Effects of Elevated Circulating Hormones on
Resistance Exercise-Induced Akt Signaling
Med. Sci. Sports Exerc., Vol. 40, No. 6, pp. 1041–1050, 2008.
BARRY A.
ABSTRACT
Purpose: Hormones and muscle contraction alter protein kinase B (Akt) signaling via distinct mechanisms. Therefore, the purpose of this study was to determine whether physiologically elevated circulating hormones modulate resistance exercise (RE)-induced signaling
of Akt and its downstream targets. We hypothesized that elevated circulating hormones would potentiate the signaling response.
Methods: Seven healthy men (mean T SD age, 27 T 4 yr; body mass, 79.1 T 13.6 kg; body fat, 16% T 7%) performed two identical lower-body RE protocols (five sets of five maximal repetitions of knee extensions) in a randomized order and separated by 1–3 wk: one
protocol was preceded by rest [low-circulating hormonal concentration (LHC) trial], and the other was preceded by a bout of high volume upper-body RE using short rest periods designed to elicit a large increase in circulating hormones [high-circulating hormonal
concentration (HHC) trial].
Results: The HHC trial invoked significantly (P e 0.05) greater growth hormone (GH) and cortisol
concentrations compared with the LHC trial. There were minimal differences between trials in insulin and insulin-like growth factor-I (IGF-I) concentrations. Contrary to our hypothesis, 70-kDa ribosomal protein S6 kinase (p70 S6K) threonine (Thr) 389 phosphorylation
within the vastus lateralis was attenuated at 180 min post-RE during the HHC trial. RE did not affect Akt or glycogen synthase kinase- 3A (GSK-3A) phosphorylation nor were there differences between trials. Immediately post-RE, eukaryotic initiation factor (eIF) 4E binding protein-1 (4E-BP1) phosphorylation declined, and adenosine monophosphate-activated protein kinase (AMPK) phosphorylation increased; however, there were no differences between trials in these variables.
Conclusion: p70 S6K Thr 389 phosphorylation
was attenuated during the HHC trial despite dramatically greater (92.5-fold) circulating GH concentrations; this was potentially due to
cortisol-induced inhibition of p70 S6K Thr 389 phosphorylation.
Resistance Exercise-Induced Akt Signaling
Med. Sci. Sports Exerc., Vol. 40, No. 6, pp. 1041–1050, 2008.
BARRY A.
ABSTRACT
Purpose: Hormones and muscle contraction alter protein kinase B (Akt) signaling via distinct mechanisms. Therefore, the purpose of this study was to determine whether physiologically elevated circulating hormones modulate resistance exercise (RE)-induced signaling
of Akt and its downstream targets. We hypothesized that elevated circulating hormones would potentiate the signaling response.
Methods: Seven healthy men (mean T SD age, 27 T 4 yr; body mass, 79.1 T 13.6 kg; body fat, 16% T 7%) performed two identical lower-body RE protocols (five sets of five maximal repetitions of knee extensions) in a randomized order and separated by 1–3 wk: one
protocol was preceded by rest [low-circulating hormonal concentration (LHC) trial], and the other was preceded by a bout of high volume upper-body RE using short rest periods designed to elicit a large increase in circulating hormones [high-circulating hormonal
concentration (HHC) trial].
Results: The HHC trial invoked significantly (P e 0.05) greater growth hormone (GH) and cortisol
concentrations compared with the LHC trial. There were minimal differences between trials in insulin and insulin-like growth factor-I (IGF-I) concentrations. Contrary to our hypothesis, 70-kDa ribosomal protein S6 kinase (p70 S6K) threonine (Thr) 389 phosphorylation
within the vastus lateralis was attenuated at 180 min post-RE during the HHC trial. RE did not affect Akt or glycogen synthase kinase- 3A (GSK-3A) phosphorylation nor were there differences between trials. Immediately post-RE, eukaryotic initiation factor (eIF) 4E binding protein-1 (4E-BP1) phosphorylation declined, and adenosine monophosphate-activated protein kinase (AMPK) phosphorylation increased; however, there were no differences between trials in these variables.
Conclusion: p70 S6K Thr 389 phosphorylation
was attenuated during the HHC trial despite dramatically greater (92.5-fold) circulating GH concentrations; this was potentially due to
cortisol-induced inhibition of p70 S6K Thr 389 phosphorylation.