scholarly journals Resistance Exercise Reverses Aging in Human Skeletal Muscle

PLoS ONE ◽  
2007 ◽  
Vol 2 (5) ◽  
pp. e465 ◽  
Author(s):  
Simon Melov ◽  
Mark A. Tarnopolsky ◽  
Kenneth Beckman ◽  
Krysta Felkey ◽  
Alan Hubbard
2011 ◽  
Vol 61 (2) ◽  
pp. 131-140 ◽  
Author(s):  
Ryo Kakigi ◽  
Hisashi Naito ◽  
Yuji Ogura ◽  
Hiroyuki Kobayashi ◽  
Norio Saga ◽  
...  

2017 ◽  
Vol 49 (5S) ◽  
pp. 339
Author(s):  
Jared M. Dickinson ◽  
Andrew C. D’Lugos ◽  
Marcus Naymik ◽  
Matt De Both ◽  
Ashley Siniard ◽  
...  

2019 ◽  
Vol 7 (12) ◽  
Author(s):  
Roldan M. de Guia ◽  
Marianne Agerholm ◽  
Thomas S. Nielsen ◽  
Leslie A. Consitt ◽  
Ditte Søgaard ◽  
...  

2017 ◽  
Vol 49 (5S) ◽  
pp. 801
Author(s):  
Andrew C. D’Lugos ◽  
Shivam H. Patel ◽  
Jordan C. Ormsby ◽  
Tara N. Mahmood ◽  
Don P. Curtis ◽  
...  

Autophagy ◽  
2015 ◽  
Vol 11 (3) ◽  
pp. 538-546 ◽  
Author(s):  
Anna Ulbricht ◽  
Sebastian Gehlert ◽  
Barbara Leciejewski ◽  
Thorsten Schiffer ◽  
Wilhelm Bloch ◽  
...  

2015 ◽  
Vol 47 (9) ◽  
pp. 1922-1931 ◽  
Author(s):  
CRAIG PORTER ◽  
PAUL T. REIDY ◽  
NISHA BHATTARAI ◽  
LABROS S. SIDOSSIS ◽  
BLAKE B. RASMUSSEN

2017 ◽  
Vol 313 (1) ◽  
pp. R44-R50 ◽  
Author(s):  
Shivam H. Patel ◽  
Andrew C. D’Lugos ◽  
Erica R. Eldon ◽  
Donald Curtis ◽  
Jared M. Dickinson ◽  
...  

Acetaminophen (APAP) given during chronic exercise reduces skeletal muscle collagen and cross-linking in rats. We propose that the effect of APAP on muscle extracellular matrix (ECM) may, in part, be mediated by dysregulation of the balance between matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs). The purpose of this study was to evaluate the impact of APAP consumption during acute resistance exercise (RE) on several regulators of the ECM in human skeletal muscle. In a double-blinded, placebo-controlled, randomized crossover design, recreationally active men ( n = 8, 25 ± 2 yr) performed two trials of knee extension. Placebo (PLA) or APAP (1,000 mg/6 h) was given for 24 h before and immediately following RE. Vastus lateralis biopsies were taken at baseline and 1 and 3 h post-RE. Quantitative RT-PCR was used to determine differences in mRNA expression. MMP-2, type I collagen, and type III collagen mRNA expression was not altered by exercise or APAP ( P > 0.05). When compared with PLA, TIMP-1 expression was lower at 1 h post-RE during APAP conditions but greater than PLA at 3 h post-RE ( P < 0.05). MMP-9 expression and protein levels were elevated at 3 h post-RE independent of treatment ( P < 0.05). Lysyl oxidase expression was greater at 3 h post-RE during APAP consumption ( P < 0.05) compared with PLA. MMP-2 and TIMP-1 protein was not altered by RE or APAP ( P > 0.05). Phosphorylation of ERK1/2 and p38-MAPK increased ( P < 0.05) with RE but was not influenced by APAP. Our findings do not support our hypothesis and suggest that short-term APAP consumption before RE has a small impact on the measured ECM molecules in human skeletal muscle following acute RE.


2016 ◽  
Vol 41 (8) ◽  
pp. 856-863 ◽  
Author(s):  
Neil A. Schwarz ◽  
Sarah K. McKinley-Barnard ◽  
Mike B. Spillane ◽  
Thomas L. Andre ◽  
Joshua J. Gann ◽  
...  

The purpose of this study was to investigate the acute messenger (mRNA) expression of the peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) isoforms, insulin-like growth factor-1Ea (IGF-1Ea), and myostatin in response to 2 resistance exercise intensities. In a uniform-balanced, crossover design, 10 participants performed 2 separate testing sessions involving a lower body resistance exercise component consisting of a lower intensity (50% of 1-repetition maximum; 1RM) protocol and a higher intensity (80% of 1RM) protocol of equal volumes. Muscle samples were obtained at before exercise, 45 min, 3 h, 24 h, and 48 h postexercise. Resistance exercise did not alter total PGC-1α mRNA expression; however, distinct responses of each PGC-1α isoform were observed. The response of each isoform was consistent between sessions, suggesting no effect of resistance exercise intensity on the complex transcriptional expression of the PGC-1α gene. IGF-1Ea mRNA expression significantly increased following the higher intensity session compared with pre-exercise and the lower intensity session. Myostatin mRNA expression was significantly reduced compared with pre-exercise values at all time points with no difference between exercise intensity. Further research is needed to determine the effects of the various isoforms of PGC-1α in human skeletal muscle on the translational level as well as their relation to the expression of IGF-1 and myostatin.


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