Purpose: Recently, it has been suggested that a cellular pathway composed of integrin, integrin-linked kinase (ILK), rapamycin-insensitive companion of mTOR (RICTOR), and Akt may facilitate long-term structural and functional adaptations associated with exercise, independent of the mTORC1 pathway. Therefore, we examined changes in integrin-ILK-RICTOR-Akt protein in vastus lateralis (VL) before and after 8 wk of eccentric cycling training (ECC), which was expected to increase muscle function and VL cross-sectional area (CSA).
Methods: Eleven men (23 ± 4 yr) completed 24 sessions of ECC with progressive increases in intensity and duration, resulting in a twofold increase in work from the first three (75.4 ± 14.1 kJ) to the last three sessions (150.7 ± 28.4 kJ). Outcome measures included lower limb lean mass, VL CSA, static strength, and peak and average cycling power output. These measures and VL samples were taken before and 4-5 d after the last training session.
Results: Significant (P < 0.05) increases in integrin-β1 (1.64-fold) and RICTOR (2.99-fold) protein as well as the phosphorylated-to-total ILK ratio (1.70-fold) were found, but integrin-α7 and Akt did not change. Increases in lower limb, thigh, and trunk lean mass (2.8%-5.3%, P < 0.05) and CSA (13.3% ± 9.0%, P < 0.001) were observed. Static strength (18.1% ± 10.8%) and both peak (8.6% ± 10.5%) and average power output (7.4% ± 8.3%) also increased (P < 0.05). However, no significant correlations were found between the magnitude of increases in protein and the magnitude of increases in CSA, static strength, or power output.
Conclusions: In addition to increased muscle mass, strength, and power, we demonstrate that ECC increases integrin-β1 and RICTOR total protein and p-ILK/t-ILK, which may play a role in protection against muscle damage as well as anabolic signaling to induce muscle adaptations.
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http://dx.doi.org/10.1249/MSS.0000000000002778 | DOI Listing |
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School of Chemistry, Liaoning University, Shenyang 110036, China. Electronic address:
In this study, the interactions between three quaternary ammonium salt (QAS) cationic surfactants with different branched-chain lengths (TMBAC, TEBAC, and TBBAC) and DNA are investigated by UV-vis absorption, fluorescence and CD spectroscopy, viscosity method, and gel electrophoresis. Berberine hydrochloride (BR) is utilized as a fluorescent probe. The three interaction modes and strengths are compared.
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School of Mechanical and Aerospace Engineering, Jilin University, Changchun 130025 PR China.
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Laboratory of Biomechanics and Medical Imaging, Faculty of Medicine, Saint-Joseph University of Beirut, Beirut, Lebanon; Institut de Biomécanique Humaine Georges Charpak, Arts et Métiers, Paris, France. Electronic address:
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