Research

Hormonal

Resistance exercise followed immediately by protein feeding significantly increases phosphorylation of Akt Ser473, p70S6K1 Thr412, and rpS6 Ser235/236 in human skeletal muscle, with the combined stimulus producing greater or more sustained signaling than feeding alone.

To maximize the cellular signaling for muscle growth, combine resistance exercise with protein intake. This study shows that doing both together triggers a stronger and more sustained activation of key muscle-building pathways (mTORC1) than eating protein alone. Specifically, performing resistance training followed by a protein-containing meal leads to higher levels of signaling molecules like Akt and p70S6K1, which are critical for muscle protein synthesis.

GoodSupportsMEDIUM confidence
Phosphorylated Akt Ser473 was significantly elevated (~2.0-fold) from Pre at 1 h FEDEX... Phosphorylated p70S6K1 Thr412 was significantly increased above Pre at 1 h FEDEX (~3.0-fold) and 1 h FED (~1.0-fold; P < 0.05) and was still significantly elevated at 3 h FEDEX but not at 3 h FED... Phosphorylated rpS6 Ser235/236 was also significantly increased above Pre at 1 h FEDEX (~3.0-fold; P < 0.05) and 1 h FED (~1.2-fold; P < 0.05) with 1 h FEDEX greater than 1 h FED
Chris McGlory et al. · Applied Physiology Nutrition and Metabolism · 2018

Why this rating

Small sample size (n=8) and cross-sectional biopsy design limit generalizability, but the use of multiplex assays validated against immunoblotting and previous activity assays adds methodological rigor.

Source

Assessing the mechanistic target of rapamycin complex-1 pathway in response to resistance exercise and feeding in human skeletal muscle by multiplex assay

Chris McGlory et al. · Applied Physiology Nutrition and Metabolism · 2018

DOI 10.1139/apnm-2017-0852

mechanism_only · n=8Cited 2×
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DOI resolved against Crossref · corpus check 2026-06-10

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