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The effects of aging and muscle contraction on AMPK activity
Author(s) -
Hardman Shalene E.,
Hall Derrick E.,
Mitchell Alyssa J.,
Black Kyler M.,
Compton Richard A.,
Thomson David M.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.1149.3
Subject(s) - ampk , skeletal muscle , medicine , endocrinology , protein kinase a , amp activated protein kinase , chemistry , contraction (grammar) , phosphorylation , muscle contraction , biochemistry
Many cell processes that are disrupted in aging skeletal muscle are also regulated by AMP‐activated protein kinase (AMPK). However, the effect of aging on skeletal muscle AMPK activation is controversial and unclear. Our purpose was to determine the effect of old‐age on endurance‐type contraction‐induced AMPK activation in skeletal muscle. Gastrocnemius muscles from YA (8 mo old) and O (30 mo old) male Fischer344 x Brown Norway F1 hybrid rats were removed after 10 minutes of electrically stimulated in situ contractions (STIM). Muscles from the resting legs served as controls (REST). AMPK phosphorylation and AMPKα2 activity were 63% and 19% lower, respectively, in O vs. YA muscles after STIM. AMPKα1 activity was unaffected by STIM in YA, but increased by 30% in O muscles. AMPK α1 protein concentration was 45% greater, while α2 content was 18% lower in O vs. YA muscles. AMPK β1, β2, and γ1 proteins were unaffected by age, but AMPK γ2 and γ3 concentrations were 75% and 85% lower in O vs. YA muscles, respectively. In conclusion, AMPKα2 activation is impaired while AMPKα1 activation is enhanced after endurance‐type in situ contractions in aged skeletal muscle. This work was funded by NIAMSD Grant AR‐51928.