Hindlimb unloading increases muscle content of cytosolic but not nuclear Id2 and p53 proteins in young adult and aged rats.
This study tested the hypothesis that inhibitor of differentiation-2 (Id2), p53, and heat shock proteins (HSP) are responsive to suspension-induced muscle atrophy. Fourteen days of hindlimb suspension were used to unload the hindlimbs and induce atrophy in gastrocnemius muscles of young adult and aged rats. Following suspension, medial gastrocnemius muscle wet weight was reduced by approximately 30%, and the muscle wet weight normalized to the animal body weight 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 compared with the control muscle in both young adult and aged animals. Our immunoblot analyses indicated that protein expressions of HSP70 and HSP60 were not different between suspended and control muscles in both ages, whereas 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 compared with the control muscle in both young and aged animals, but these changes were not found in the nuclear protein fraction. Furthermore, compared with 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.
Siu
Parco M
PM
Laboratory of Muscle Biology and Sarcopenia, Division of Exercise Physiology, School of Medicine, Robert C. Byrd Health Sciences Center, West Virginia Univ., Morgantown, WV 26506-9227, USA.
Pistilli
Emidio E
EE
Murlasits
Zsolt
Z
Alway
Stephen E
SE
D000375:Aging; D000818:Animals; D017209:Apoptosis / Q000235:genetics / Q000502:physiology; D002467:Cell Nucleus / Q000737:chemistry*; D018834:Chaperonin 60 / Q000032:analysis / Q000235:genetics / Q000502:physiology; D003600:Cytosol / Q000737:chemistry*; D005786:Gene Expression Regulation; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D006360:Heat-Shock Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D019417:Hindlimb Suspension / Q000502:physiology*; D051797:Inhibitor of Differentiation Protein 2 / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D018482:Muscle, Skeletal / Q000737:chemistry*; D009133:Muscular Atrophy / Q000235:genetics / Q000503:physiopathology; D009363:Neoplasm Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D016133:Polymerase Chain Reaction; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D051381:Rats; D011914:Rats, Inbred BN; D011916:Rats, Inbred F344; D013997:Time Factors; D016159:Tumor Suppressor Protein p53 / Q000032:analysis* / Q000235:genetics / Q000502:physiology
D018834:Chaperonin 60; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; C497451:Id2 protein, rat; D051797:Inhibitor of Differentiation Protein 2; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D016159:Tumor Suppressor Protein p53