Resistance training increases heat shock protein levels in skeletal muscle of young and old rats.
Heat shock proteins (HSP) HSP72, HSC70 and HSP25 protein levels and mRNA levels of HSP72 genes (Hsp72-1, Hsp72-2, Hsp72-3) and HSC70 were examined in tibialis anterior muscles from young and old rats following 4.5 weeks of heavy resistance exercise. Young (3 months) (n=10) and old (30 months) (n=9) rats were subjected to 14 sessions of electrically evoked resistance training using stretch-shortening contractions of the left limb that activated the dorsiflexor muscle group, including the tibialis anterior muscle, while the right side served as the intra-animal control. Muscle wet weight of the left tibialis anterior increased by 15.6% in young animals compared to the untrained right side, while the aged rats demonstrated no significant hypertrophy based on muscle wet weight. There were no differences in mRNA expression between the control and experimental muscles in either the old or the young animals for any of the four genes examined. On the other hand, HSP72 levels as determined by Western blots were significantly (p<0.01) higher (968.8 and 409.1%) in the trained as compared to the contralateral control muscle in young and old animals, respectively. HSP25 expression was increased significantly (p<0.01) by training in muscles of young rats (943.1%) and old rats (420.3%). Moreover, there was no training by age interaction for HSP72, while a significant age and training by age effects were found in muscles for HSP25. There was no change in HSC70 protein expression in response to the training intervention in either age group. SOD-1 enzyme level increased by 66.6% in the trained muscles of the young rats, while this enzyme was 33% lower in trained muscles compared to the untrained control side in old rats. Moreover, a significant (p<0.05) training by age interaction was found for SOD-1 enzyme levels. This study suggests that fast contracting muscles in young and old animals are capable of increasing HSP expression in response to high intensity contractile stress. Furthermore, the data are consistent with the hypothesis that higher levels of oxidative stress in muscles of old animals limit HSP levels and/or function in response to high intensity contractile stress.
Murlasits
Zsolt
Z
Division of Exercise Physiology, Laboratory of Muscle Biology and Sarcopenia, West Virginia University School of Medicine, Robert C. Byrd Health Sciences Center, Morgantown, WV 26506-9227, USA.
Cutlip
Robert G
RG
Geronilla
Kenneth B
KB
Rao
K Murali K
KM
Wonderlin
William F
WF
Alway
Stephen E
SE
D000375:Aging / Q000378:metabolism* / Q000473:pathology / Q000502:physiology; D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology; D015153:Blotting, Western / Q000379:methods; D001835:Body Weight / Q000502:physiology; D004558:Electric Stimulation; D055551:HSP27 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins / Q000032:analysis / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D007537:Isometric Contraction / Q000187:drug effects / Q000502:physiology; D008297:Male; D018482:Muscle, Skeletal / Q000033:anatomy & histology / Q000378:metabolism* / Q000502:physiology; D009363:Neoplasm Proteins / Q000032:analysis / Q000378:metabolism; D009929:Organ Size / Q000502:physiology; D005082:Physical Exertion / Q000502:physiology*; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D011916:Rats, Inbred F344; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013482:Superoxide Dismutase / Q000032:analysis / Q000378:metabolism; D000072105:Superoxide Dismutase-1; D014810:Vitamin E / Q000494:pharmacology
D055551:HSP27 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D014810:Vitamin E; C000606292:Sod1 protein, rat; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D001205:Ascorbic Acid