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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Dietary Protein to Support Anabolism with Resistance Exercise in Young Men
Phillips, S. M., Hartman, J. W., & Wilkinson, S. B. (2005) · Journal of the American College of Nutrition · doi:10.1080/07315724.2005.10719454 · Cited by 174
“When MPB is examined at the same time as MPS after resistance exercise muscle NPB has been shown to be negative but approaches zero, due to a relatively greater stimulation of MPS than MPB [8,9,11].”
BackgroundInfluentialFasted‐state skeletal muscle protein synthesis after resistance exercise is altered with training
Kim, P. L., Staron, R. S., & Phillips, S. M. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.093708 · Cited by 171
“Email: phillis@mcmaster.ca Resistance exercise has been shown to stimulate muscle protein synthesis (MPS) in an absolute sense and also compared with muscle protein breakdown (MPB; (Biolo et al. 1995; Phillips et al. 1997, 1999).”
BackgroundResultInfluentialEffect of glucose supplement timing on protein metabolism after resistance training
Roy, B. D., Tarnopolsky, M. A., MacDOUGALL, J. D., Fowles, J. R., & Yarasheski, K. E. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.82.6.1882 · Cited by 171
“Net protein balance, although more positive, was still negative after resistance exercise in the fasted state (4).”
BackgroundMethodResultInfluentialGlynn, E. L., Fry, C. S., Drummond, M. J., Timmerman, K. L., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2010) · The Journal of Nutrition · doi:10.3945/jn.110.127647 · Cited by 194
Resistance-training-induced adaptations in skeletal muscle protein turnover in the fed state
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“It has been shown in a number of previous investigations (Biolo et al. 1995; Phillips et al. 1997, 1999; Tipton et al. 1999) that an isotopic plateau would occur in these sampled pools, given the total infusion times and appropriate priming doses.”
BackgroundResultInfluentialSelf-citationGlynn, E. L., Fry, C. S., Drummond, M. J., Dreyer, H. C., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00077.2010 · Cited by 177
Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy
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“Indeed, exercise has been demonstrated to enhance the transport of other amino acids (4), which has been suggested to be only partly dependent on increased muscle blood flow (42).”
Backgroundvan Loon, L. J. C., Kruijshoop, M., Verhagen, H., Saris, W. H. M., & Wagenmakers, A. J. M. (2000) · Journal of Nutrition · doi:10.1093/jn/130.10.2508 · Cited by 155
Assessing the role of muscle protein breakdown in response to nutrition and exercise in humans.
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“Given that exercise increases the metabolism of the muscle with little impact on other tissues, it is a reasonable assumption that measurements made using these AV models following exercise represent changes in muscle metabolism [3, 7].”
BackgroundMethodResultInfluentialSelf-citationBabault, N., Païzis, C., Deley, G., Guérin-Deremaux, L., Saniez, M.-H., Lefranc-Millot, C., & Allaert, F. A. (2015) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-014-0064-5 · Cited by 151
“, muscle hypertrophy) is observed immediately after resistance exercises [2-4] as a result of a positive protein net balance; the difference between muscle fiber catabolism and anabolism.”
BackgroundEffects of aging and lifelong aerobic exercise on basal and exercise-induced inflammation
Lavin, K. M., Perkins, R. K., Jemioło, B., Raue, U., Trappe, S. W., & Trappe, T. A. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00495.2019 · Cited by 150
Promoting training adaptations through nutritional interventions
Hawley, J. A., Tipton, K. D., & Millard-Stafford, M. L. (2006) · Journal of Sports Sciences · doi:10.1080/02640410500482727 · Cited by 157
Self-citationProtein supplements and exercise
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Self-citationTracers to investigate protein and amino acid metabolism in human subjects
Wagenmakers, A. J. M. (1999) · Proceedings of The Nutrition Society · doi:10.1017/s0029665199001305 · Cited by 150
Sex-based comparisons of myofibrillar protein synthesis after resistance exercise in the fed state
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“Discussion In this study, we sought to understand the relationships between whole-body leucine flux, muscle protein synthesis (MPS), small molecule metabolites and glucose homeostasis in lean, insulin sensitive and OW, insulin-resistant individuals, and to understand the effects of a combined aerobic and resistance ex…”
InfluentialResistance exercise increases leg muscle protein synthesis and mTOR signalling independent of sex
Dreyer, H. C., Fujita, S., Glynn, E. L., Drummond, M. J., Volpi, E., & Rasmussen, B. B. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02074.x · Cited by 149
“High-intensity resistance exercise stimulates both muscle protein synthesis and breakdown during the post-exercise recovery period; however, the magnitude of the change in each is not proportional with increases in synthesis exceeding that of breakdown (Biolo et al. 1995).”
BackgroundRegulation of mTOR by amino acids and resistance exercise in skeletal muscle
Deldicque, L., Theisen, D., & Francaux, M. (2005) · European Journal of Applied Physiology · doi:10.1007/s00421-004-1255-6 · Cited by 147
“2003; Tipton and Wolfe 1998), but not protein breakdown (Biolo et al. 1995; Phillips et al. 1997), is enhanced, and the net protein balance becomes positive.”
BackgroundInfluentialBeyond the Zone: Protein Needs of Active Individuals
Lemon, P. W. R. (2000) · Journal of the American College of Nutrition · doi:10.1080/07315724.2000.10718974 · Cited by 137
“5 [25]) and the need to maintain a greater overall muscle mass [26].”
BackgroundMcGlory, C., Devries, M. C., & Phillips, S. M. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00613.2016 · Cited by 135
Androgen receptor content following heavy resistance exercise in men
Ratamess, N. A., Kraemer, W. J., Volek, J. S., Maresh, C. M., VanHeest, J. L., Sharman, M. J., Rubin, M. R., French, D. N., Vescovi, J. D., Silvestre, R., et al. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.10.019 · Cited by 140
Holm, L., van Hall, G., Rose, A. J., Miller, B. F., Doessing, S., Richter, E. A., & Kjaer, M. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00609.2009 · Cited by 132
Andersen, J. L., & Aagaard, P. (2010) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2010.01196.x · Cited by 133
“Furthermore, the increase in synthesis is withheld for a longer period than the increase in protein degradation (Biolo et al., 1995).”
BackgroundPhilp, A., Hamilton, D. L., & Baar, K. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00941.2010 · Cited by 131
Muscle Protein Synthetic Responses to Exercise: Effects of Age, Volume, and Intensity
Kumar, V., Atherton, P. J., Selby, A., Rankin, D., Williams, J., Smith, K., Hiscock, N. J., & Rennie, M. J. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/gls141 · Cited by 146
Howarth, K. R., Phillips, S. M., MacDonald, M. J., Richards, D. L., Moreau, N. A., & Gibala, M. J. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00108.2009 · Cited by 131
“A two-pool model was used to calculate the muscle Ra and Rd of phenylalanine across the muscle as an estimate of muscle protein degradation and synthesis, respectively, as previously described (1, 3):”
MethodProtein Considerations for Optimising Skeletal Muscle Mass in Healthy Young and Older Adults
Witard, O., Wardle, S., Macnaughton, L., Hodgson, A., & Tipton, K. (2016) · Nutrients · doi:10.3390/nu8040181 · Cited by 132
“The most likely contributing mechanism is 55 an exercise-induced increase in blood flow to the muscle [5] that increases the delivery of amino acid 56 to the muscle, thus increasing the provision of substrate for MPS [9].”
Self-citationFujita, S., Dreyer, H. C., Drummond, M. J., Glynn, E. L., Volpi, E., & Rasmussen, B. B. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90395.2008 · Cited by 129
Hevia-Larraín, V., Gualano, B., Longobardi, I., Gil, S., Fernandes, A. L., Costa, L. A. R., Pereira, R. M. R., Artioli, G. G., Phillips, S. M., & Roschel, H. (2021) · Sports Medicine · doi:10.1007/s40279-021-01434-9 · Cited by 132
Leucine attenuates skeletal muscle wasting via inhibition of ubiquitin ligases
Baptista, I. L., Leal, M. L., Artioli, G. G., Aoki, M. S., Fiamoncini, J., Turri, A. O., Curi, R., Miyabara, E. H., & Moriscot, A. S. (2010) · Muscle & Nerve · doi:10.1002/mus.21578 · Cited by 131
“Possibilities include different fiber-type leucine uptake capacity and preferred metabolization of leucine by type I fibers.(36,37) In order to investigate the mechanisms associ-”
BackgroundMacronutrient Considerations for the Sport of Bodybuilding
Lambert, C. P., Frank, L. L., & Evans, W. J. (2004) · Sports Medicine · doi:10.2165/00007256-200434050-00004 · Cited by 134
Dietary protein, metabolism, and body-weight regulation: dose–response effects
Westerterp-Plantenga, M. S., Luscombe-Marsh, N., Lejeune, M. P. G. M., Diepvens, K., Nieuwenhuizen, A., Engelen, M. P. K. J., Deutz, N. E. P., Azzout-Marniche, D., Tome, D., & Westerterp, K. R. (2006) · International Journal of Obesity · doi:10.1038/sj.ijo.0803487 · Cited by 127
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“and net protein balance becomes even more positive (49).”
BackgroundShad, B. J., Thompson, J. L., & Breen, L. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00213.2016 · Cited by 131
“Ultimately, overall NBAL dictates long-term skeletal muscle remodeling, which is the end point in the diagnosis of sarcopenia, and as such, the findings of this systematic review should be considered within this broader context.”
BackgroundInfluentialFunctional impact of high protein intake on healthy elderly people
Walrand, S., Short, K. R., Bigelow, M. L., Sweatt, A. J., Hutson, S. M., & Nair, K. S. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90536.2008 · Cited by 125
Exercise‐induced changes in protein metabolism
Tipton, K. D., & Wolfe, R. R. (1998) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.1998.00306.x · Cited by 125
“Similarly, using the A-V model, we have shown that amino acid transport into the muscle and muscle blood ¯ow are increased following resistance exercise (Biolo et al. 1995c).”
BackgroundMethodInfluentialSelf-citationBird, S. P., Tarpenning, K. M., & Marino, F. E. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-005-0127-z · Cited by 122
“However, in the absence of nutritional intake, net muscle protein balance (i.e., the difference between protein synthesis and degradation) remains negative in the early stages of recovery (Biolo et al. 1995).”
BackgroundInfluentialBørsheim, E., Aarsland, A. A., & Wolfe, R. R. (2004) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.14.3.255 · Cited by 122
“Because previous studies have shown that net muscle protein balance remains slightly negative for several hours after resistance exercise in the absence of nutrient intake (2, 7), a placebo group was not included in this study.”
BackgroundMethodResultSelf-citationDrummond, M. J., Fry, C. S., Glynn, E. L., Timmerman, K. L., Dickinson, J. M., Walker, D. K., Gundermann, D. M., Volpi, E., & Rasmussen, B. B. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01408.2010 · Cited by 120
Baehr, L. M., West, D. W. D., Marshall, A. G., Marcotte, G. R., Baar, K., & Bodine, S. C. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00703.2016 · Cited by 123
“, less negative, in the absence of exogenous amino acids), shifting the exercised muscle toward anabolism (8, 36).”
BackgroundSong, Z., Moore, D. R., Hodson, N. W., Ward, C., Dent, J. R., O’Leary, M. F., Shaw, A. M., Hamilton, D. L., Sarkar, S., Gangloff, Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05483-x · Cited by 120
Short-Term Training: When Do Repeated Bouts of Resistance Exercise Become Training?
Phillips, S. M. (2000) · Canadian Journal of Applied Physiology · doi:10.1139/h00-014 · Cited by 119
Using Molecular Biology to Maximize Concurrent Training
Baar, K. (2014) · Sports Medicine · doi:10.1007/s40279-014-0252-0 · Cited by 135
“Specifically, leucine and glutamine are increased within the working muscle [9, 15].”
BackgroundPatterson, B. W., Zhang, X.-J., Chen, Y., Klein, S., & Wolfe, R. R. (1997) · Metabolism · doi:10.1016/s0026-0495(97)90084-6 · Cited by 118
Self-citationHarber, M. P., Konopka, A. R., Jemioło, B., Trappe, S. W., Trappe, T. A., & Reidy, P. T. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00348.2010 · Cited by 116
“In addition to the influence of exercise on muscle protein synthesis, muscle protein breakdown is elevated after both aerobic (44) and resistance (3, 40) exercise.”
BackgroundReidy, P. T., & Rasmussen, B. B. (2016) · The Journal of Nutrition · doi:10.3945/jn.114.203208 · Cited by 128
“During this time, blood flow and lactate concentrations normalize as the muscle becomes more sensitive to nutrients, presumably due to the increased AA flux (14, 98, 109), mTORC1 signaling, most noticeably through p70 ribosomal protein S6 kinase 1 (S6K1) phosphorylation (24, 33, 109), and increased insulin sensitivity.”
BackgroundWolf, S. E., Thomas, S. J., Dasu, M. R. K., Ferrando, A. A., Chinkes, D. L., Wolfe, R. R., & Herndon, D. N. (2003) · Annals of Surgery · doi:10.1097/01.sla.0000071562.12637.3e · Cited by 115
“The blood concentration of unlabeled phenylalanine was determined by gas chromatography-mass spectrometry (GCMS) using the internal standard approach and the nitrogen-acetol-n-propyl esters, as previously described.(31) The isotopic enrichment of free amino acids in blood was determined on a HP model 5989 (Hewlett-Pac…”
MethodSelf-citationA Critical Examination of Dietary Protein Requirements, Benefits, and Excesses in Athletes
Phillips, S. M., Moore, D. R., & Tang, J. E. (2007) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.17.s1.s58 · Cited by 117
“This finding may not be surprising when one considers that endurance exercise (to a small degree) (51, 76) and resistance exercise (to a very large degree) (6, 65) are anabolic in that they stimulate muscle protein synthesis even in the fasted state, forcing an increased net “conservation” of amino acids arising from…”
BackgroundHeyland, D. K., Stapleton, R. D., Mourtzakis, M., Hough, C. L., Morris, P. E., Deutz, N. E. P., Colantuoni, E., Day, A. G., Prado, C. M. M., & Needham, D. M. (2015) · Clinical Nutrition · doi:10.1016/j.clnu.2015.07.003 · Cited by 119
Dietary protein for athletes: from requirements to metabolic advantage
Phillips, S. M. (2006) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h06-035 · Cited by 121
Tipton, K. D., Ferrando, A. A., Williams, B. D., & Wolfe, R. R. (1996) · Journal of Applied Physiology · doi:10.1152/jappl.1996.81.5.2034 · Cited by 114
“(3) found that muscle PS in the vastus lateralis 4 h postexercise was increased by 133% in untrained men.”
BackgroundMethodResultInfluentialSelf-citationCharacterization and Regulation of Mechanical Loading‐Induced Compensatory Muscle Hypertrophy
Adams, G. R., & Bamman, M. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c110066 · Cited by 123
The anabolic response to resistance exercise and a protein-rich meal is not diminished by age
Symonsi, T. B., Sheffield-Moore, M., Mamerow, M. M., Wolfe, R. R., & Paddon-Jones, D. (2011) · The Journal of nutrition, health and aging · doi:10.1007/s12603-010-0319-z · Cited by 112
Self-citationPre-Sleep Protein Ingestion to Improve the Skeletal Muscle Adaptive Response to Exercise Training
Trommelen, J., & Van Loon, L. (2016) · Nutrients · doi:10.3390/nu8120763 · Cited by 116
“A single session of exercise stimulates muscle protein synthesis rates, and to a lesser extent, muscle protein breakdown rates [1,2].”
BackgroundLeucine as a pharmaconutrient to prevent and treat sarcopenia and type 2 diabetes
Leenders, M., & van Loon, L. J. C. (2011) · Nutrition Reviews · doi:10.1111/j.1753-4887.2011.00443.x · Cited by 115
Stimulation of myofibrillar synthesis by exercise is mediated by more efficient translation of mRNA
Welle, S. L., Bhatt, K. S., & Thornton, C. A. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.86.4.1220 · Cited by 112
“RESISTANCE EXERCISES STIMULATE muscle protein synthesis in humans (5, 8, 29, 32, 33).”
BackgroundSkeletal muscle protein balance and metabolism in the elderly
S. Fry, C., & B. Rasmussen, B. (2011) · Current Aging Sciencee · doi:10.2174/1874609811104030260 · Cited by 111
“The rate of muscle protein breakdown is also stimulated following a bout of resistance exercise [100,103], but to a lesser extent than the rate of synthesis.”
Monteyne, A. J., Coelho, M. O., Porter, C., Abdelrahman, D. R., Jameson, T. S., Jackman, S. R., Blackwell, J. R., Finnigan, T. J., Stephens, F. B., Dirks, M. L., et al. (2020) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa092 · Cited by 110
Terzis, G., Spengos, K., Mascher, H., Georgiadis, G., Manta, P., & Blomstrand, E. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1527-2 · Cited by 110
Dideriksen, K., Reitelseder, S., & Holm, L. (2013) · Nutrients · doi:10.3390/nu5030852 · Cited by 110
“Resistance exercise increases both MPS and MPB, but the MPS is stimulated to greater extent [74].”
BackgroundThe Molecular Basis for Load-Induced Skeletal Muscle Hypertrophy
Marcotte, G. R., West, D. W. D., & Baar, K. (2014) · Calcified Tissue International · doi:10.1007/s00223-014-9925-9 · Cited by 123
“However, we do know that intracellular amino acid levels (leucine in particular) increase acutely after strength exercise [64, 65], possibly due to an increase in amino acid transporters, including the primary leucine transporter in muscle LAT1 [116, 117].”
BackgroundAerobic Exercise Training Increases Skeletal Muscle Protein Turnover in Healthy Adults at Rest
Pikosky, M. A., Gaine, P. C., Martin, W. F., Grabarz, K. C., Ferrando, A. A., Wolfe, R. R., & Rodriguez, N. R. (2006) · Journal of Nutrition · doi:10.1093/jn/136.2.379 · Cited by 110
Self-citationAmino Acid Supplements and Recovery from High-Intensity Resistance Training
Sharp, C., & Pearson, D. R. (2010) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e3181c7c655 · Cited by 114
“24(4): 1125–1130, 2010—The purpose of this study was to”
BackgroundThe Muscle Protein Synthetic Response to Meal Ingestion Following Resistance-Type Exercise
Trommelen, J., Betz, M. W., & van Loon, L. J. C. (2019) · Sports Medicine · doi:10.1007/s40279-019-01053-5 · Cited by 117
“A single session of exercise stimulates muscle protein synthesis (MPS) rates and, to a lesser extent, muscle protein breakdown rates [1, 2].”
BackgroundTipton, K. D., & Witard, O. C. (2007) · Clinics in Sports Medicine · doi:10.1016/j.csm.2006.11.003 · Cited by 105
Self-citationKaspy, M. S., Hannaian, S. J., Bell, Z. W., & Churchward‐Venne, T. A. (2023) · Nutrition Research Reviews · doi:10.1017/s0954422423000197 · Cited by 117
“The stimulation of MPB that occurs in response to resistance exercise in the postabsorptive (i.e. fasted) state (42) may be prevented when amino acids are administered after exercise (43) .”
InfluentialBeelen, M., Tieland, M., Gijsen, A. P., Vandereyt, H., Kies, A. K., Kuipers, H., Saris, W. H. M., Koopman, R., & van Loon, L. J. C. (2008) · The Journal of Nutrition · doi:10.3945/jn.108.092924 · Cited by 104
Hermans, W. J. H., Senden, J. M., Churchward‐Venne, T. A., Paulussen, K. J. M., Fuchs, C. J., Smeets, J. S. J., van Loon, J. J. A., Verdijk, L. B., & van Loon, L. J. C. (2021) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqab115 · Cited by 109
“Exercise before protein intake sensitizes skeletal muscle tissue to the anabolic properties of amino acids, resulting in an even greater postprandial increase in muscle protein synthesis rates (11, 49).”
BackgroundWelle, S. L., & Thornton, C. A. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.274.4.e677 · Cited by 102
“The present study confirms previous reports that muscle protein synthesis increases after resistance exercise (3, 4, 7, 11, 29, 40, 41).”
BackgroundResultThe impact of exercise and nutrition on the regulation of skeletal muscle mass
McGlory, C., van Vliet, S., Stokes, T., Mittendorfer, B., & Phillips, S. M. (2018) · The Journal of Physiology · doi:10.1113/jp275443 · Cited by 110
“Since then, a series of studies by Professor Rennie’s group (e.g. Rennie et al. 2004; Atherton et al. 2010) and others (e.g. Biolo et al. 1995, 1997; Reidy et al. 2017) have explored the diurnal regulation of muscle protein turnover (e.g. the balance between synthesis and breakdown).”
BackgroundMetabolic consequences of physical inactivity
Biolo, G., Ciocchi, B., Stulle, M., Piccoli, A., Lorenzon, S., Mas, V. D., Barazzoni, R., Zanetti, M., & Guarnieri, G. (2005) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2004.09.009 · Cited by 101
Self-citationTannerstedt, J., Apró, W., & Blomstrand, E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91243.2008 · Cited by 104
Cooke, M. B., Rybalka, E., Stathis, C. G., Cribb, P. J., & Hayes, A. (2010) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-7-30 · Cited by 101
“However, providing exogenous amino acids, especially within the first 4 hours after resistance exercise (as implemented in the present study), increases protein synthesis, decreases protein breakdown, and produces a positive protein balance [31,33], thus providing an environment for muscle”
BackgroundLuiking, Y. C., Deutz, N. E. P., Memelink, R. G., Verlaan, S., & Wolfe, R. R. (2014) · Nutrition Journal · doi:10.1186/1475-2891-13-9 · Cited by 104
“with net protein breakdown, in the absence of nutrient intake [16].”
BackgroundSelf-citationDickinson, J. M., Gundermann, D. M., Walker, D. K., Reidy, P. T., Borack, M. S., Drummond, M. J., Arora, M., Volpi, E., & Rasmussen, B. B. (2014) · Journal of Nutrition · doi:10.3945/jn.114.198671 · Cited by 107
Role of Functional Beverages on Sport Performance and Recovery
Orrù, S., Imperlini, E., Nigro, E., Alfieri, A., Cevenini, A., Polito, R., Daniele, A., Buono, P., & Mancini, A. (2018) · Nutrients · doi:10.3390/nu10101470 · Cited by 123
“Historically, early studies on protein supplementation took into account individual amino acids (AAs) or their mixtures [139,140], whereas more recent investigations focus on intact high-quality proteins [131,141–147].”
BackgroundMersmann, F., Böhm, S., & Arampatzis, A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00987 · Cited by 99
“It has been demonstrated that the increase of muscle protein synthesis following an acute bout of resistance exercise exceeds the increase of protein breakdown, given a sufficient amino acid availability provided by appropriate feeding (Rennie et al., 1982; Biolo et al., 1995; Phillips et al., 1997).”
BackgroundExploring the Impact of Obesity on Skeletal Muscle Function in Older Age
Morgan, P. T., Smeuninx, B., & Breen, L. (2020) · Frontiers in Nutrition · doi:10.3389/fnut.2020.569904 · Cited by 108
Trappe, T. A., Williams, R. H., Carrithers, J. A., Raue, U., Esmarck, B., Kjær, M., & Hickner, R. C. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.051755 · Cited by 100
Stable isotope tracers and exercise physiology: Past, present and future
Wilkinson, D. J., Brook, M. S., Smith, K., & Atherton, P. J. (2017) · The Journal of Physiology · doi:10.1113/jp272277 · Cited by 97
“when performed in the absence of nutrition, exercise is catabolic (Biolo et al. 1995; Phillips et al. 1999; Kumar et al. 2009), and that the essential amino acid (EAA) constituents of food are the key nutrients supporting exercise-induced increases in muscle protein synthesis (MPS) (Pennings et al.”
BackgroundReidy, P. T., Walker, D. K., Dickinson, J. M., Gundermann, D. M., Drummond, M. J., Timmerman, K. L., Cope, M. B., Mukherjea, R., Jennings, K., Volpi, E., et al. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01093.2013 · Cited by 97
“transport into muscle, FM,A EM Ev ⁄ EA EM · CV CA · BF (4)”
BackgroundResultInfluentialClinical Impact of Sarcopenia on Gastric Cancer
Kuwada, K., Kuroda, S., Kikuchi, S., Yoshida, R., Nishizaki, M., Kagawa, S., & Fujiwara, T. (2019) · Anticancer Research · doi:10.21873/anticanres.13340 · Cited by 98
“According to the data that resistance exercise promotes muscle protein synthesis (47), Biolo et al. have demonstrated that the stimulatory effect of exogenous amino ANTICANCER RESEARCH 39: 2241-2249 (2019)”
BackgroundBird, S. P., Tarpenning, K. M., & Marino, F. E. (2006) · Metabolism · doi:10.1016/j.metabol.2005.11.011 · Cited by 96
“Resistance exercise stimulates immediate changes in the rate of muscle protein turnover, resulting in an increase in both protein synthesis and protein degradation [1-3].”
BackgroundHypertrophy of skeletal muscle in diabetic rats in response to chronic resistance exercise
Farrell, P. A., Fedele, M. J., Hernandez, J. M., Fluckey, J. D., Miller, J. L., Lang, C. H., Vary, T. C., Kimball, S. R., & Jefferson, L. S. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.87.3.1075 · Cited by 95
“Rates of proteolysis were not assessed in this study; however, other studies show that proteolysis increases after resistance exercise (1).”
BackgroundmVps34 is activated following high‐resistance contractions
MacKenzie, M. G., Hamilton, D. L., Murray, J. T., Taylor, P. M., & Baar, K. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159830 · Cited by 94
“This increase in intracellular amino acid levels is consistent with the increase in leucine, lysine and alanine influx observed 3 h after a bout of resistance exercise in humans (Biolo et al. 1995).”
BackgroundKim, I.-Y., Schutzler, S., Schrader, A., Spencer, H. J., Azhar, G., Ferrando, A. A., & Wolfe, R. R. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00365.2015 · Cited by 109
“MPB increases in response to resistance exercise (6, 8, 23).”
BackgroundSelf-citationAlemañy, G. M., Valdez-Ortiz, R., Olvera-Soto, G., Gómez-Guerrero, I., Aguire-Esquivel, G., Cantú-Quintanilla, G., López-Alvarenga, J. C., Miranda-Alatriste, P., & Espinosa-Cuevas, Á. (2016) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfw297 · Cited by 94
“On the other hand, we speculate that the addition of one can of ONS to RE is unable to increase this anabolic effect, as some studies have described that in addition of the HD procedure, which induces a catabolic state [4, 5], both muscle protein synthesis and muscle protein breakdown are increased after RE [55, 56].”
BackgroundProtein coingestion stimulates muscle protein synthesis during resistance-type exercise
Beelen, M., Koopman, R., Gijsen, A. P., Vandereyt, H., Kies, A. K., Kuipers, H., Saris, W. H. M., & van Loon, L. J. C. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00774.2007 · Cited by 94
“Previous studies (3, 26, 34) have reported that an acute bout of resistance-type exercise stimulates both muscle protein synthesis and breakdown rates.”
BackgroundTang, J. E., Manolakos, J. J., Kujbida, G. W., Lysecki, P. J., Moore, D. R., & Phillips, S. M. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-076 · Cited by 130
“1993); however, net protein balance (the algebraic difference between MPS and muscle protein breakdown (MPB)) remains negative in the absence of amino acid – protein consumption (Biolo et al. 1995b; Phillips et al. 1997, 1999).”
BackgroundInfluence of Nutrition on Responses to Resistance Training
VOLEK, J. S. (2004) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000121944.19275.c4 · Cited by 93
“Nutrient availability is critical during this time as evidenced by studies showing little glycogen resynthesis (43,51) and a negative protein balance (4,5) in the absence of nutritional intake after exercise.”
BackgroundMaximizing Post-exercise Anabolism: The Case for Relative Protein Intakes
Moore, D. R. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00147 · Cited by 106
“Since the first observations that skeletal muscle protein turnover is elevated in response to resistance exercise and that exogenous amino acids augment the increase in net protein balance of this tissue (2, 3), studies have investigated the nutritional factors that contribute to the optimal enhancement of post-exerci…”
BackgroundHolwerda, A. M., Paulussen, K. J. M., Overkamp, M., Goessens, J. P. B., Kramer, I. F., Wodzig, W. K. W. H., Verdijk, L. B., & van Loon, L. J. C. (2019) · Journal of Nutrition · doi:10.1093/jn/nxy263 · Cited by 96
Lohuis, T., Harlow, H. J., & Beck, T. D. (2007) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2006.12.020 · Cited by 90
Petersen, S. G., Beyer, N., Hansen, M., Holm, L., Aagaard, P., Mackey, A. L., & Kjær, M. (2011) · Archives of Physical Medicine and Rehabilitation · doi:10.1016/j.apmr.2011.03.009 · Cited by 87
Circulating protein synthesis rates reveal skeletal muscle proteome dynamics
Shankaran, M., King, C. L., Angel, T. E., Holmes, W. E., Li, K. W., Colangelo, M., Price, J. C., Turner, S., Bell, C., Hamilton, K. L., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79639 · Cited by 90
Glover, E. I., Oates, B. R., Tang, J. E., Moore, D. R., Tarnopolsky, M. A., & Phillips, S. M. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00097.2008 · Cited by 87
“MUSCLE PROTEIN SYNTHESIS (MPS) is synergistically increased by resistance exercise (3, 12, 17, 18, 48, 61) and feeding (4, 25, 51, 57).”
BackgroundProtein Source and Muscle Health in Older Adults: A Literature Review
Putra, C., Konow, N., Gage, M. J., York, C., & Mangano, K. M. (2021) · Nutrients · doi:10.3390/nu13030743 · Cited by 95
β-Blockade and Growth Hormone After Burn
Hart, D. W., Wolf, S. E., Chinkes, D. L., Lal, S. O., Ramzy, P. I., & Herndon, D. N. (2002) · Annals of Surgery · doi:10.1097/00000658-200210000-00007 · Cited by 83
“The blood concentration of unlabeled phenylalanine was determined by gas chromatography-mass spectrometry (GCMS) using the internal standard approach and the nitrogen-acetol-n-propyl esters, as previously described.(29) The isotopic enrichment of free amino acids in blood was determined on a HP model 5989 (Hewlett-Pac…”
MethodStimulation of muscle anabolism by resistance exercise and ingestion of leucine plus protein
Tipton, K. D., Elliott, T. A., Ferrando, A. A., Aarsland, A. A., & Wolfe, R. R. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-006 · Cited by 84
“As opposed to resistance exercise in rats (Hernandez et al. 2000; Kubica et al. 2005) and humans (Biolo et al. 1995b; Phillips et al. 1997), muscle protein synthesis is inhibited by the exercise model used by Anthony and colleagues (Anthony et al. 1999, 2000b; Gautsch et al. 1998).”
BackgroundMethodInfluentialSelf-citation
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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