scholarly journals Amino Acid-Carbohydrate Intake Combined with Multiple Bouts of Resistance Exercise Increases Resting Energy Expenditure

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Kyle J. Hackney ◽  
Andrew R. Kelleher ◽  
Lori L. Ploutz-Snyder

Increasing the rate of muscle protein synthesis is an energy consuming process that explains the acute elevations in resting energy expenditure (REE) observed 12 to 72 hours after a resistance exercise session. We hypothesized that multiple sessions of resistance exercise combined with the intake of amino acids would increase REE and alter the nonprotein respiratory exchange ratio (RER). Ten male participants completed two separate seven-day trials where REE and RER were measured on each morning via indirect calorimetry. On four consecutive days within each seven-day trial, acute resistance exercise was performed, and nutritional intake was manipulated by providing (1) amino acids and carbohydrate (AA-RT) or (2) nonnitrogenous, isoenergetic carbohydrate (CHO-RT) before and during each resistance exercise session. Average REE within the training period was 3.61% greater in AA-RT (7897 ± 252 kJ) compared to CHO-RT (7622 ± 289 kJ; P=0.02). RER declined (P<0.0001) from baseline after each resistance exercise was initiated in both AA-RT (0.82 ± 0.01 to 0.77 ± 0.01) and CHO-RT (0.82 ± 0.02 to 0.77 ± 0.02). We conclude the provision of amino acids with multiple bouts of resistance exercise enhances energy expenditure at rest without altering the utilization of lipid.

2000 ◽  
Vol 11 (11) ◽  
pp. 2106-2113
Author(s):  
GIACOMO GARIBOTTO ◽  
ANTONINA BARRECA ◽  
ANTONELLA SOFIA ◽  
RODOLFO RUSSO ◽  
FULVIO FIORINI ◽  
...  

Abstract. The relationships among growth hormone (GH), leptin, and resting energy expenditure (REE) are not understood. It has been reported that in malnourished hemodialysis patients, GH increases muscle protein synthesis, a process that requires energy. The present study evaluated the arterial levels and the forearm exchange of leptin, as well as the REE of the same patients during their participation in the same study, in four sequential 6-wk periods: I, baseline; II, GH treatment; III, washout; and IV, GH + intradialytic parenteral nutrition. During periods II and IV, patients received GH (5 mg three times per week). REE rose by 5% in period II, declined during period III, and rose by 7% during period IV. Basal leptin levels were low (2.0 ± 0.19 ng/L). Insulin and leptin levels, as well as leptin release from the forearm, were unchanged during periods I through III but rose (+ 36%; P < 0.05) during period IV. Changes in arterial leptin were directly related to changes in forearm leptin release (P < 0.002), indicating a role of leptin production by peripheral tissues on leptinemia. Changes in leptin release were directly related to insulin (P < 0.001) and, less consistently, to insulin-like growth factor-binding protein-1 levels (P < 0.02). Similarly, variations in leptin levels were directly related to insulin (P < 0.01). Variations in REE were not related to variations in leptin or insulin levels but to changes in muscle protein synthesis (P < 0.025). The data show that in malnourished hemodialysis patients, treatment with GH is not invariably associated with an increase in leptin production. An increase in leptin release by peripheral tissues and leptin levels occurs only in the setting of hyperinsulinemia. The increase in REE that is induced by treatment with GH is not dependent on changes in leptin but is largely accounted for by the energy cost of the stimulation of muscle protein synthesis.


Diabetes Care ◽  
2009 ◽  
Vol 32 (12) ◽  
pp. 2161-2167 ◽  
Author(s):  
I. G. Fatouros ◽  
A. Chatzinikolaou ◽  
S. Tournis ◽  
M. G. Nikolaidis ◽  
A. Z. Jamurtas ◽  
...  

2008 ◽  
Vol 44 ◽  
pp. 85-98 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando

Muscle mass is critical for athletic performance and, perhaps more importantly for most, health and survival. The metabolic basis for a change in muscle mass is an increase in net muscle protein balance (termed NBAL). NBAL is the difference between MPS (muscle protein synthesis) and MPB (muscle protein breakdown). Thus an increase in MPS and/or a decrease in MPB are necessary for NBAL to increase, leading to accretion of muscle proteins. In particular, accretion of myofibrillar proteins is necessary. NBAL responds to exercise, feeding and other factors. In healthy, weight-stable adults, muscle mass remains constant because periods of positive balance following feeding are countered by periods of negative balance during fasting. A combination of resistance exercise and nutrition is a potent anabolic stimulus through stimulation of MPS from amino acids and attenuation of MPB by carbohydrates. Increased muscle mass results from the accumulation of small amounts of protein in response to each bout of exercise combined with nutrient intake. The magnitude of the response may be influenced by factors other than just the amount of a nutrient ingested. Timing of ingestion, co-ingestion of nutrients and the type of protein may all influence protein accretion. Testosterone is a potent anabolic stimulus primarily through improvement in re-utilization of amino acids from MPB. There is a general lack of efficacy in studies assessing the potential for growth hormone, androstenedione and dehydroepiandrostenedione to increase muscle mass. Creatine supplementation is clearly an effective means to increase muscle mass, especially in combination with resistance exercise, however the mechanisms remain unclear. Results from acute metabolic studies provide useful information for estimation of the efficacy of anabolic agents.


Obesity ◽  
2006 ◽  
Vol 14 (11) ◽  
pp. 2018-2025 ◽  
Author(s):  
Gary R. Hunter ◽  
Nuala M. Byrne ◽  
Barbara A. Gower ◽  
Bovorn Sirikul ◽  
Andrew P. Hills

1999 ◽  
Vol 276 (4) ◽  
pp. E628-E634 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando ◽  
Stuart M. Phillips ◽  
David Doyle ◽  
Robert R. Wolfe

We examined the response of net muscle protein synthesis to ingestion of amino acids after a bout of resistance exercise. A primed, constant infusion ofl-[ ring-2H5]phenylalanine was used to measure net muscle protein balance in three male and three female volunteers on three occasions. Subjects consumed in random order 1 liter of 1) a mixed amino acid (40 g) solution (MAA), 2) an essential amino acid (40 g) solution (EAA), and 3) a placebo solution (PLA). Arterial amino acid concentrations increased ∼150–640% above baseline during ingestion of MAA and EAA. Net muscle protein balance was significantly increased from negative during PLA ingestion (−50 ± 23 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) to positive during MAA ingestion (17 ± 13 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) and EAA (29 ± 14 nmol ⋅ min−1 ⋅ 100 ml leg volume−1; P < 0.05). Because net balance was similar for MAA and EAA, it does not appear necessary to include nonessential amino acids in a formulation designed to elicit an anabolic response from muscle after exercise. We concluded that ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused.


Circulation ◽  
2020 ◽  
Vol 142 (Suppl_3) ◽  
Author(s):  
Yoko Kudo-sakamoto ◽  
Tomohito Ohtani ◽  
kei nakamoto ◽  
Fusako Sera ◽  
Shungo Hikoso ◽  
...  

Introduction: Cachexia is a critical issue in patients with refractory heart failure (HF). Although the elevation of resting energy expenditure (REE) can progress cachexia through relatively insufficient calorie intake, the detail of REE in HF patients remains uncertain and no useful marker for predicting insufficient calorie intake has been established. This study aimed to assess the REE of HF patients and to evaluate the detectability of serum and urine laboratory markers for insufficient calorie intake. Methods: We measured REE using indirect calorimetry in 69 HF patients (NYHA class II-IV) in our hospital. In 25 out of 69 patients, serum albumin, amino acids, and 24-hour urine amino acids were measured. The calorie intake insufficiency was determined based on measured REE multiplied by activity index Results: As compared to the predicted values by Harris-Benedict equation, 43 patients (63%) had an elevated REE and the mean REE was approximately 4% elevated. There was no significant correlation between the REE and parameters indicating HF severity, including cardiac index on right heart catheterization and BNP level. Only body mass index (BMI) negatively correlated with the REE (r=-0,66, p<0.01). Of 25 patients, 16 (64%) had calorie intake insufficiency. The excreted amount of urine essential amino acids was lower and mostly under normal range, especially significantly decreased in Histidine and Phenylalanine levels in the patients with calorie intake insufficiency compared to those without calorie intake insufficiency, whereas serum levels of albumin and essential amino acids were kept within a normal range in the both. Conclusions: Our findings suggest that the patients with refractory HF, especially having low BMI, are likely to be under inadequate calorie intake due to elevated REE. The calorie intake insufficiency could not be identified with serum levels of albumin nor essential amino acids. Instead, urine essential amino acids would decrease first prior to plasma levels, indicating this measurement would be a useful marker to detect calorie intake insufficiency.


2009 ◽  
Vol 106 (4) ◽  
pp. 1374-1384 ◽  
Author(s):  
Micah J. Drummond ◽  
Hans C. Dreyer ◽  
Christopher S. Fry ◽  
Erin L. Glynn ◽  
Blake B. Rasmussen

In this review we discuss current findings in the human skeletal muscle literature describing the acute influence of nutrients (leucine-enriched essential amino acids in particular) and resistance exercise on muscle protein synthesis and mammalian target of rapamycin complex 1 (mTORC1) signaling. We show that essential amino acids and an acute bout of resistance exercise independently stimulate human skeletal muscle protein synthesis. It also appears that ingestion of essential amino acids following resistance exercise leads to an even larger increase in the rate of muscle protein synthesis compared with the independent effects of nutrients or muscle contraction. Until recently the cellular mechanisms responsible for controlling the rate of muscle protein synthesis in humans were unknown. In this review, we highlight new studies in humans that have clearly shown the mTORC1 signaling pathway is playing an important regulatory role in controlling muscle protein synthesis in response to nutrients and/or muscle contraction. We propose that essential amino acid ingestion shortly following a bout of resistance exercise is beneficial in promoting skeletal muscle growth and may be useful in counteracting muscle wasting in a variety of conditions such as aging, cancer cachexia, physical inactivity, and perhaps during rehabilitation following trauma or surgery.


2002 ◽  
Vol 283 (4) ◽  
pp. E648-E657 ◽  
Author(s):  
Elisabet Børsheim ◽  
Kevin D. Tipton ◽  
Steven E. Wolf ◽  
Robert R. Wolfe

This study tests the hypothesis that a dose of 6 g of orally administered essential amino acids (EAAs) stimulates net muscle protein balance in healthy volunteers when consumed 1 and 2 h after resistance exercise. Subjects received a primed constant infusion ofl-[2H5]phenylalanine andl-[1-13C]leucine. Samples from femoral artery and vein and biopsies from vastus lateralis were obtained. Arterial EAA concentrations increased severalfold after drinks. Net muscle protein balance (NB) increased proportionally more than arterial AA concentrations in response to drinks, and it returned rapidly to basal values when AA concentrations decreased. Area under the curve for net phenylalanine uptake above basal value was similar for the first hour after each drink (67 ± 17 vs. 77 ± 20 mg/leg, respectively). Because the NB response was double the response to two doses of a mixture of 3 g of EAA + 3 g of nonessential AA (NEAA) (14), we conclude that NEAA are not necessary for stimulation of NB and that there is a dose-dependent effect of EAA ingestion on muscle protein synthesis.


2008 ◽  
Vol 104 (5) ◽  
pp. 1452-1461 ◽  
Author(s):  
Micah J. Drummond ◽  
Hans C. Dreyer ◽  
Bart Pennings ◽  
Christopher S. Fry ◽  
Shaheen Dhanani ◽  
...  

Skeletal muscle loss during aging leads to an increased risk of falls, fractures, and eventually loss of independence. Resistance exercise is a useful intervention to prevent sarcopenia; however, the muscle protein synthesis (MPS) response to resistance exercise is less in elderly compared with young subjects. On the other hand, essential amino acids (EAA) increase MPS equally in both young and old subjects when sufficient EAA is ingested. We hypothesized that EAA ingestion following a bout of resistance exercise would stimulate anabolic signaling and MPS similarly between young and old men. Each subject ingested 20 g of EAA 1 h following leg resistance exercise. Muscle biopsies were obtained before and 1, 3, and 6 h after exercise to measure the rate of MPS and signaling pathways that regulate translation initiation. MPS increased early in young (1–3 h postexercise) and later in old (3–6 h postexercise). At 1 h postexercise, ERK1/2 MNK1 phosphorylation increased and eIF2α phosphorylation decreased only in the young. mTOR signaling (mTOR, S6K1, 4E-BP1, eEF2) was similar between groups at all time points, but MNK1 phosphorylation was lower at 3 h and AMP-activated protein kinase-α (AMPKα) phosphorylation was higher in old 1–3 h postexercise. We conclude that the acute MPS response after resistance exercise and EAA ingestion is similar between young and old men; however, the response is delayed with aging. Unresponsive ERK1/2 signaling and AMPK activation in old muscle may be playing a role in the delayed activation of MPS. Notwithstanding, the combination of resistance exercise and EAA ingestion should be a useful strategy to combat sarcopenia.


2000 ◽  
Vol 88 (2) ◽  
pp. 386-392 ◽  
Author(s):  
Blake B. Rasmussen ◽  
Kevin D. Tipton ◽  
Sharon L. Miller ◽  
Steven E. Wolf ◽  
Robert R. Wolfe

This study was designed to determine the response of muscle protein to the bolus ingestion of a drink containing essential amino acids and carbohydrate after resistance exercise. Six subjects (3 men, 3 women) randomly consumed a treatment drink (6 g essential amino acids, 35 g sucrose) or a flavored placebo drink 1 h or 3 h after a bout of resistance exercise on two separate occasions. We used a three-compartment model for determination of leg muscle protein kinetics. The model involves the infusion of ring-2H5-phenylalanine, femoral arterial and venous blood sampling, and muscle biopsies. Phenylalanine net balance and muscle protein synthesis were significantly increased above the predrink and corresponding placebo value ( P < 0.05) when the drink was taken 1 or 3 h after exercise but not when the placebo was ingested at 1 or 3 h. The response to the amino acid-carbohydrate drink produced similar anabolic responses at 1 and 3 h. Muscle protein breakdown did not change in response to the drink. We conclude that essential amino acids with carbohydrates stimulate muscle protein anabolism by increasing muscle protein synthesis when ingested 1 or 3 h after resistance exercise.


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