title: Id2 and p53 participate in apoptosis during unloading-induced muscle atrophy.
abstract: Apoptotic signaling was examined in the patagialis (PAT) muscles of young adult and old quail. One wing was loaded for 14 days to induce hypertrophy and then unloaded for 7 or 14 days to induce muscle atrophy. Although the nuclear Id2 protein content was not different between unloaded and control muscles in either age group, cytoplasmic Id2 protein content of unloaded muscles was higher than that in contralateral control muscles after 7 days of unloading in young quails. Nuclear and cytoplasmic p53 contents and the p53 nuclear index of the unloaded muscles were higher than those in control muscles after 7 days of unloading in young quails, whereas in aged quails, the p53 and Id2 contents and p53 nuclear index of the unloaded muscles were not altered by unloading. Immunofluorescent staining indicated that myonuclei and activated satellite cell nuclei contributed to the increased number of p53-positive nuclei. Conversely, unloading in either young adult or aged PAT muscles did not alter c-Myc protein content. Although Cu-Zn-SOD content was not different in unloaded and control muscles, Mn-SOD content increased in PAT muscles after 7 days of unloading in young quails, suggesting that unloading induced an oxidative disturbance in these muscles. Moderate correlational relationships existed among Id2, p53, c-Myc, SOD, apoptosis-regulatory factors, and TdT-mediated dUTP nick end labeling index. These data indicate that Id2 and p53 are involved in the apoptotic responses during unloading-induced muscle atrophy after hypertrophy in young adult birds. Furthermore, our data suggest that there is an aging-dependent regulation of Id2 and p53 during unloading of previously hypertrophied muscles.
authors.affiliation: Division of Exercise Physiology, West Virginia Univ. School of Medicine, Robert C. Byrd Health Science Center, Morgantown, WV 26506-9227, USA.
authors.forename: Parco M
authors.initials: PM
authors.lastname: Siu
authors.forename: Stephen E
authors.initials: SE
authors.lastname: Alway
mesh_terms: D000367:Age Factors; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D019417:Hindlimb Suspension / Q000502:physiology; D006984:Hypertrophy / Q000503:physiopathology; D020287:In Situ Nick-End Labeling; D051797:Inhibitor of Differentiation Protein 2; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000503:physiopathology; D009133:Muscular Atrophy / Q000378:metabolism* / Q000503:physiopathology; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism; D011784:Quail; D012097:Repressor Proteins / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D051797:Inhibitor of Differentiation Protein 2; D016271:Proto-Oncogene Proteins c-myc; D012097:Repressor Proteins; D014157:Transcription Factors; D016159:Tumor Suppressor Protein p53; D013482:Superoxide Dismutase