Browsing by Author "Romero, Matthew A"
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Item Open Access An intron variant of the GLI family zinc finger 3 (GLI3) gene differentiates resistance training-induced muscle fiber hypertrophy in younger men.(FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2021-05) Vann, Christopher G; Morton, Robert W; Mobley, Christopher B; Vechetti, Ivan J; Ferguson, Brian K; Haun, Cody T; Osburn, Shelby C; Sexton, Casey L; Fox, Carlton D; Romero, Matthew A; Roberson, Paul A; Oikawa, Sara Y; McGlory, Chris; Young, Kaelin C; McCarthy, John J; Phillips, Stuart M; Roberts, Michael DWe examined the association between genotype and resistance training-induced changes (12 wk) in dual x-ray energy absorptiometry (DXA)-derived lean soft tissue mass (LSTM) as well as muscle fiber cross-sectional area (fCSA; vastus lateralis; n = 109; age = 22 ± 2 y, BMI = 24.7 ± 3.1 kg/m2 ). Over 315 000 genetic polymorphisms were interrogated from muscle using DNA microarrays. First, a targeted investigation was performed where single nucleotide polymorphisms (SNP) identified from a systematic literature review were related to changes in LSTM and fCSA. Next, genome-wide association (GWA) studies were performed to reveal associations between novel SNP targets with pre- to post-training change scores in mean fCSA and LSTM. Our targeted investigation revealed no genotype-by-time interactions for 12 common polymorphisms regarding the change in mean fCSA or change in LSTM. Our first GWA study indicated no SNP were associated with the change in LSTM. However, the second GWA study indicated two SNP exceeded the significance level with the change in mean fCSA (P = 6.9 × 10-7 for rs4675569, 1.7 × 10-6 for rs10263647). While the former target is not annotated (chr2:205936846 (GRCh38.p12)), the latter target (chr7:41971865 (GRCh38.p12)) is an intron variant of the GLI Family Zinc Finger 3 (GLI3) gene. Follow-up analyses indicated fCSA increases were greater in the T/C and C/C GLI3 genotypes than the T/T GLI3 genotype (P < .05). Data from the Auburn cohort also revealed participants with the T/C and C/C genotypes exhibited increases in satellite cell number with training (P < .05), whereas T/T participants did not. Additionally, those with the T/C and C/C genotypes achieved myonuclear addition in response to training (P < .05), whereas the T/T participants did not. In summary, this is the first GWA study to examine how polymorphisms associate with the change in hypertrophy measures following resistance training. Future studies are needed to determine if the GLI3 variant differentiates hypertrophic responses to resistance training given the potential link between this gene and satellite cell physiology.Item Open Access Biomarkers associated with low, moderate, and high vastus lateralis muscle hypertrophy following 12 weeks of resistance training(PLOS ONE) Mobley, Christopher B; Haun, Cody T; Roberson, Paul A; Mumford, Petey W; Kephart, Wesley C; Romero, Matthew A; Osburn, Shelby C; Vann, Christopher G; Young, Kaelin C; Beck, Darren T; Martin, Jeffrey S; Lockwood, Christopher M; Roberts, Michael DItem Open Access Effects of Graded Whey Supplementation During Extreme-Volume Resistance Training(Frontiers in Nutrition) Haun, Cody T; Vann, Christopher G; Mobley, Christopher B; Roberson, Paul A; Osburn, Shelby C; Holmes, Hudson M; Mumford, Petey M; Romero, Matthew A; Young, Kaelin C; Moon, Jordan R; Gladden, L Bruce; Arnold, Robert D; Israetel, Michael A; Kirby, Annie N; Roberts, Michael DItem Open Access LAT1 Protein Content Increases Following 12 Weeks of Resistance Exercise Training in Human Skeletal Muscle(Frontiers in Nutrition) Roberson, Paul A; Mobley, C Brooks; Romero, Matthew A; Haun, Cody T; Osburn, Shelby C; Mumford, Petey W; Vann, Christopher G; Greer, Rory A; Ferrando, Arny A; Roberts, Michael DIntroduction: Amino acid transporters are essential for cellular amino acid transport and promoting protein synthesis. While previous literature has demonstrated the association of amino acid transporters and protein synthesis following acute resistance exercise and amino acid supplementation, the chronic effect of resistance exercise and supplementation on amino acid transporters is unknown. The purpose herein was to determine if amino acid transporters and amino acid metabolic enzymes were related to skeletal muscle hypertrophy following resistance exercise training with different nutritional supplementation strategies.Methods: 43 college-aged males were separated into a maltodextrin placebo (PLA, n = 12), leucine (LEU, n = 14), or whey protein concentrate (WPC, n = 17) group and underwent 12 weeks of total-body resistance exercise training. Each group's supplement was standardized for total energy and fat, and LEU and WPC supplements were standardized for total leucine (6 g/d). Skeletal muscle biopsies were obtained prior to training and ~72 h following each subject's last training session.Results: All groups increased type I and II fiber cross-sectional area (fCSA) following training (p < 0.050). LAT1 protein increased following training (p < 0.001) and increased more in PLA than LEU and WPC (p < 0.050). BCKDHα protein increased and ATF4 protein decreased following training (p < 0.001). Immunohistochemistry indicated total LAT1/fiber, but not membrane LAT1/fiber, increased with training (p = 0.003). Utilizing all groups, the change in ATF4 protein, but no other marker, trended to correlate with the change in fCSA (r = 0.314; p = 0.055); however, when regression analysis was used to delineate groups, the change in ATF4 protein best predicted the change in fCSA only in LEU (r2 = 0.322; p = 0.043). In C2C12 myoblasts, LAT1 protein overexpression caused a paradoxical decrease in protein synthesis levels (p = 0.002) and decrease in BCKDHα protein (p = 0.001).Conclusions: Amino acid transporters and metabolic enzymes are affected by resistance exercise training, but do not appear to dictate muscle fiber hypertrophy. In fact, overexpression of LAT1 in vitro decreased protein synthesis.Item Open Access Molecular Differences in Skeletal Muscle After 1 Week of Active vs. Passive Recovery From High-Volume Resistance Training(Journal of Strength and Conditioning Research, 2021-08) Vann, Christopher G; Haun, Cody T; Osburn, Shelby C; Romero, Matthew A; Roberson, Paul A; Mumford, Petey W; Mobley, C Brooks; Holmes, Hudson M; Fox, Carlton D; Young, Kaelin C; Roberts, Michael DAbstract Vann, CG, Haun, CT, Osburn, SC, Romero, MA, Roberson, PA, Mumford, PW, Mobley, CB, Holmes, HM, Fox, CD, Young, KC, and Roberts, MD. Molecular differences in skeletal muscle after 1 week of active vs. passive recovery from high-volume resistance training. J Strength Cond Res 35(8): 2102–2113, 2021—Numerous studies have evaluated how deloading after resistance training (RT) affects strength and power outcomes. However, the molecular adaptations that occur after deload periods remain understudied. Trained, college-aged men (n = 30) performed 6 weeks of whole-body RT starting at 10 sets of 10 repetitions per exercise per week and finishing at 32 sets of 10 repetitions per exercise per week. After this period, subjects performed either active (AR; n = 16) or passive recovery (PR; n = 14) for 1 week where AR completed ∼15% of the week 6 training volume and PR ceased training. Variables related to body composition and recovery examined before RT (PRE), after 6 weeks of RT (POST), and after the 1-week recovery period (DL). Vastus lateralis (VL) muscle biopsies and blood samples were collected at each timepoint, and various biochemical and histological assays were performed. Group × time interactions (p < 0.05) existed for skeletal muscle myosin heavy chain (MHC)-IIa mRNA (AR > PR at POST and DL) and 20S proteasome activity (post-hoc tests revealed no significance in groups over time). Time effects (P < 0.05) existed for total mood disturbance and serum creatine kinase and mechano growth factor mRNA (POST > PRE &D L), VL pressure to pain threshold and MHC-IIx mRNA (PRE&DL > POST), Atrogin-1 and MuRF-1 mRNA (PRE < POST < DL), MHC-I mRNA (PRE < POST & DL), myostatin mRNA (PRE & POST < DL), and mechanistic target of rapamycin (PRE > POST & DL). No interactions or time effects were observed for barbell squat velocity, various hormones, histological metrics, polyubiquitinated proteins, or phosphorylated/pan protein levels of 4E-BP1, p70S6k, and AMPK. One week of AR after a high-volume training block instigates marginal molecular differences in skeletal muscle relative to PR. From a practical standpoint, however, both paradigms elicited largely similar responses.Item Open Access Muscle fiber hypertrophy in response to 6 weeks of high-volume resistance training in trained young men is largely attributed to sarcoplasmic hypertrophy(PLOS ONE) Haun, Cody T; Vann, Christopher G; Osburn, Shelby C; Mumford, Petey W; Roberson, Paul A; Romero, Matthew A; Fox, Carlton D; Johnson, Christopher A; Parry, Hailey A; Kavazis, Andreas N; Moon, Jordan R; Badisa, Veera LD; Mwashote, Benjamin M; Ibeanusi, Victor; Young, Kaelin C; Roberts, Michael DItem Open Access Physiological Differences Between Low Versus High Skeletal Muscle Hypertrophic Responders to Resistance Exercise Training: Current Perspectives and Future Research Directions(Frontiers in Physiology) Roberts, Michael D; Haun, Cody T; Mobley, Christopher B; Mumford, Petey W; Romero, Matthew A; Roberson, Paul A; Vann, Christopher G; McCarthy, John JItem Open Access Pre-training Skeletal Muscle Fiber Size and Predominant Fiber Type Best Predict Hypertrophic Responses to 6 Weeks of Resistance Training in Previously Trained Young Men(Frontiers in Physiology) Haun, Cody T; Vann, Christopher G; Mobley, C Brooks; Osburn, Shelby C; Mumford, Petey W; Roberson, Paul A; Romero, Matthew A; Fox, Carlton D; Parry, Hailey A; Kavazis, Andreas N; Moon, Jordan R; Young, Kaelin C; Roberts, Michael DItem Open Access Protein Supplementation Throughout 10 Weeks of Progressive Run Training Is Not Beneficial for Time Trial Improvement(Frontiers in Nutrition) Roberson, Paul A; Romero, Matthew A; Mumford, Petey W; Osburn, Shelby C; Haun, Cody T; Vann, Christopher G; Kluess, Heidi A; Roberts, Michael DItem Open Access Skeletal muscle LINE-1 ORF1 mRNA is higher in older humans but decreases with endurance exercise and is negatively associated with higher physical activity(Journal of Applied Physiology, 2019-10-01) Roberson, Paul A; Romero, Matthew A; Osburn, Shelby C; Mumford, Petey W; Vann, Christopher G; Fox, Carlton D; McCullough, Danielle J; Brown, Michael D; Roberts, Michael DThe long interspersed nuclear element-1 (L1) is a retrotransposon that constitutes 17% of the human genome and is associated with various diseases and aging. Estimates suggest that ~100 L1 copies are capable of copying and pasting into other regions of the genome. Herein, we examined if skeletal muscle L1 markers are affected by aging or an acute bout of cycling exercise in humans. Apparently healthy younger (23 ± 3 y, n = 15) and older participants (58 ± 8 y, n = 15) donated a vastus lateralis biopsy before 1 h of cycling exercise (PRE) at ~70% of heart rate reserve. Second (2 h) and third (8 h) postexercise muscle biopsies were also obtained. L1 DNA and mRNA expression were quantified using three primer sets [5′ untranslated region (UTR), L1.3, and ORF1]. 5′UTR and L1.3 DNA methylation as well as ORF1 protein expression were also quantified. PRE 5′UTR, ORF1, or L1.3 DNA were not different between age groups ( P > 0.05). ORF1 mRNA was greater in older versus younger participants ( P = 0.014), and cycling lowered this marker at 2 h versus PRE ( P = 0.027). 5′UTR and L1.3 DNA methylation were higher in younger versus older participants ( P < 0.05). Accelerometry data collected during a 2-wk period before the exercise bout indicated higher moderate-to-vigorous physical activity (MVPA) levels per day was associated with lower PRE ORF1 mRNA in all participants ( r = −0.398, P = 0.032). In summary, skeletal muscle ORF1 mRNA is higher in older apparently healthy humans, which may be related to lower DNA methylation patterns. ORF1 mRNA is also reduced with endurance exercise and is negatively associated with higher daily MVPA levels. NEW & NOTEWORTHY The long interspersed nuclear element-1 (L1) gene is highly abundant in the genome and encodes for an autonomous retrotransposon, which is capable of copying and pasting itself into other portions of the genome. This is the first study in humans to demonstrate that certain aspects of skeletal muscle L1 activity are altered with aging. Additionally, this is the first study in humans to demonstrate that L1 ORF1 mRNA levels decrease after a bout of endurance exercise, regardless of age.Item Open Access Skeletal muscle LINE-1 retrotransposon activity is upregulated in older versus younger rats(American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 2019-09-01) Mumford, Petey W; Romero, Matthew A; Osburn, Shelby C; Roberson, Paul A; Vann, Christopher G; Mobley, Christopher B; Brown, Michael D; Kavazis, Andreas N; Young, Kaelin C; Roberts, Michael DLong interspersed element-1 (LINE-1) is a retrotransposon capable of replicating and inserting LINE-1 copies into the genome. Others have reported skeletal muscle LINE-1 markers are higher in older versus younger mice, but data are lacking in other species. Herein, gastrocnemius muscle from male Fischer 344 rats that were 3, 12, and 24 mo old ( n = 9 per group) were analyzed for LINE-1 mRNA, DNA, promoter methylation and DNA accessibility. qPCR primers were designed for active (L1.3) and inactive (L1.Tot) LINE-1 elements as well as part of the ORF1 sequence. L1.3, L1.Tot, and ORF1 mRNAs were higher ( P < 0.05) in 12/24 versus 3-mo-old rats. L1.3 DNA was higher in the 24-mo-old rats versus other groups, and ORF1 DNA was greater in 12/24 versus 3-mo-old rats. ORF1 protein was higher in 12/24 versus 3-mo-old rats. RNA-sequencing indicated mRNAs related to DNA methylation ( Tet1) and histone acetylation ( Hdac2) were lower in 24 versus 3-mo-old rats. L1.3 DNA accessibility was higher in 24-mo-old versus 3-mo-old rats. No age-related differences in nuclear histone deacetylase (HDAC) activity existed, although nuclear DNA methyltransferase (DNMT) activity was lower in 12/24 versus 3-mo-old rats ( P < 0.05). In summary, markers of skeletal muscle LINE-1 activity increase across the age spectrum of rats, and this may be related to deficits in DNMT activity and/or increased LINE-1 DNA accessibility.Item Open Access Skeletal muscle mitochondrial volume and myozenin-1 protein differences exist between high versus low anabolic responders to resistance training(PeerJ) Roberts, Michael D; Romero, Matthew A; Mobley, Christopher B; Mumford, Petey W; Roberson, Paul A; Haun, Cody T; Vann, Christopher G; Osburn, Shelby C; Holmes, Hudson H; Greer, Rory A; Lockwood, Christopher M; Parry, Hailey A; Kavazis, Andreas NBackgroundWe sought to examine how 12 weeks of resistance exercise training (RET) affected skeletal muscle myofibrillar and sarcoplasmic protein levels along with markers of mitochondrial physiology in high versus low anabolic responders.MethodsUntrained college-aged males were classified as anabolic responders in the top 25th percentile (high-response cluster (HI);n= 13, dual x-ray absorptiometry total body muscle mass change (Δ) = +3.1 ± 0.3 kg, Δ vastus lateralis (VL) thickness = +0.59 ± 0.05 cm, Δ muscle fiber cross sectional area = +1,426 ± 253 μm2) and bottom 25th percentile (low-response cluster (LO);n= 12, +1.1 ± 0.2 kg, +0.24 ± 0.07 cm, +5 ± 209 μm2;p< 0.001 for all Δ scores compared to HI). VL muscle prior to (PRE) and following RET (POST) was assayed for myofibrillar and sarcoplasmic protein concentrations, myosin and actin protein content, and markers of mitochondrial volume. Proteins related to myofibril formation, as well as whole lysate PGC1-α protein levels were assessed.ResultsMain effects of cluster (HI > LO,p= 0.018, Cohen’sd= 0.737) and time (PRE > POST,p= 0.037, Cohen’sd= −0.589) were observed for citrate synthase activity, although no significant interaction existed (LO PRE = 1.35 ± 0.07 mM/min/mg protein, LO POST = 1.12 ± 0.06, HI PRE = 1.53 ± 0.11, HI POST = 1.39 ± 0.10). POST myofibrillar myozenin-1 protein levels were up-regulated in the LO cluster (LO PRE = 0.96 ± 0.13 relative expression units, LO POST = 1.25 ± 0.16, HI PRE = 1.00 ± 0.11, HI POST = 0.85 ± 0.12; within-group LO increasep= 0.025, Cohen’sd= 0.691). No interactions or main effects existed for other assayed markers.DiscussionOur data suggest myofibrillar or sarcoplasmic protein concentrations do not differ between HI versus LO anabolic responders prior to or following a 12-week RET program. Greater mitochondrial volume in HI responders may have facilitated greater anabolism, and myofibril myozenin-1 protein levels may represent a biomarker that differentiates anabolic responses to RET. However, mechanistic research validating these hypotheses is needed.Item Open Access Skeletal Muscle Myofibrillar Protein Abundance Is Higher in Resistance-Trained Men, and Aging in the Absence of Training May Have an Opposite Effect(Sports) Vann, Christopher G; Roberson, Paul A; Osburn, Shelby C; Mumford, Petey W; Romero, Matthew A; Fox, Carlton D; Moore, Johnathon H; Haun, Cody; Beck, Darren T; Moon, Jordan R; Kavazis, Andreas N; Young, Kaelin C; Badisa, Veera LD; Mwashote, Benjamin M; Ibeanusi, Victor; Singh, Rakesh K; Roberts, Michael DResistance 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.Item Open Access Soy protein supplementation is not androgenic or estrogenic in college-aged men when combined with resistance exercise training(Scientific Reports) Haun, Cody T; Mobley, C Brooks; Vann, Christopher G; Romero, Matthew A; Roberson, Paul A; Mumford, Petey W; Kephart, Wesley C; Healy, James C; Patel, Romil K; Osburn, Shelby C; Beck, Darren T; Arnold, Robert D; Nie, Ben; Lockwood, Christopher M; Roberts, Michael DAbstractIt is currently unclear as to whether sex hormones are significantly affected by soy or whey protein consumption. Additionally, estrogenic signaling may be potentiated via soy protein supplementation due to the presence of phytoestrogenic isoflavones. Limited evidence suggests that whey protein supplementation may increase androgenic signalling. Therefore, the purpose of this study was to examine the effects of soy protein concentrate (SPC), whey protein concentrate (WPC), or placebo (PLA) supplementation on serum sex hormones, androgen signaling markers in muscle tissue, and estrogen signaling markers in subcutaneous (SQ) adipose tissue of previously untrained, college-aged men (n = 47, 20 ± 1 yrs) that resistance trained for 12 weeks. Fasting serum total testosterone increased pre- to post-training, but more so in subjects consuming WPC (p < 0.05), whereas serum 17β-estradiol remained unaltered. SQ estrogen receptor alpha (ERα) protein expression and hormone-sensitive lipase mRNA increased with training regardless of supplementation. Muscle androgen receptor (AR) mRNA increased while ornithine decarboxylase mRNA (a gene target indicative of androgen signaling) decreased with training regardless of supplementation (p < 0.05). No significant interactions of supplement and time were observed for adipose tissue ERα/β protein levels, muscle tissue AR protein levels, or mRNAs in either tissue indicative of altered estrogenic or androgenic activity. Interestingly, WPC had the largest effect on increasing type II muscle fiber cross sectional area values (Cohen’s d = 1.30), whereas SPC had the largest effect on increasing this metric in type I fibers (Cohen’s d = 0.84). These data suggest that, while isoflavones were detected in SPC, chronic WPC or SPC supplementation did not appreciably affect biomarkers related to muscle androgenic signaling or SQ estrogenic signaling. The noted fiber type-specific responses to WPC and SPC supplementation warrant future research.