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J Appl Physiol (November 10, 2005). doi:10.1152/japplphysiol.01012.2005
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Submitted on August 22, 2005
Accepted on November 4, 2005

Hindlimb unloading increases muscle content of cytosolic but not nuclear Id2 and p53 proteins in young adult and aged rats

Parco M. Siu1, Emidio E. Pistilli1, Zsolt Murlasits1, and Stephen E. Alway1*

1 Laboratory of Muscle Biology and Sarcopenia, Exercise Physiology, West Virginia University School of Medicine, Morgantown, WV, USA

* To whom correspondence should be addressed. E-mail: salway{at}hsc.wvu.edu.

This study tested the hypothesis that Id2, p53, and heat shock proteins (HSP) are responsive to suspension-induced muscle atrophy. Fourteen days of hindlimb suspension was used to unload the leg musculature and induce atrophy in gastrocnemius muscles of young adult and aged rats. Following suspension, medial gastrocnemius muscle wet weight was reduced by ~30% and the muscle wet weight normalized to the animal bodyweight decreased by 11% and 15% in young adult and aged animals, respectively. mRNA abundances of Id2, p53, HSP70-2, and HSP27 did not change with suspension whereas HSP70-1 mRNA content was lower in the suspended muscle when compared to the control muscle in both young adult and aged animals. Our immunoblot analyses indicated protein expressions of HSP70 and HSP60 were not different between suspended and control muscles in both ages while HSP27 protein content was increased in suspended muscle relative to control muscle only in young adult animals. Id2 and p53 protein contents were elevated in the cytosolic fraction of suspended muscle when compared to the control muscle in both young and aged animals but these changes were not found in the nuclear protein fraction. Furthermore, as compared to young adult, aged muscles had a lower HSP70-1 mRNA content but higher HSP70-2 mRNA content and protein contents of Id2, p53, HSP70 and HSP27. These findings are consistent with the hypothesis that Id2 and p53 are responsive to unloading-induced muscle atrophy. Moreover, our data indicate that aging is accompanied with altered abundances of HSP70-1 and HSP70-2 mRNA in addition to Id2, p53, HSP70 and HSP27 protein in rat gastrocnemius muscle.




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