Resistance exercise acutely increases MHC and mixed muscle protein synthesis rates in 78–84 and 23–32 yr olds

2000 ◽  
Vol 278 (4) ◽  
pp. E620-E626 ◽  
Author(s):  
Debbie L. Hasten ◽  
Jina Pak-Loduca ◽  
Kathleen A. Obert ◽  
Kevin E. Yarasheski

We determined whether short-term weight-lifting exercise increases the synthesis rate of the major contractile proteins, myosin heavy chain (MHC), actin, and mixed muscle proteins in nonfrail elders and younger women and men. Fractional synthesis rates of mixed, MHC, and actin proteins were determined in seven healthy sedentary 23- to 32-yr-old and seven healthy 78- to 84-yr-old participants in paired studies done before and at the end of a 2-wk weight-lifting program. The in vivo rate of incorporation of 1-[13C]leucine into vastus lateralis MHC, actin, and mixed proteins was determined using a 14-h constant intravenous infusion of 1-[13C]leucine. Before exercise, the mixed and MHC fractional synthetic rates were lower in the older than in the younger participants ( P ≤ 0.04). Baseline actin protein synthesis rates were similar in the two groups ( P = not significant). Over a 2-wk period, participants completed ten 1- to 1.5-h weight-lifting exercise sessions: 2–3 sets per day of 9 exercises, 8–12 repetitions per set, at 60–90% of maximum voluntary muscle strength. At the end of exercise, MHC and mixed protein synthetic rates increased in the younger (88 and 121%) and older participants (105 and 182%; P < 0.001 vs. baseline). These findings indicate that MHC and mixed protein synthesis rates are reduced more than actin in advanced age. Similar to that of 23–32 yr olds, the vastus lateralis muscle in 78–84 yr olds retains the capacity to increase MHC and mixed protein synthesis rates in response to short-term resistance exercise.

2010 ◽  
Vol 298 (2) ◽  
pp. E354-E361 ◽  
Author(s):  
Nicholas A. Burd ◽  
Jared M. Dickinson ◽  
Jennifer K. LeMoine ◽  
Chad C. Carroll ◽  
Bridget E. Sullivan ◽  
...  

Nonselective blockade of the cyclooxygenase (COX) enzymes in skeletal muscle eliminates the normal increase in muscle protein synthesis following resistance exercise. The current study tested the hypothesis that this COX-mediated increase in postexercise muscle protein synthesis is regulated specifically by the COX-2 isoform. Sixteen males (23 ± 1 yr) were randomly assigned to one of two groups that received three doses of either a selective COX-2 inhibitor (celecoxib; 200 mg/dose, 600 mg total) or a placebo in double-blind fashion during the 24 h following a single bout of knee extensor resistance exercise. At rest and 24 h postexercise, skeletal muscle protein fractional synthesis rate (FSR) was measured using a primed constant infusion of [2H5]phenylalanine coupled with muscle biopsies of the vastus lateralis, and measurements were made of mRNA and protein expression of COX-1 and COX-2. Mixed muscle protein FSR in response to exercise ( P < 0.05) was not suppressed by the COX-2 inhibitor (0.056 ± 0.004 to 0.108 ± 0.014%/h) compared with placebo (0.074 ± 0.004 to 0.091 ± 0.005%/h), nor was there any difference ( P > 0.05) between the placebo and COX-2 inhibitor postexercise when controlling for resting FSR. The COX-2 inhibitor did not influence COX-1 mRNA, COX-1 protein, or COX-2 protein levels, whereas it did increase ( P < 0.05) COX-2 mRNA (3.0 ± 0.9-fold) compared with placebo (1.3 ± 0.3-fold). It appears that the elimination of the postexercise muscle protein synthesis response by nonselective COX inhibitors is not solely due to COX-2 isoform blockade. Furthermore, the current data suggest that the COX-1 enzyme is likely the main isoform responsible for the COX-mediated increase in muscle protein synthesis following resistance exercise in humans.


1999 ◽  
Vol 277 (1) ◽  
pp. E118-E125 ◽  
Author(s):  
Kevin E. Yarasheski ◽  
Jina Pak-Loduca ◽  
Debbie L. Hasten ◽  
Kathleen A. Obert ◽  
Mary Beth Brown ◽  
...  

Muscle atrophy (sarcopenia) in the elderly is associated with a reduced rate of muscle protein synthesis. The purpose of this study was to determine if weight-lifting exercise increases the rate of muscle protein synthesis in physically frail 76- to 92-yr-old women and men. Eight women and 4 men with mild to moderate physical frailty were enrolled in a 3-mo physical therapy program that was followed by 3 mo of supervised weight-lifting exercise. Supervised weight-lifting exercise was performed 3 days/wk at 65–100% of initial 1-repetition maximum on five upper and three lower body exercises. Compared with before resistance training, the in vivo incorporation rate of [13C]leucine into vastus lateralis muscle protein was increased after resistance training in women and men ( P < 0.01), although it was unchanged in five 82 ± 2-yr-old control subjects studied two times in 3 mo. Maximum voluntary knee extensor muscle torque production increased in the supervised resistance exercise group. These findings suggest that muscle contractile protein synthetic pathways in physically frail 76- to 92-yr-old women and men respond and adapt to the increased contractile activity associated with progressive resistance exercise training.


2012 ◽  
Vol 113 (1) ◽  
pp. 71-77 ◽  
Author(s):  
Cameron J. Mitchell ◽  
Tyler A. Churchward-Venne ◽  
Daniel W. D. West ◽  
Nicholas A. Burd ◽  
Leigh Breen ◽  
...  

We have reported that the acute postexercise increases in muscle protein synthesis rates, with differing nutritional support, are predictive of longer-term training-induced muscle hypertrophy. Here, we aimed to test whether the same was true with acute exercise-mediated changes in muscle protein synthesis. Eighteen men (21 ± 1 yr, 22.6 ± 2.1 kg/m2; means ± SE) had their legs randomly assigned to two of three training conditions that differed in contraction intensity [% of maximal strength (1 repetition maximum)] or contraction volume (1 or 3 sets of repetitions): 30%-3, 80%-1, and 80%-3. Subjects trained each leg with their assigned regime for a period of 10 wk, 3 times/wk. We made pre- and posttraining measures of strength, muscle volume by magnetic resonance (MR) scans, as well as pre- and posttraining biopsies of the vastus lateralis, and a single postexercise (1 h) biopsy following the first bout of exercise, to measure signaling proteins. Training-induced increases in MR-measured muscle volume were significant ( P < 0.01), with no difference between groups: 30%-3 = 6.8 ± 1.8%, 80%-1 = 3.2 ± 0.8%, and 80%-3= 7.2 ± 1.9%, P = 0.18. Isotonic maximal strength gains were not different between 80%-1 and 80%-3, but were greater than 30%-3 ( P = 0.04), whereas training-induced isometric strength gains were significant but not different between conditions ( P = 0.92). Biopsies taken 1 h following the initial resistance exercise bout showed increased phosphorylation ( P < 0.05) of p70S6K only in the 80%-1 and 80%-3 conditions. There was no correlation between phosphorylation of any signaling protein and hypertrophy. In accordance with our previous acute measurements of muscle protein synthetic rates a lower load lifted to failure resulted in similar hypertrophy as a heavy load lifted to failure.


2004 ◽  
Vol 14 (3) ◽  
pp. 255-271 ◽  
Author(s):  
Elisabet Børsheim ◽  
Asle Aarsland ◽  
Robert R. Wolfe

This study tests the hypotheses that (a) a mixture of whey protein, amino acids (AA), and carbohydrates (CHO) stimulates net muscle protein synthesis to a greater extent than isoenergetic CHO alone after resistance exercise; and (b) that the stimulatory effect of a protein, AA, and CHO mixture will last beyond the 1 st hour after intake. Eight subjects participated in 2 trials. In one (PAAC), they ingested 77.4 g CHO, 17.5 g whey protein, and 4.9 g AA 1 hr after resistance exercise. In the other (CON), 100 g CHO was ingested instead. They received a primed constant infusion of L-[2H5]-phenylalanine, and samples from femoral artery and vein, and biopsies from vastus lateralis were obtained. The area under the curve for net uptake of phenylalanine into muscle above pre-drink value was 128 ±42 mg • leg-1 (PAAC) versus 32 ± 10 mg - leg-1 (CON) for the 3 hr after the drink (p = .04). The net protein balance response to the mixture consisted of two components, one rapid immediate response, and a smaller delayed response about 90 min after drink, whereas in CON only a small delayed response was seen. We conclude that after resistance exercise, a mixture of whey protein, AA, and CHO stimulated muscle protein synthesis to a greater extent than isoenergetic CHO alone. Further, compared to previously reported findings, the addition of protein to an AA + CHO mixture seems to extend the anabolic effect.


1992 ◽  
Vol 262 (3) ◽  
pp. E261-E267 ◽  
Author(s):  
K. E. Yarasheski ◽  
J. A. Campbell ◽  
K. Smith ◽  
M. J. Rennie ◽  
J. O. Holloszy ◽  
...  

The purpose of this study was to determine whether growth hormone (GH) administration enhances the muscle anabolism associated with heavy-resistance exercise. Sixteen men (21-34 yr) were assigned randomly to a resistance training plus GH group (n = 7) or to a resistance training plus placebo group (n = 9). For 12 wk, both groups trained all major muscle groups in an identical fashion while receiving 40 micrograms recombinant human GH.kg-1.day-1 or placebo. Fat-free mass (FFM) and total body water increased (P less than 0.05) in both groups but more (P less than 0.01) in the GH recipients. Whole body protein synthesis rate increased more (P less than 0.03), and whole body protein balance was greater (P = 0.01) in the GH-treated group, but quadriceps muscle protein synthesis rate, torso and limb circumferences, and muscle strength did not increase more in the GH-treated group. In the young men studied, resistance exercise with or without GH resulted in similar increments in muscle size, strength, and muscle protein synthesis, indicating that 1) the larger increase in FFM with GH treatment was probably due to an increase in lean tissue other than skeletal muscle and 2) resistance training supplemented with GH did not further enhance muscle anabolism and function.


2006 ◽  
Vol 291 (2) ◽  
pp. E381-E387 ◽  
Author(s):  
Christos S. Katsanos ◽  
Hisamine Kobayashi ◽  
Melinda Sheffield-Moore ◽  
Asle Aarsland ◽  
Robert R. Wolfe

This study was designed to evaluate the effects of enriching an essential amino acid (EAA) mixture with leucine on muscle protein metabolism in elderly and young individuals. Four (2 elderly and 2 young) groups were studied before and after ingestion of 6.7 g of EAAs. EAAs were based on the composition of whey protein [26% leucine (26% Leu)] or were enriched in leucine [41% leucine (41% Leu)]. A primed, continuous infusion of l-[ ring-2H5]phenylalanine was used together with vastus lateralis muscle biopsies and leg arteriovenous blood samples for the determinations of fractional synthetic rate (FSR) and balance of muscle protein. FSR increased following amino acid ingestion in both the 26% (basal: 0.048 ± 0.005%/h; post-EAA: 0.063 ± 0.007%/h) and the 41% (basal: 0.036 ± 0.004%/h; post-EAA: 0.051 ± 0.007%/h) Leu young groups ( P < 0.05). In contrast, in the elderly, FSR did not increase following ingestion of 26% Leu EAA (basal: 0.044 ± 0.003%/h; post-EAA: 0.049 ± 0.006%/h; P > 0.05) but did increase following ingestion of 41% Leu EAA (basal: 0.038 ± 0.007%/h; post-EAA: 0.056 ± 0.008%/h; P < 0.05). Similar to the FSR responses, the mean response of muscle phenylalanine net balance, a reflection of muscle protein balance, was improved ( P < 0.05) in all groups, with the exception of the 26% Leu elderly group. We conclude that increasing the proportion of leucine in a mixture of EAA can reverse an attenuated response of muscle protein synthesis in elderly but does not result in further stimulation of muscle protein synthesis in young subjects.


2011 ◽  
Vol 43 (9) ◽  
pp. 1635-1642 ◽  
Author(s):  
CARL J. HULSTON ◽  
EMIL WOLSK ◽  
THOMAS S. GRØNDAHL ◽  
CHRISTINA YFANTI ◽  
GERRIT VAN HALL

2007 ◽  
Vol 293 (3) ◽  
pp. E833-E842 ◽  
Author(s):  
René Koopman ◽  
Milou Beelen ◽  
Trent Stellingwerff ◽  
Bart Pennings ◽  
Wim H. M. Saris ◽  
...  

The present study was designed to assess the impact of coingestion of various amounts of carbohydrate combined with an ample amount of protein intake on postexercise muscle protein synthesis rates. Ten healthy, fit men (20 ± 0.3 yr) were randomly assigned to three crossover experiments. After 60 min of resistance exercise, subjects consumed 0.3 g·kg−1·h−1 protein hydrolysate with 0, 0.15, or 0.6 g·kg−1·h−1 carbohydrate during a 6-h recovery period (PRO, PRO + LCHO, and PRO + HCHO, respectively). Primed, continuous infusions with l-[ ring-13C6]phenylalanine, l-[ ring-2H2]tyrosine, and [6,6-2H2]glucose were applied, and blood and muscle samples were collected to assess whole body protein turnover and glucose kinetics as well as protein fractional synthesis rate (FSR) in the vastus lateralis muscle over 6 h of postexercise recovery. Plasma insulin responses were significantly greater in PRO + HCHO compared with PRO + LCHO and PRO (18.4 ± 2.9 vs. 3.7 ± 0.5 and 1.5 ± 0.2 U·6 h−1·l−1, respectively, P < 0.001). Plasma glucose rate of appearance (Ra) and disappearance (Rd) increased over time in PRO + HCHO and PRO + LCHO, but not in PRO. Plasma glucose Ra and Rd were substantially greater in PRO + HCHO vs. both PRO and PRO + LCHO ( P < 0.01). Whole body protein breakdown, synthesis, and oxidation rates, as well as whole body protein balance, did not differ between experiments. Mixed muscle protein FSR did not differ between treatments and averaged 0.10 ± 0.01, 0.10 ± 0.01, and 0.11 ± 0.01%/h in the PRO, PRO + LCHO, and PRO + HCHO experiments, respectively. In conclusion, coingestion of carbohydrate during recovery does not further stimulate postexercise muscle protein synthesis when ample protein is ingested.


1993 ◽  
Vol 265 (2) ◽  
pp. E210-E214 ◽  
Author(s):  
K. E. Yarasheski ◽  
J. J. Zachwieja ◽  
D. M. Bier

Muscle mass and function are improved in the elderly during resistance exercise training. These improvements must result from alterations in the rates of muscle protein synthesis and breakdown. We determined the rate of quadriceps muscle protein synthesis using the in vivo rate of incorporation of intravenously infused [13C]leucine into mixed-muscle protein in both young (24 yr) and elderly (63-66 yr) men and women before and at the end of 2 wk of resistance exercise training. Before training, the fractional rate of muscle protein synthesis was lower in the elderly than in the young (0.030 +/- 0.003 vs. 0.049 +/- 0.004%/h; P = 0.004) but increased (P < 0.03) to a comparable rate of muscle protein synthesis in both young (0.075 +/- 0.009%/h) and elderly subjects (0.076 +/- 0.011%/h) after 2 wk of exercise. In the elderly, muscle mass, 24-h urinary 3-methylhistidine and creatinine excretion, and whole body protein breakdown rate determined during the [13C]leucine infusion were not changed after 2 wk of exercise. These findings demonstrate that, during the initial phase of a resistance exercise training program, a marked increase in quadriceps muscle protein synthesis rate occurs in elderly and young adults without an increase in the rate of whole body protein breakdown. In the elderly, this was not accompanied by an increase in urinary 3-methylhistidine excretion, an index of myofibrillar protein breakdown.


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