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Dietary carbohydrate and protein manipulation and exercise recovery in novice weight-Lifters
Abstract
The influence of nutritional status on recovery from exercise-induced muscle damage is poorly understood. Co-ingestion of carbohydrate with ample protein during the first 6 hours of recovery did not augment protein synthesis. Also acutely increasing carbohydrate intake (48-hrs prior to eccentric exercise) had no recovery effect. The purpose of this study was to evaluate 5-days of a dietary carbohydrate/protein manipulation on markers of exercise-induced muscle damage, soreness, and function as well as markers of whole-body protein metabolism. Subjects were randomly assigned to a low carbohydrate (3.4 g/kg), higher protein diet (1.5 g/kg = LOW) or a high carbohydrate (5.0 g/kg), lower protein diet (1.2 g/kg = HIGH). Both diets exceeded the protein RDA. After eccentric exercise muscle soreness, CK, isometric strength, nitrogen retention, and whole-body protein metabolism were determined. LOW had a greater strength loss and lower CK (p < 0.04) after exercise when compared with HIGH. LOW also had a reduced protein turnover, synthesis, and breakdown during recovery (p < 0.01). These findings indicate that dietary carbohydrate, as opposed to protein, may be a more important nutrient to the novice weight lifter when recovering from eccentric exercise-induced muscle damage.
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The effects of one 45-min bout of high-intensity eccentric exercise (250 W) were studied in four male runners and five untrained men. Plasma creatine kinase (CK) activity in these runners was higher (P less than 0.001) than in the untrained men before exercise and peaked at 207 IU/ml 1 day after exercise, whereas in untrained men the maximum was 2,143 IU/ml 5 days after exercise. Plasma interleukin-1 (IL-1) in the trained men was also higher (P less than 0.001) than in the untrained men before exercise but did not significantly increase after exercise. In the untrained men, IL-1 was significantly elevated 3 h after exercise (P less than 0.001). In the untrained group only, 24-h urines were collected before and after exercise while the men consumed a meat-free diet. Urinary 3-methylhistidine/creatinine in the untrained group rose significantly from 127 mumol/g before exercise to 180 mumol/g 10 days after exercise. The results suggest that in untrained men eccentric exercise leads to a metabolic response indicative of delayed muscle damage. Regularly performed long distance running was associated with chronically elevated plasma IL-1 levels and serum CK activities without acute increases after an eccentric exercise bout.
Whole-body protein synthesis was measured with [15N]glycine in malnourished and recovered infants and in obese patients. Comparisons were made: 1) between results obtained with single (S) and repeated (R) oral dosage of tracer; and 2) between urea and ammonia as end products. In the infants S and R gave similar values for the synthesis rate. With both methods of dosage, the values obtained with NH3 as end product were about two-thirds of those with urea. It is suggested that the cause of this result is that glycine contributes preferentially to the formation of urinary NH3. With NH3 as end product, a collection period of 12 h has been found to be suitable. With urea it is not possible to define an appropriate collection period. The combination of single dose of [15N]glycine with urinary NH3 as end product provides a simple method for measuring whole-body protein synthesis under clinical and field conditions. It can be repeated at short intervals and can give useful comparative information provided that conditions are carefully standardized. The reproducibility so far is +/- 13%.
We determined the effect of the timing of glucose supplementation on fractional muscle protein synthetic rate (FSR), urinary urea excretion, and whole body and myofibrillar protein degradation after resistance exercise. Eight healthy men performed unilateral knee extensor exercise (8 sets/approximately 10 repetitions/approximately 85% of 1 single maximal repetition). They received a carbohydrate (CHO) supplement (1 g/kg) or placebo (Pl) immediately (t = 0 h) and 1 h (t = +1 h) postexercise. FSR was determined for exercised (Ex) and control (Con) limbs by incremental L-[1-13C]leucine enrichment into the vastus lateralis over approximately 10 h postexercise. Insulin was greater (P < 0.01) at 0.5, 0.75, 1.25, 1.5, 1.75, and 2 h, and glucose was greater (P < 0.05) at 0.5 and 0.75 h for CHO compared with Pl condition. FSR was 36.1% greater in the CHO/Ex leg than in the CHO/Con leg (P = not significant) and 6.3% greater in the Pl/Ex leg than in the Pl/Con leg (P = not significant). 3-Methylhistidine excretion was lower in the CHO (110.43 +/- 3.62 mumol/g creatinine) than P1 condition (120.14 +/- 5.82, P < 0.05) as was urinary urea nitrogen (8.60 +/- 0.66 vs. 12.28 +/- 1.84 g/g creatinine, P < 0.05). This suggests that CHO supplementation (1 g/kg) immediately and 1 h after resistance exercise can decrease myofibrillar protein breakdown and urinary urea excretion, resulting in a more positive body protein balance.
Delayed onset muscle soreness (DOMS) occurs after unaccustomed exercise and has been suggested to be attributable to reactive oxygen species (ROS). Previous studies have shown increased ROS after lengthening contractions, attributable to invading phagocytes. Plasma glucose is a vital fuel for phagocytes, therefore carbohydrate (CHO) status before exercise may influence ROS production and DOMS.
To examine the effect of pre-exercise CHO status on DOMS, ROS production, and muscle function after contraction induced muscle damage.
Twelve subjects performed two downhill runs, one after a high CHO diet and one after a low CHO diet. Blood samples were drawn for analysis of malondialdehyde, total glutathione, creatine kinase, non-esterified fatty acids, lactate, glucose, and leucocytes. DOMS and muscle function were assessed daily.
The high CHO diet resulted in higher respiratory exchange ratio and lactate concentrations than the low CHO diet before exercise. The low CHO diet resulted in higher non-esterified fatty acid concentrations before exercise. DOMS developed after exercise and remained for up to 96 hours, after both diets. A biphasic response in creatine kinase occurred after both diets at 24 and 96 hours after exercise. Malondialdehyde had increased 72 hours after exercise after both diets, and muscle function was attenuated up to this time.
Downhill running resulted in increased ROS production and ratings of DOMS and secondary increases in muscle damage. CHO status before exercise had no effect.
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 x kg(-1) x h(-1) protein hydrolysate with 0, 0.15, or 0.6 g x kg(-1) x h(-1) carbohydrate during a 6-h recovery period (PRO, PRO + LCHO, and PRO + HCHO, respectively). Primed, continuous infusions with L-[ring-(13)C(6)]phenylalanine, L-[ring-(2)H(2)]tyrosine, and [6,6-(2)H(2)]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) x l(-1), respectively, P < 0.001). Plasma glucose rate of appearance (R(a)) and disappearance (R(d)) increased over time in PRO + HCHO and PRO + LCHO, but not in PRO. Plasma glucose R(a) and R(d) 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.
This brief review focuses on the time course of changes in muscle function and other correlates of muscle damage following maximal effort eccentric actions of the forearm flexor muscles. Data on 109 subjects are presented to describe an accurate time course of these changes and attempt to establish relationships among the measures. Peak soreness is experienced 2-3 d postexercise while peak swelling occurs 5 d postexercise. Maximal strength and the ability to fully flex the arm show the greatest decrements immediately after exercise with a linear restoration of these functions over the next 10 d. Blood creatine kinase (CK) levels increase precipitously at 2 d after exercise which is also the time when spontaneous muscle shortening is most pronounced. Whether the similarity in the time courses of some of these responses implies that they are caused by similar factors remains to be determined. Performance of one bout of eccentric exercise produces an adaptation such that the muscle is more resistant to damage from a subsequent bout of exercise. The length of the adaptation differs among the measures such that when the exercise regimens are separated by 6 wk, all measures show a reduction in response on the second, compared with the first, bout. After 10 wk, only CK and muscle shortening show a reduction in response. After 6 months only the CK response is reduced. A combination of cellular factors and neurological factors may be involved in the adaptation process.
This study examined exercise-induced muscle damage, repair, and rapid adaptation. Eight college-age women performed three eccentric exercises of the forearm flexors. One arm performed 70 maximal contractions (70-MAX condition), and the other arm performed 24 maximal contractions (24-MAX) followed 2 wk later by 70 maximal contractions (70-MAX2). Criterion measures of serum creatine kinase, muscle soreness and pain, isometric strength, and muscle shortening were assessed before, immediately after, and for 5 days after each exercise. Significant changes in all criterion measures were found after the 70-MAX exercise with a slow recovery that was not complete by day 5 after exercise. The 24-MAX condition showed only small changes in the criterion measures. Changes in the criterion measures after the 70-MAX2 exercise were significantly smaller than those after the 70-MAX exercise. Results from this study, with regard to the ability of the muscle to adapt to exercise-induced damage, suggest that an adaptation takes place such that the muscle is more resistant to damage and any damage that does occur is repaired at a faster rate. It is also clear that a relatively small insult will produce this adaptation.
The purposes of this study were to: 1) determine the time course of changes in serum enzyme activities and muscular soreness following muscular exercise, 2) quantify the relative amounts and importance of intensity and duration of muscular exercise in inducing elevated serum enzyme activities and muscular soreness in untrained individuals, and 3) determine the correlation between magnitude of soreness sensation and level of post-exercise serum enzyme activity. It was determined that the highest serum enzyme activities and muscular soreness sensation occurred 8-24 h and 48 h post-exercise, respectively. Intensity and duration of exercise were varied by adjusting the percent 10-repetition maximum (% 10RM) and number of contractions (NR) performed. Increasing intensity and duration of exercise resulted in corresponding increases in serum enzyme activities and muscular soreness. High-intensity, short-duration exercise (80% 10RM, 170 NR) resulted in greater serum enzyme activities and muscular soreness than long-duration, low-intensity exercise (30% 10RM, 545 NR). Most subjects experiencing high levels of muscular soreness were unable to lift resistances of 90% 1RM, 48 h post-exercise. These findings indicate that a positive relationship exists among exercise performed, serum enzyme activity 24 h post-exercise, and muscular soreness. Increased intensity and duration of exercise produced increased serum enzyme activities and muscular soreness, with intensity having the more pronounced effect.
1. In order to study injury-related changes in muscle stiffness, injury to the elbow flexors of thirteen human subjects was induced by a regimen of eccentric exercise. 2. Passive stiffness over an intermediate range of elbow angles was measured with a device which held the relaxed arm of the subject in the horizontal plane and stepped it through the range of elbow angles from 90 deg to near full extension at 180 deg. The relation between static torque and elbow angle was quite linear over the first 50 deg and was taken as stiffness. 3. Stiffness over this range of angles more than doubled immediately after exercise and remained elevated for about 4 days, and may result from low level myofibrillar activation induced by muscle stretch. 4. Arm swelling was biphasic; arm circumference increased by about 3% immediately after exercise, fell back toward normal, then increased by as much as 9% and remained elevated for as long as 9 days. 5. Ultrasound imaging showed most of the swelling immediately following the exercise to be localized to the flexor muscle compartment; subsequent swelling involved other tissue compartments as well. 6. Muscle strength declined by almost 40% after the exercise and recovery was only slight 10 days later; the half-time of recovery appeared to be as long as 5-6 weeks.
Whole body leucine kinetics was compared in endurance-trained athletes and sedentary controls matched for age, gender, and body weight. Kinetic studies were performed during 3 h of rest, 1 h of exercise (50% maximal oxygen consumption), and 2 h of recovery. When leucine kinetics were expressed both per unit of body weight and per unit of fat-free mass, both groups demonstrated an increase in leucine oxidation during exercise (P < 0.01). Trained athletes had a greater leucine rate of appearance during exercise and recovery compared with their sedentary counterparts (P < 0.05) and an increased leucine oxidation at all times on the basis of body weight (P < 0.05). However, all of these between-group differences were eliminated when leucine kinetics were corrected for fat-free tissue mass. Therefore, correction of leucine kinetics for fat-free mass may be important when cross-sectional investigations on humans are performed. Furthermore, leucine oxidation, when expressed relative to whole-body oxygen consumption during exercise, was similar between groups. It is concluded that there was no difference between endurance-trained and sedentary humans in whole body leucine kinetics during rest, exercise, or recovery when expressed per unit of fat-free tissue mass.
The objective of this investigation was to determine the effects of varying levels of dietary protein on the postexercise increase in serum and muscle enzyme activity normally observed following exercise-induced muscle injury.
Serum creatine kinase (CK), serum aspartate aminotransferase (AST), and muscle glucose-6-phosphate dehydrogenase (G-6-PD) activities were measured in rats fed for 10 d on high (50%), normal (12%), or low (4%) protein diets following a single bout of eccentric exercise (treadmill running at 16 m.min(-1), -16 degrees incline, 90 min).
The exercise intervention resulted in significant increases in serum CK and AST activities in all diet groups. Serum CK demonstrated peak activity immediately postexercise with increases reaching 910+/-94, 594+/-53, and 283+/-52 IU.L(-1) for animals on high, normal, and low protein diets, respectively. Similarly, peak postexercise AST activity for high, normal, and low protein diets reached 193+/-10, 147+/-3, and 162+/-9 IU.L(-1), respectively. The exercise intervention resulted in increases in muscle G-6-PD activity for all diet groups; however, LP rats demonstrated significantly lower values than NP or HP rats.
These data show that dietary protein intake can significantly effect both serum and muscle enzyme activity following acute exercise-induced muscle injury.
Consumption of macronutrients, particularly carbohydrate (CHO) and possibly a small amount of protein, in the early recovery phase after endurance exercise can enhance muscle glycogen resynthesis rates. A target of at least 1.2 g x kg body weight(-1) x h(-1) CHO (over several hours) is suggested. This rate of CHO intake could be sustained with liquid, gel, or solid food rich in CHO for maximizing muscle glycogen. Whether the coingestion of protein with CHO compared with isocaloric CHO results in meaningful differences in glycogen replenishment that translate into subsequent performance enhancement is equivocal. Advantages of added protein with CHO in reducing true muscle damage from endurance exercise remain to be verified. There are, however, no apparent contraindications for using milk or specialty CHO/protein/amino acid products either. Future investigations that examine signaling mechanisms within muscle should be conducted in parallel with translational evidence in humans.
Dietitians of Canada and the American College of Sports Medicine. Position stand: Nutrition and athletic performance
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