) and old (26–27 mo) mice were subjected to intermittent 15% passive stretch (ex vivo) as a source of mechanical stimulation and analyzed for alterations in the phosphorylation of stress-activated protein kinase (p38), ribosomal S6 kinase (p70^S6k), and the p54 jun N-terminal kinase (JNK2). The results indicated that the average magnitude of specific tension (mechanical stimuli) induced by 15% stretch was similar in muscles from young and old mice. Young and old muscles also revealed similar increases in the magnitude of mechanically induced p38, p70^S6k (threonine/serine 421/424 and threonine 389), and JNK2 phosphorylation. In addition, coincubation experiments demonstrated that the release of locally acting growth factors was not sufficient for the induction of JNK2 phosphorylation, suggesting that JNK2 was activated by a mechanical rather than a mechanical/growth factor-dependent mechanism. Taken together, the results of this study demonstrate that aging does not alter the mechanosensitivity of the p38, p70^S6k, and JNK2 signaling pathways in skeletal muscle.

stretch; mechanotransduction; growth; hypertrophy; atrophy

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