Glover · The Journal of physiology 2008 · within-subject controlled trial · n=12

Immobilization induces anabolic resistance in human myofibrillar protein synthesis with low and high dose amino acid infusion.

Cited 413 times in the scientific literature.

Level 3 - non-randomized controlled study

Prospective within-subject controlled physiological trial using the contralateral limb as control without randomization.

PubMed 18955382 · doi:10.1113/jphysiol.2008.160333 · record verified 2026-08-30

What was done

Twelve young healthy adults (10 men, 2 women, age 21 ± 1 years, body weight 80.2 ± 4.0 kg) underwent 14 days of unilateral knee immobilization with the contralateral leg serving as a non-immobilized control. Quadriceps myofibrillar protein synthesis (MPS) was measured in both legs in the post-absorptive state and during intravenous amino acid infusion (10% Primene) at low (43 mg/kg/h) or high (261 mg/kg/h) doses. Quadriceps muscle cross-sectional area (MRI), peak isometric torque, anabolic signaling phosphorylation, and polyubiquitinated protein content were also assessed.

What was found

In the immobilized leg, muscle cross-sectional area decreased by -5.0 ± 1.2% and peak isometric torque decreased by -25 ± 3% (both P < 0.005), with no changes in the non-immobilized leg (P > 0.6). Basal post-absorptive MPS was 27% lower in the immobilized leg (0.027 ± 0.003%/h) compared to the non-immobilized leg (0.037 ± 0.003%/h; P < 0.001). Amino acid infusion stimulated MPS in both legs, but the response was blunted in the immobilized limb: at 4 h, MPS was higher in the non-immobilized leg by +54 ± 12% at the low dose and +68 ± 17% at the high dose (both P < 0.001). Phosphorylation of focal adhesion kinase (Tyr576/577) declined with immobilization (P < 0.05), whereas polyubiquitinated protein content remained unchanged.

Why it matters

This study shows that disuse muscle atrophy is primarily driven by reduced basal muscle protein synthesis and blunted sensitivity to hyperaminoacidemia, which cannot be rescued simply by increasing amino acid availability.

Limits

The sample size was small (n = 12) with an uneven sex distribution (10 men, 2 women) and tested only young, healthy adults. Amino acids were administered intravenously rather than through oral protein feeding, and muscle protein breakdown rates were not directly quantified.

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