Alterations in molecular muscle mass regulators after 8 days immobilizing Special Forces mission.

In military operations, declined physical capacity can endanger the life of soldiers. During special support and reconnaissance (SSR) missions, Special Forces soldiers sustain 1-2 weeks full-body horizontal immobilization, which impairs muscle strength and performance. Adequate muscle mass and strength are necessary in combat or evacuation situations, which prompt for improved understanding of muscle mass modulation during SSR missions. To explore the molecular regulation of myofiber size during a simulated SSR operation, nine male Special Forces soldiers were biopsied in m. vastus lateralis pre and post 8 days immobilizing restricted prone position. After immobilization, total mammalian target of rapamycin protein was reduced by 42% (P < 0.05), whereas total and phosphorylated protein levels of Akt, ribosomal protein S6k, 4E-BP1, and glycogen synthase kinase3ß were unchanged. Messenger RNA (mRNA) levels of the atrogenes forkhead box O3 (FoxO3), atrogin1, and muscle ring finger protein1 (MuRF1) increased by 36%, 53%, and 71% (P < 0.01), MuRF1 protein by 51% (P = 0.05), whereas FoxO1 and peroxisome proliferator-activated receptor γ coactivator-1 ß mRNAs decreased by 29% and 40% (P < 0.01). In conclusion, occupational immobilization in Special Forces soldiers led to modulations in molecular muscle mass regulators during 8 days prone SSR mission, which likely contribute to muscle loss observed in such operations. The present data expand our knowledge of human muscle mass regulation during short-term immobilization.

Myostatin expression during human muscle hypertrophy and subsequent atrophy: increased myostatin with detraining.

Myostatin is a potent negative regulator of skeletal muscle mass, but its role in human skeletal muscle hypertrophy and atrophy is sparsely described. Muscle biopsies were obtained from young male subjects before and after 30 and 90 days of resistance training as well as after 3, 10, 30, 60 and 90 days of subsequent detraining. Myostatin mRNA increased significantly with detraining. We observed a 28 kDa myostatin immunoreactive protein, which, however, was also present in myostatin knock out mice skeletal muscle. As a novel finding we consistently detected a 10 kDa band, which may represent a mature myostatin monomer under reducing conditions or a novel, unknown myostatin form. Further, we observed a significant increase in this 10 kDa band after 3 days of detraining preceding the rapid type II fiber atrophy, in which almost half of the acquired fiber area was lost after only 10 days of detraining. Accordingly, an increase in the level of the 10 kDa protein is associated with rapid type II fiber atrophy, suggesting myostatin-mediated specific type II fiber atrophy, which in combination with our mRNA data support a role for myostatin in the negative regulation of adult human skeletal muscle mass.