The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans
Abstract
The rates of protein synthesis and degradation and of amino acid transport were determined in the leg muscle of untrained postabsorptive normal volunteers at rest and approximately 3 h after a resistance exercise routine. The methodology involved use of stable isotopic tracers of amino acids, arteriovenous catheterization of the femoral vessels, and biopsy of the vastus lateralis muscle. During postexercise recovery, the rate of intramuscular phenylalanine utilization for protein synthesis increased above the basal value by 108 +/- 18%, whereas the rate of release from proteolysis increased by 51 +/- 17%. Muscle protein balance improved (P < 0.05) after exercise but did not become positive (from -15 +/- 12 to -6 +/- 3 nmol phenylalanine.min-1.100 ml leg volume-1). After exercise, rates of inward transport of leucine, lysine, and alanine increased (P < 0.05) above the basal state from 132 +/- 16 to 208 +/- 29, from 122 +/- 8 to 260 +/- 8, and from 384 +/- 71 to 602 +/- 89 nmol.min-1.100 ml leg-1, respectively. Transport of phenylalanine did not change significantly. These results indicate that, during recovery after resistance exercise, muscle protein turnover is increased because of an acceleration of synthesis and degradation. A postexercise acceleration of amino acid transport may contribute to the relatively greater stimulation of protein synthesis.
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“In the absence of feeding, muscle protein balance remains negative in response to an acute bout of resistance exercise [48].”
From International Society of Sports Nutrition Position Stand: protein and exercise (2017) · cites this paper as [48]
In the citing paper
“In the hours after resistance exercise there is also an increase in the rate of amino acid uptake from the blood into the muscle.”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [15]
In the citing paper
“Specifically, leucine and glutamine are increased within the working muscle [9, 15].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [15]
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“Recently, the importance of blood flow for increasing muscle protein synthesis has been demonstrated (12).”
BackgroundHormonal Responses and Adaptations to Resistance Exercise and Training
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Self-citationNutrition and Athletic Performance
(2009) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31890eb86 · Cited by 1,084
“Although earlier investigations in this area involved supplementation with individual amino acids (37,38), more recent work has shown that intact high-quality proteins such as whey, casein, or soy are effectively used for the maintenance, repair, and synthesis of skeletal muscle proteins in…”
Tang, J. E., Moore, D. R., Kujbida, G. W., Tarnopolsky, M. A., & Phillips, S. M. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00076.2009 · Cited by 998
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International Society of Sports Nutrition Position Stand: protein and exercise
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“In the absence of feeding, muscle protein balance remains negative in response to an acute bout of resistance exercise [48].”
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An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein
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“(Chesley et al. 1992; Biolo et al. 1995; Phillips et al. 1997; Miller et al. 2005; Dreyer et al. 2006; Drummond et al. 2008; Wilkinson et al. 2008).”
Mountjoy, M., Ackerman, K. E., Bailey, D. M., Burke, L. M., Constantini, N., Hackney, A. C., Heikura, I. A., Melin, A., Pensgaard, A. M., Stellingwerff, T., et al. (2023) · British Journal of Sports Medicine · doi:10.1136/bjsports-2023-106994 · Cited by 724
International Society of Sports Nutrition position stand: protein and exercise
Campbell, B., Kreider, R. B., Ziegenfuss, T., La Bounty, P., Roberts, M., Burke, D., Landis, J., Lopez, H., & Antonio, J. (2007) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-4-8 · Cited by 716
“Protein timing It is generally recognized that active individuals require more dietary protein due to an increase in intramuscular protein oxidation [39] and protein breakdown [40] that occurs during exercise, as well as the need to further complement intramuscular protein resynthesis and attenuate proteolytic mechani…”
From space to Earth: Advances in human physiology from 20 years of bed rest studies (1986–2006)
Pavy-Le Traon, A., Heer, M., Narici, M. V., Rittweger, J., & Vernikos, J. (2007) · European Journal of Applied Physiology · doi:10.1007/s00421-007-0474-z · Cited by 658
“Hyperinsulinemia caused by insulin infusion—while holding blood amino acid concentrations normal—leads to increased rates of muscle protein synthesis without changing protein breakdown in muscle in ambulatory healthy volunteers (Biolo et al. 1995a, 1999).”
BackgroundReversal of Catabolism by Beta-Blockade after Severe Burns
Herndon, D. N., Hart, D. W., Wolf, S. E., Chinkes, D. L., & Wolfe, R. R. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa010342 · Cited by 638
Self-citationWilkinson, S. B., Phillips, S. M., Atherton, P. J., Patel, R., Yarasheski, K. E., Tarnopolsky, M. A., & Rennie, M. J. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.153916 · Cited by 628
“…muscle protein synthesis (MPS), an average measure of all muscle proteins, is stimulated by resistance (Chesley et al. 1992; Yarasheski et al. 1993; Biolo et al. 1995; MacDougall et al. 1995; Phillips et al. 1997) and endurance (Carraro et al. 1990; Sheffield-Moore et al. 2004) exercise, but the…”
BackgroundPostexercise net protein synthesis in human muscle from orally administered amino acids
Tipton, K. D., Ferrando, A. A., Phillips, S. M., Doyle, D., & Wolfe, R. R. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.276.4.e628 · Cited by 616
Self-citationDreyer, H. C., Fujita, S., Cadenas, J. G., Chinkes, D. L., Volpi, E., & Rasmussen, B. B. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.113175 · Cited by 570
“In fact, an acute bout of resistance exercise results in an increase in muscle protein synthesis within 2–3 h, and remains elevated for 24–48 h post-exercise (Biolo et al. 1995; MacDougall et al. 1995; Phillips et al. 1997).”
BackgroundPersistence of muscle catabolism after severe burn
Hart, D. W., Wolf, S. E., Mlcak, R. P., Chinkes, D. L., Ramzy, P. I., Obeng, M. K., Ferrando, A. A., Wolfe, R. R., & Herndon, D. N. (2000) · Surgery · doi:10.1067/msy.2000.108059 · Cited by 551
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“Moreover, since the amino acid delivery is dependent on blood flow (Biolo et al. 1995), the intracellular amino acid availability in the exercised muscle may have been larger in P0 than in P2, hence favouring an increased anabolic response in P0 as it correlates with intracellular amino acid…”
BackgroundInfluentialWilkinson, S. B., Tarnopolsky, M. A., MacDonald, M. J., MacDonald, J. R., Armstrong, D., & Phillips, S. M. (2007) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/85.4.1031 · Cited by 530
“The result is thatourestimates of Ra, and Rd are lower than those previously reported (3, 8, 28, 33); the differences between our studies and others appear to be due, for the most part, to a lower blood flow.”
ResultTipton, K. D., Rasmussen, B. B., Miller, S. L., Wolf, S. E., Owens-Stovall, S. K., Petrini, B. E., & Wolfe, R. R. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.2.e197 · Cited by 526
“To determine the enrichment of infused amino acids in whole blood, the tert-butyldimethylsilyl (t-BDMS) derivative of each amino acid was made according to previously described procedures (5, 18, 19).”
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“Resistance exercise also stimulates muscle protein synthesis, but muscle protein breakdown is also elevated so that, although net nitrogen balance increases, this balance remains negative (4).”
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Areta, J. L., Burke, L. M., Ross, M. L., Camera, D. M., West, D. W. D., Broad, E. M., Jeacocke, N. A., Moore, D. R., Stellingwerff, T., Phillips, S. M., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2012.244897 · Cited by 495
“…intervention but the additive effect of protein ingestion on the anabolic response following resistance exercise is well established and rates of MPS would be superior compared with resistance exercise in isolation regardless of the ingestion protocol (Biolo et al. 1995, 1997; Moore et al. 2009a).”
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“Studies have also shown that synthesis rates of mixed muscle proteins increase 3–4 h after resistance exercise (18).”
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Essential amino acids and muscle protein recovery from resistance exercise
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“Although earlier nvestigations in this area involved e upplementation with individual mino acids (37,38) more recent work as shown that intact, high-quality roteins such as whey, casein, or soy re effectively used for the mainteance, repair, and synthesis of skeleal muscle proteins in response to raining (39).”
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“Kinetic studies have demonstrated an impairment in the amino acid transport systems and increased shunting of blood away from the muscles [20].”
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Coyle, E. F. (2004) · Journal of Sports Sciences · doi:10.1080/0264041031000140545 · Cited by 423
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Muscle protein synthesis in response to nutrition and exercise
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“This is exemplified by the fact that acute increases in MPS after exercise in the absence of EAA nutrition provide a more prolonged rise in MPB such that the net effect is negative muscle protein balance (Biolo et al. 1995).”
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“In response to this signal, it appears that both protein synthesis and degradative rates increase, but synthetic rates increase disproportionally, resulting in muscle cell hypertrophy (Biolo et al., 1995; Tipton and Wolfe, 1998).”
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Aging impairs contraction-induced human skeletal muscle mtorc1 signaling and protein synthesis
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BackgroundIngestion of Casein and Whey Proteins Result in Muscle Anabolism after Resistance Exercise
Tipton, K. D., Elliott, T. A., Cree‐Green, M., Wolf, S. E., Sanford, A. P., & Wolfe, R. R. (2004) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000147582.99810.c5 · Cited by 353
“Blood samples were analyzed for phenylalanine and leucine concentrations using the internal standard method and gas chromatography-mass spectrometry (GCMS) analysis (2,3).”
BackgroundMethodInfluentialSelf-citationDeterminants of Skeletal Muscle Catabolism After Severe Burn
Hart, D. W., Wolf, S. E., Chinkes, D. L., Gore, D. C., Mlcak, R. P., Beauford, R. B., Obeng, M. K., Lal, S., Gold, W. F., Wolfe, R. R., et al. (2000) · Annals of Surgery · doi:10.1097/00000658-200010000-00001 · Cited by 340
Self-citationResistance training reduces the acute exercise-induced increase in muscle protein turnover
Phillips, S. M., Tipton, K. D., Ferrando, A. A., & Wolfe, R. R. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.276.1.e118 · Cited by 336
“Previous studies that have examined the effects of an isolated bout of exercise on human muscle protein synthesis have reported that muscle protein FSR was increased in the postexercise period (3, 5, 17, 25, 26).”
BackgroundMethodResultInfluentialSelf-citationP ROTEIN AND A MINO A CID M ETABOLISM D URING AND A FTER E XERCISE AND THE E FFECTS OF N UTRITION
Rennie, M. J., & Tipton, K. D. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.457 · Cited by 321
Self-citationBurn size determines the inflammatory and hypermetabolic response
Jeschke, M. G., Mlcak, R. P., Finnerty, C. C., Norbury, W. B., Gauglitz, G. G., Kulp, G. A., & Herndon, D. N. (2007) · Critical Care · doi:10.1186/cc6102 · Cited by 325
“As a consequence, the structure and function of essential organs such as skeletal muscle, skin, immune system, and cellular membrane transport functions are compromised [17-19].”
BackgroundDrummond, M. J., Dreyer, H. C., Fry, C. S., Glynn, E. L., & Rasmussen, B. B. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91397.2008 · Cited by 322
“For example, several human studies in the early 1990s demonstrated that an acute bout of resistance exercise stimulated muscle protein synthesis during the first few hours of recovery (8, 21, 68, 113).”
Protein requirements and supplementation in strength sports
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Koopman, R., Wagenmakers, A. J. M., MANDERS, R. J. F., Zorenc, A. H. G., Senden, J. M., Gorselink, M., KEIZER, H. A., & van Loon, L. J. C. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00413.2004 · Cited by 319
“Although muscle protein synthesis is stimulated during the postexercise recovery phase (35), net muscle protein balance remains negative in the absence of food intake (7, 35, 36).”
BackgroundInfluentialChurchward‐Venne, T. A., Burd, N. A., Mitchell, C. J., West, D. W. D., Philp, A., Marcotte, G. R., Baker, S. K., Baar, K., & Phillips, S. M. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.228833 · Cited by 314
“It is currently unclear whether MPS is regulated by changes in extracellular (Bohe et al. 2003), or intracellular (Biolo et al. 1995) EAAs and/or leucine availability.”
BackgroundInfluentialStimulation of net muscle protein synthesis by whey protein ingestion before and after exercise
Tipton, K. D., Elliott, T. A., Cree, M. G., Aarsland, A. A., Sanford, A. P., & Wolfe, R. R. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00166.2006 · Cited by 307
“Muscle free amino acid concentration was measured with the internal standard method, with corrections for the contribution of extracellular fluid as described in Blood and in previous studies (1, 2).”
MethodInfluentialSelf-citationHasten, D. L., Pak-Loduca, J., Obert, K. A., & Yarasheski, K. E. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.4.e620 · Cited by 294
“The reduced rate of mixed and myofibrillar protein synthesis in 601-yr-old adults and the stimulatory effect of resistance exercise on the rate of amino acid transport into muscle and the rate of muscle protein synthesis in younger adults have been reported by others (4, 7, 8, 22).”
BackgroundMuscle fiber type diversification during exercise and regeneration
Qaisar, R., Bhaskaran, S., & Van Remmen, H. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.025 · Cited by 283
“Myofibriller proteins show a preferential increase in synthesis rate in the individuals trained for RE [144–146] along with smaller increase in protein breakdown [147].”
BackgroundKimball, S. R., Farrell, P. A., & Jefferson, L. S. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00221.2002 · Cited by 304
Human muscle protein synthesis and breakdown during and after exercise
Kumar, V., Atherton, P., Smith, K., & Rennie, M. J. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91481.2008 · Cited by 249
Regulation of Muscle Protein by Amino Acids
Wolfe, R. R. (2002) · The Journal of Nutrition · doi:10.1093/jn/131.10.3219s · Cited by 288
Self-citationIndependent and Combined Effects of Amino Acids and Glucose after Resistance Exercise
MILLER, S. L., TIPTON, K. D., CHINKES, D. L., WOLF, S. E., & WOLFE, R. R. (2003) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000053910.63105.45 · Cited by 283
“, net muscle protein synthesis) remains negative after resistance exercise (3,4).”
BackgroundSelf-citationAnabolic Effects of Oxandrolone After Severe Burn
Hart, D. W., Wolf, S. E., Ramzy, P. I., Chinkes, D. L., Beauford, R. B., Ferrando, A. A., Wolfe, R. R., & Herndon, D. N. (2001) · Annals of Surgery · doi:10.1097/00000658-200104000-00012 · Cited by 283
Self-citationA Brief Review of Critical Processes in Exercise-Induced Muscular Hypertrophy
Phillips, S. M. (2014) · Sports Medicine · doi:10.1007/s40279-014-0152-3 · Cited by 281
“In addition, postexercise hyperaminoacidemia suppresses the rise in MPB [4] that occurs following resistance exercise in the fasted state [1, 2].”
BackgroundPennings, B., Koopman, R., Beelen, M., Senden, J. M., Saris, W. H., & van Loon, L. J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.29649 · Cited by 311
Protein and amino acids for athletes
Tipton, K. D., & Wolfe, R. R. (2004) · Journal of Sports Sciences · doi:10.1080/0264041031000140554 · Cited by 274
“Local insulin infusion, such that arterial amino acid concentrations are maintained, has been demonstrated to stimulate muscle protein synthesis at rest (Biolo et al., 1995a).”
BackgroundInfluentialSelf-citationEffect of two contrasting types of physical exercise on chronic neck muscle pain
Andersen, L. L., Kjær, M., Søgaard, K., Hansen, L., Kryger, A. I., & Sjøgaard, G. (2007) · Arthritis Care & Research · doi:10.1002/art.23256 · Cited by 260
“It is well known that high-intensity strength training accelerates protein synthesis as well as degradation (40), which over a prolonged period may lead to turnover of painful and abnormal muscle tissue (41).”
BackgroundHeat shock response and autophagy—cooperation and control
Dokładny, K., Myers, O., & Moseley, P. L. (2015) · Autophagy · doi:10.1080/15548627.2015.1009776 · Cited by 268
Damas, F., Libardi, C. A., & Ugrinowitsch, C. (2018) · European Journal of Applied Physiology · doi:10.1007/s00421-017-3792-9 · Cited by 254
“RE induces acute increases in MPS, but also stimulates MPB (although in a lower extent than MPS), resulting in a still negative net protein balance in a fasted state, but ‘less-negative’ compared to a rested control (Biolo et al. 1995; Phillips et al. 1997).”
BackgroundRizzoli, R., Stevenson, J. C., Bauer, J. M., van Loon, L. J. C., Walrand, S., Kanis, J. A., Cooper, C., Brandi, M.-L., Diez-Perez, A., & Reginster, J.-Y. (2014) · Maturitas · doi:10.1016/j.maturitas.2014.07.005 · Cited by 291
Del Balso, C., & Cafarelli, E. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00477.2006 · Cited by 252
Nutritional interventions to augment resistance training-induced skeletal muscle hypertrophy
Morton, R. W., McGlory, C., & Phillips, S. M. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00245 · Cited by 234
“…(varying 4–5 times more than MPB) to changes in protein feeding and loading rendering it the primary locus determining gains in muscle mass. Performing resistance exercise (RE) followed by the consumption of protein results in an augmentation of MPS and, over time, can lead to muscle hypertrophy.”
BackgroundInfluentialMilk ingestion stimulates net muscle protein synthesis following resistance exercise
ELLIOT, T. A., CREE, M. G., SANFORD, A. P., WOLFE, R. R., & TIPTON, K. D. (2006) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000210190.64458.25 · Cited by 237
“Muscle protein synthesis can be stimulated during recovery from resistance exercise, but in the absence of nutrient intake, net muscle protein balance—the difference between protein synthesis and breakdown—remains negative (2,3,16,22).”
BackgroundMethodInfluentialSelf-citationReeves, N. D., Maganaris, C. N., Ferretti, G., & Narici, M. V. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01266.2004 · Cited by 244
“For instance, despite having similar resting rates, the soleus muscle shows a much smaller increase in the rate of protein synthesis compared with the vastus lateralis muscle in response to a single bout of high-intensity resistive exercise (16, 52, 62).”
BackgroundFerrando, A. A., Chinkes, D. L., Wolf, S. E., Matin, S., Herndon, D. N., & Wolfe, R. R. (1999) · Annals of Surgery · doi:10.1097/00000658-199901000-00002 · Cited by 234
Self-citationNutritional Strategies to Promote Postexercise Recovery
Beelen, M., Burke, L. M., Gibala, M. J., & van Loon, L. J. C. (2010) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.20.6.515 · Cited by 233
“Exercise stimulates both muscle protein synthesis and muscle protein breakdown during acute postexercise recovery (Biolo et al., 1995b; Biolo et al., 1999; Phillips et al., 1997; Pitkanen et al., 2003).”
BackgroundTipton, K. (1999) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(98)00087-4 · Cited by 231
Self-citationAndersen, L. L., Tufekovic, G., Zebis, M. K., Crameri, R. M., Verlaan, G., Kjær, M., Suetta, C., Magnusson, P., & Aagaard, P. (2005) · Metabolism · doi:10.1016/j.metabol.2004.07.012 · Cited by 228
“If a subject remains in a postabsorptive state, the net protein balance remains negative [4,19].”
BackgroundInfluentialBørsheim, E., Cree‐Green, M., Tipton, K. D., Elliott, T. A., Aarsland, A. A., & Wolfe, R. R. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00333.2003 · Cited by 237
“Blood samples for determination of amino acid enrichment and concentrations were immediately precipitated in preweighed tubes containing 15% sulfosalisylic acid and a weighed amount of an appropriate internal standard, consisting of phenylalanine labeled differently than the infused phenylalanine, was added (3, 4, 14).”
MethodSelf-citationAreta, J. L., Burke, L. M., Camera, D. M., West, D. W. D., Crawshay, S., Moore, D. R., Stellingwerff, T., Phillips, S. M., Hawley, J. A., & Coffey, V. G. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00590.2013 · Cited by 227
“Regardless, the provision of exogenous amino acid during ED appears to be a prerequisite for supporting muscle protein synthesis and allowing an increase in net muscle protein synthesis above that achieved at rest while in EB (2, 43).”
BackgroundKhodabukus, A., Madden, L. R., Prabhu, N. K., Koves, T. R., Jackman, C. P., Muoio, D. M., & Bursac, N. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.08.058 · Cited by 227
“Additionall y, stimulation-dependent increase in branch chain amino acid (BCAA) concentration (Fig S3A and B) was consistent with known regulatory roles of BCAA availability in mTORC1 activation and muscle hypertrophy found in resistance exercise [87, 90-94].”
Protein Ingestion before Sleep Improves Postexercise Overnight Recovery
RES, P. T., GROEN, B., PENNINGS, B., BEELEN, M., WALLIS, G. A., GIJSEN, A. P., SENDEN, J. M. G., & VAN LOON, L. J. C. (2012) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31824cc363 · Cited by 226
“A single session of resistance-type exercise stimulates both protein synthesis and breakdown rates (6,31,37).”
BackgroundBolster, D. R., Jefferson, L. S., & Kimball, S. R. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004355 · Cited by 231
“Biolo et al. (1995a) have impressively demonstrated marked increases in the delivery of amino acids to the leg 3 h after resistance exercise in a post-absorptive state.”
BackgroundResistance exercise maintains skeletal muscle protein synthesis during bed rest
Ferrando, A. A., Tipton, K. D., Bamman, M. M., & Wolfe, R. R. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.82.3.807 · Cited by 221
Self-citationMcGlory, C., Calder, P. C., & Nunes, E. A. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00144 · Cited by 242
Mayhew, D. L., Kim, J.-S., Cross, J. M., Ferrando, A. A., & Bamman, M. M. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91234.2008 · Cited by 215
Frailty and nutrition: Searching for evidence
Bonnefoy, M., Berrut, G., Lesourd, B., Ferry, M., Gilbert, T., Guérin, O., Hanon, O., Jeandel, C., Paillaud, É., Raynaud-Simon, A., et al. (2014) · The journal of nutrition health & aging · doi:10.1007/s12603-014-0568-3 · Cited by 207
“It is now well established that dietary proteins, in addition with resistance exercise, increase muscle protein accretion during the post exercise period (111).”
Nutritional modulation of training-induced skeletal muscle adaptations
Hawley, J. A., Burke, L. M., Phillips, S. M., & Spriet, L. L. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00949.2010 · Cited by 205
“, increased AA availability) or the associated rise in insulin (8) also suppresses the resistance exercise-induced MPB that occurs in the absence of nutrition (6, 78).”
BackgroundDamas, F., Phillips, S., Vechin, F. C., & Ugrinowitsch, C. (2015) · Sports Medicine · doi:10.1007/s40279-015-0320-0 · Cited by 225
“Increases in skeletal muscle mass can be achieved through resistance exercise (RE), which is a potent stimulator of muscle protein synthesis (MPS) [1–8].”
BackgroundKoopman, R., Verdijk, L. B., MANDERS, R. J. F., Gijsen, A. P., Gorselink, M., Pijpers, E., Wagenmakers, A. J. M., & van Loon, L. J. C. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/84.3.623 · Cited by 204
“(19, 20), which leads to net muscle protein loss.”
Phillips, S. M., Tang, J. E., & Moore, D. R. (2009) · Journal of the American College of Nutrition · doi:10.1080/07315724.2009.10718096 · Cited by 243
“While MPB also rises to a small degree (10–25%) with resistance exercise in the fasted state [80,82,83], this rise is completely suppressed with the provision of amino acids [62] or carbohydrates [76].”
BackgroundEnergy Expenditure and Caloric Balance After Burn
Hart, D. W., Wolf, S. E., Herndon, D. N., Chinkes, D. L., Lal, S., Obeng, M. K., Beauford, R. B., & Mlcak, R. P. (2002) · Annals of Surgery · doi:10.1097/00000658-200201000-00020 · Cited by 200
Sheffield-Moore, M., Yeckel, C. W., Volpi, E., Wolf, S. E., Morio, B., Chinkes, D. L., Paddon-Jones, D., & Wolfe, R. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00334.2003 · Cited by 197
“Numerous studies have supported this recommendation, demonstrating that resistance exercise clearly elevates muscle protein synthesis (4, 5, 13, 42, 56, 63, 64).”
ResultSelf-citationCancer cachexia prevention via physical exercise: molecular mechanisms
Gould, D. W., Lahart, I. M., Carmichael, A. R., Koutedakis, Y., & Metsios, G. S. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0096-0 · Cited by 200
“However, the restriction of muscle protein synthesis that occurs during exercise is rapidly reversed following exercise recovery, a very consistent finding in the literature [166–171].”
ResultTipton, K. D., Borsheim, E., Wolf, S. E., Sanford, A. P., & Wolfe, R. R. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00234.2002 · Cited by 193
“The femoral arterial catheter was also used for infusion of indocyanine green dye (ICG) for blood flow measurement using the dye-dilution technique, as previously described (4, 6).”
BackgroundMethodInfluentialSelf-citationMacnaughton, L. S., Wardle, S. L., Witard, O. C., McGlory, C., Hamilton, D. L., Jeromson, S., Lawrence, C. E., Wallis, G. A., & Tipton, K. D. (2016) · Physiological Reports · doi:10.14814/phy2.12893 · Cited by 191
Self-citationReitelseder, S., Agergaard, J., Doessing, S., Helmark, I. C., Lund, P., Kristensen, N. B., Frystyk, J., Flyvbjerg, A., Schjerling, P., van Hall, G., et al. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00513.2010 · Cited by 190
“Resistance exercise, either alone (5, 13, 47) or in combination with AAs or whole proteins (6, 11, 44), is able to increase muscle protein synthesis (MPS), and as a consequence of repeated training sessions muscle mass and strength will increase (1, 29, 30).”
BackgroundWolfe, R. R. (2012) · British Journal Of Nutrition · doi:10.1017/s0007114512002590 · Cited by 187
“The stimulatory effect of amino acid intake is amplified if combined with the performance of resistance exercise((13)).”
BackgroundSelf-citationStrategies to Prevent Sarcopenia in the Aging Process: Role of Protein Intake and Exercise
Rogeri, P. S., Zanella, R., Martins, G. L., Garcia, M. D. A., Leite, G., Lugaresi, R., Gasparini, S. O., Sperandio, G. A., Ferreira, L. H. B., Souza-Junior, T. P., et al. (2021) · Nutrients · doi:10.3390/nu14010052 · Cited by 181
“When the rate of MPS exceeds MPB, a positive net muscle protein balance occurs, meaning that new proteins are being incorporated into muscle tissue, resulting in muscle hypertrophy in the long term.”
BackgroundInfluentialNunes, E. A., Stokes, T., McKendry, J., Currier, B. S., & Phillips, S. M. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00425.2021 · Cited by 194
Whey protein supplementation during resistance training augments lean body mass
Volek, J. S., Volk, B. M., Gómez, A. L., Kunces, L. J., Kupchak, B. R., Freidenreich, D. J., Aristizabal, J. C., Saenz, C., Dunn-Lewis, C., Ballard, K. D., et al. (2013) · Journal of the American College of Nutrition · doi:10.1080/07315724.2013.793580 · Cited by 181
“Compared to the fasting state, a bout of resistance exercise has a positive impact on muscle protein synthesis, but in the absence of dietary protein intake, net protein balance remains negative [2], even if carbohydrate is ingested [3].”
BackgroundHulmi, J. J., Lockwood, C. M., & Stout, J. R. (2010) · Nutrition & Metabolism · doi:10.1186/1743-7075-7-51 · Cited by 238
“Thus, there seems to exist an enhanced time-window for the uptake of amino acids and glucose into muscle [2,73-75].”
Maximizing muscle protein anabolism: the role of protein quality
Tang, J. E., & Phillips, S. M. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32831cef75 · Cited by 178
Resistance exercise alters MRF and IGF-I mRNA content in human skeletal muscle
Psilander, N., Damsgaard, R., & Pilegaard, H. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00903.2002 · Cited by 178
“CONVENTIONAL RESISTANCE EXERCISE induces increased synthesis of skeletal muscle proteins, leading to muscle hypertrophy (8, 10, 41).”
BackgroundPasiakos, S. M., Lieberman, H. R., & McLellan, T. M. (2014) · Sports Medicine · doi:10.1007/s40279-013-0137-7 · Cited by 178
Snijders, T., Res, P. T., Smeets, J. S., van Vliet, S., van Kranenburg, J., Maase, K., Kies, A. K., Verdijk, L. B., & van Loon, L. J. (2015) · The Journal of Nutrition · doi:10.3945/jn.114.208371 · Cited by 175
Resistance training alters the response of fed state mixed muscle protein synthesis in young men
Tang, J. E., Perco, J. G., Moore, D. R., Wilkinson, S. B., & Phillips, S. M. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00636.2007 · Cited by 181
Metadata
- Authors
- Biolo, G., Maggi, S. P., Williams, B. D., Tipton, K. D., & Wolfe, R. R.
- Affiliations
- The University of Texas Medical Branch at Galveston (US)
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 1995-03-01
- Volume
- 268
- Issue
- 3
- Pages
- E514-E520
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2183437665
- Cited by
- 713
- References
- 28
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 17 · 2023: 23 · 2022: 20 · 2021: 29 · 2020: 29 · 2019: 27 · 2018: 31 · 2017: 28 · 2016: 27 · 2015: 35 · 2014: 32 · 2013: 40 · 2012: 36
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
- Stirling Online Research Repository (University of Stirling) (submittedVersion, public-domain)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-38010, R01DK038010)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Keywords
- muscle protein turnover, resistance training, amino acid transport, protein synthesis, proteolysis, post-exercise recovery, leucine transport, lysine transport, alanine transport, vastus lateralis, lower limb muscles, muscle protein balance
- MeSH terms
- Adult, Alanine, Amino Acids, Biological Transport, Blood Flow Velocity, Humans, Kinetics, Leg, Leucine, Lysine, Male, Muscle Proteins, Phenylalanine, Weight Lifting, Exercise
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