Skeletal Muscle Myofibrillar Protein Abundance Is Higher in Resistance-Trained Men, and Aging in the Absence of Training May Have an Opposite Effect.

Christopher G Vann,Carlton D Fox,Michael D Roberts,Petey W Mumford,Shelby C Osburn,Kaelin C Young,Johnathon H Moore,Veera L D Badisa,Jordan R Moon,Rakesh K Singh,Victor Ibeanusi,Cody Haun,Darren T Beck,Benjamin M Mwashote,Matthew A Romero,Paul A Roberson,Andreas N Kavazis

doi:10.3390/sports8010007

Abstract

Resistance training generally increases skeletal muscle hypertrophy, whereas aging is associated with a loss in muscle mass. Interestingly, select studies suggest that aging, as well as resistance training, may lead to a reduction in the abundance of skeletal muscle myofibrillar (or contractile) protein (per mg tissue). Proteomic interrogations have also demonstrated that aging, as well as weeks to months of resistance training, lead to appreciable alterations in the muscle proteome. Given this evidence, the purpose of this small pilot study was to examine total myofibrillar as well as total sarcoplasmic protein concentrations (per mg wet muscle) from the vastus lateralis muscle of males who were younger and resistance-trained (denoted as YT, n = 6, 25 ± 4 years old, 10 ± 3 self-reported years of training), younger and untrained (denoted as YU, n = 6, 21 ± 1 years old), and older and untrained (denoted as OU, n = 6, 62 ± 8 years old). The relative abundances of actin and myosin heavy chain (per mg tissue) were also examined using SDS-PAGE and Coomassie staining, and shotgun proteomics was used to interrogate the abundances of individual sarcoplasmic and myofibrillar proteins between cohorts. Whole-body fat-free mass (YT > YU = OU), VL thickness (YT > YU = OU), and leg extensor peak torque (YT > YU = OU) differed between groups (p < 0.05). Total myofibrillar protein concentrations were greater in YT versus OU (p = 0.005), but were not different between YT versus YU (p = 0.325). The abundances of actin and myosin heavy chain were greater in YT versus YU (p < 0.05) and OU (p < 0.001). Total sarcoplasmic protein concentrations were not different between groups. While proteomics indicated that marginal differences existed for individual myofibrillar and sarcoplasmic proteins between YT versus other groups, age-related differences were more prominent for myofibrillar proteins (YT = YU > OU, p < 0.05: 7 proteins; OU > YT = YU, p < 0.05: 11 proteins) and sarcoplasmic proteins (YT = YU > OU, p < 0.05: 8 proteins; OU > YT&YU, p < 0.05: 29 proteins). In summary, our data suggest that modest (~9%) myofibrillar protein packing (on a per mg muscle basis) was evident in the YT group. This study also provides further evidence to suggest that notable skeletal muscle proteome differences exist between younger and older humans. However, given that our n-sizes are low, these results only provide a preliminary phenotyping of the reported protein and proteomic variables.

Highlights

Skeletal muscle is a unique tissue in that it possesses cylindrical multi-nucleated cells with an abundance of contractile proteins in order to facilitate muscular contractions
There were no differences between groups for percent body fat (YT: 21.3 ± 3.1 %, young untrained men (YU): 23.1 ± 6.7 %, older untrained (OU): 19.4 ± 4.4 %, data not shown)
These findings suggest long-term resistance training may not result in sarcoplasmic hypertrophy

Summary

Introduction

Skeletal muscle is a unique tissue in that it possesses cylindrical multi-nucleated cells with an abundance of contractile (or myofibrillar) proteins in order to facilitate muscular contractions (reviewed in [1]). Certain studies have reported aging [6,7], and paradoxically weeks to months of resistance training, reduce skeletal muscle myofibrillar protein density [8,9] or actin and myosin heavy chain protein abundances [10]; the latter two proteins being the predominant myofibrillar proteins While the former occurrence is thought to be a molecular phenotype of aging [6], the latter occurrence may be reflective of sarcoplasmic hypertrophy where increases in muscle fiber size may occur through a more rapid expansion of the sarcoplasm relative to myofibril protein accretion [1]. Other human studies have reported similar findings in the vastus lateralis using TEM [9] and biochemical methods [10]

Results

Discussion

Conclusion