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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Citations
Cites
Hemodynamic actions of insulin
Baron, A. (1994) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1994.267.2.e187 · Cited by 611 · cited 1×
“The importance of blood flow in determining substrate uptake by tissues has been already shown for glucose (1).”
BackgroundRadioactive and Stable Isotope Tracers in Biomedicine: Principles and Practice of Kinetic Analysis
Wolfe, R. R. (1992) · Medical Entomology and Zoology · Cited by 610
Self-citationChanges in human muscle protein synthesis after resistance exercise
Chesley, A., MacDougall, J. D., Tarnopolsky, M. A., Atkinson, S. A., & Smith, K. (1992) · Journal of Applied Physiology · doi:10.1152/jappl.1992.73.4.1383 · Cited by 436 · cited 2×
“The leucine tracer incorporation technique has shown that the rate of muscle protein synthesis in humans is increased after exercise (6, 7) and remains elevated for > 24 h (7).”
BackgroundResultEffect of Exercise on Protein Turnover in Man
Rennie, M. J., Edwards, R. H. T., Krywawych, S., Davies, C., Halliday, D., Waterlow, J. C., & Millward, D. J. (1981) · Clinical Science · doi:10.1042/cs0610627 · Cited by 309
Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle
Biolo, G., Fleming, R. Y., Maggi, S. P., & Wolfe, R. R. (1995) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1995.268.1.e75 · Cited by 287 · cited 10×
“Blood samples from the femoral and arterialized wrist veins were collected to measure indocyanine green concentration in serum, as described elsewhere (2).”
BackgroundMethodInfluentialSelf-citationEffect of exercise and recovery on muscle protein synthesis in human subjects
Carraro, F., Stuart, C. A., Hartl, W. H., Rosenblatt, J., & Wolfe, R. R. (1990) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1990.259.4.e470 · Cited by 247 · cited 4×
“The leucine tracer incorporation technique has shown that the rate of muscle protein synthesis in humans is increased after exercise (6, 7) and remains elevated for > 24 h (7).”
BackgroundInfluentialSelf-citation3 The Metabolic Effects of Exercise-Induced Muscle Damage
Evans, W. J., & Cannon, J. G. (1991) · Exercise and Sport Sciences Reviews · doi:10.1249/00003677-199101000-00003 · Cited by 230
Structural changes in skeletal muscle tissue with heavy-resistance exercise
Lüthi, J., Howald*, H., Claassen, H., Rösler, K., Vock**, P., & Hoppeler, H. (1986) · International Journal of Sports Medicine · doi:10.1055/s-2008-1025748 · Cited by 221 · cited 1×
“Furthermore the increase in skeletal muscle size with resistance exercise training represents a fundamental biologic adaptation to an increased workload (16, 17).”
BackgroundRennie, M. J., & Millward, D. J. (1983) · Clinical Science · doi:10.1042/cs0650217 · Cited by 198
Effect of exercise on synthesis and degradation of muscle protein
Dohm, G. L., Kasperek, G. J., Tapscott, E. B., & Beecher, G. R. (1980) · Biochemical Journal · doi:10.1042/bj1880255 · Cited by 145
Research works printed but not linked: 10
- Baron A. D, 1994, Metab. 30), E187
- Biolo G., 1995, Metab. 31), E75
- Bylund-Fellenius A. C., Am. J. Physiol., 246
- Carraro F., 1990, Metab. 21), E821
- Carraro F., 1990, Metab. 22), E470
- Devlin J. T., 1990, Metab. 21), E249
- Evans W. J., Exercise Sport Sci. Rev., 19, 99
- MacDougall J. D, 1986, IL: Human Kinetics, 269
- Wolfe R. R, 1986, CA: Sot. Crit. Care Med., 7, 19
- Zorzano A., 1985, Metab. 11), E546
Cited by
Sorted by citations
Items 301–400 of 708
Protein Synthesis and Antioxidant Capacity in Aging Mice: Effects of Long‐Term Voluntary Exercise
Vaanholt, L. M., Speakman, J. R., Garland, T., Lobley, G. E., & Visser, G. H. (2008) · Physiological and Biochemical Zoology · doi:10.1086/525289 · Cited by 42
Hoffman, J. R., Stout, J. R., Williams, D. R., Wells, A. J., Fragala, M. S., Mangine, G. T., Gonzalez, A. M., Emerson, N. S., McCormack, W. P., Scanlon, T. C., et al. (2012) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-9-47 · Cited by 43
“The mechanical stimulus of resistance training has been demonstrated to be a potent stimulus for increasing protein synthesis [23,24].”
BackgroundIs There a Need for Protein Ingestion During Exercise?
van Loon, L. J. C. (2014) · Sports Medicine · doi:10.1007/s40279-014-0156-z · Cited by 48
“Physical activity (or exercise) directly stimulates skeletal muscle protein synthesis [4–6], an effect that has been shown to persist for up to 48 h after the cessation of exercise [6].”
BackgroundKitaoka, Y., Nakazato, K., & Ogasawara, R. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00465.2016 · Cited by 43
“Although resistance exercise results in marked increases muscle protein synthesis, the net protein balance remains negative in the absence of feeding because there is a concomitant increase in protein breakdown; the net balance becomes positive when amino acids are provided orally (3, 46).”
BackgroundFACTS AND FALLACIES OF PURPORTED ERGOGENIC AMINO ACID SUPPLEMENTS
Williams, M. H. (1999) · Clinics in Sports Medicine · doi:10.1016/s0278-5919(05)70173-3 · Cited by 45
Resistance exercise enhances long-term mTORC1 sensitivity to leucine
D'Hulst, G., Masschelein, E., & De Bock, K. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101615 · Cited by 42
“Exercise acutely increases amino acid uptake in the muscle [2,44], but whether this effect is still present 48 h after exercise cessation, and how it is related to mTORC1 activation, is unknown.”
BackgroundIncreased Protein Requirements in Female Athletes after Variable-Intensity Exercise
WOODING, D. J., PACKER, J. E., KATO, H., WEST, D. W. D., COURTNEY-MARTIN, G., PENCHARZ, P. B., & MOORE, D. R. (2017) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001366 · Cited by 42
Bosco, F., Musolino, V., Gliozzi, M., Nucera, S., Carresi, C., Zito, M. C., Scarano, F., Scicchitano, M., Reale, F., Ruga, S., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105427 · Cited by 47
Moberg, M., Apró, W., Ohlsson, I., Pontén, M., Villanueva, A., Ekblom, B. T., & Blomstrand, E. (2013) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2013-0244 · Cited by 46
“Even a single session of resistance exercise enhances the rate of protein synthesis significantly; however, also the rate of degradation increases, although to a lesser extent, resulting in an improved net balance (Biolo et al. 1995; Phillips et al. 1997).”
BackgroundLeg glucose and protein metabolism during an acute bout of resistance exercise in humans
Durham, W. J., Miller, S. L., Yeckel, C. W., Chinkes, D. L., Tipton, K. D., Rasmussen, B. B., & Wolfe, R. R. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00635.2003 · Cited by 43
“Support for this scenario comes from the high correlation between inward and outward amino acid transport (8, 9, 11).”
BackgroundSelf-citationNutritional Strategies to Combat Type 2 Diabetes in Aging Adults: The Importance of Protein
Beaudry, K. M., & Devries, M. C. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00138 · Cited by 41
“In the fasted state, rates of MPB exceed MPS, resulting in negative protein balance in skeletal muscle (26).”
BackgroundMulazzani, G., Corti, F., Valle, S. D., & Bartolomeo, M. D. (2021) · Nutrients · doi:10.3390/nu13082766 · Cited by 42
“Resistance exercise promotes muscle protein synthesis [85,86]; the stimulatory effect on protein synthesis exerted by exogenous amino acids”
BackgroundRoy, B. D., Luttmer, K., Bosman, M. J., & Tarnopolsky, M. A. (2002) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.12.2.172 · Cited by 44
Nutritional Considerations for the Vegan Athlete
West, S., Monteyne, A. J., van der Heijden, I., Stephens, F. B., & Wall, B. T. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.04.012 · Cited by 42
Ackerman, K. E., Rogers, M. A., Heikura, I. A., Burke, L. M., Stellingwerff, T., Hackney, A. C., Verhagen, E., Schley, S., Saville, G. H., Mountjoy, M., et al. (2023) · British Journal of Sports Medicine · doi:10.1136/bjsports-2023-107359 · Cited by 43
Wilkinson, K., Koscien, C. P., Monteyne, A. J., Wall, B. T., & Stephens, F. B. (2023) · Physiological Reports · doi:10.14814/phy2.15775 · Cited by 44
“However, resistance exercise also stimulates muscle protein breakdown (MPB) rates such that, in the postabsorptive state, muscle protein net balance remains negative (Biolo et al., 1995).”
BackgroundAge-Associated Differences in Recovery from Exercise-Induced Muscle Damage
Li, D. C. W., Rudloff, S., Langer, H. T., Norman, K., & Herpich, C. (2024) · Cells · doi:10.3390/cells13030255 · Cited by 45
“An acute bout of RE is known to increase MPS rates by ~100% in untrained individuals [71].”
Improving muscle mass and function in cachexia
Maddocks, M. M., Murton, A. J., & Wilcock, A. (2011) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e32834bdde3 · Cited by 41
Acute resistance exercise augments integrative myofibrillar protein synthesis
Gasier, H. G., Fluckey, J. D., Previs, S. F., Wiggs, M. P., & Riechman, S. E. (2011) · Metabolism · doi:10.1016/j.metabol.2011.07.001 · Cited by 43
“[1] Biolo G, Maggi SP, Williams BD, et al.”
BackgroundParker, B. L., Kiens, B., Wojtaszewski, J. F. P., Richter, E. A., & James, D. E. (2020) · The FASEB Journal · doi:10.1096/fj.202000075r · Cited by 39
Hermans, W. J. H., Fuchs, C. J., Hendriks, F. K., Houben, L. H. P., Senden, J. M., Verdijk, L. B., & van Loon, L. J. C. (2022) · Journal of Nutrition · doi:10.1093/jn/nxac007 · Cited by 39
“Exercise performed prior to food ingestion augments the postprandial increase in muscle protein synthesis rates and allows more of the protein-derived amino acids to be used for de novo muscle protein synthesis (2, 4, 42).”
MethodNutrition for Acute Exercise-Induced Injuries
Tipton, K. D. (2010) · Annals of Nutrition and Metabolism · doi:10.1159/000322703 · Cited by 40
Self-citationProtein Intake for Skeletal Muscle Hypertrophy with Resistance Training in Seniors
Andrews, R. D., MacLean, D. A., & Riechman, S. E. (2006) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.16.4.362 · Cited by 38
“RET induces amino acid mobilization from the body’s free amino acid pool during recovery from an acute bout of resistance training, emphasizing the role of amino acids and their use during an increased anabolic period (3).”
BackgroundKakigi, R., Yoshihara, T., Ozaki, H., Ogura, Y., Ichinoseki‐Sekine, N., Kobayashi, H., & Naıto, H. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2812-7 · Cited by 41
Seino, S., Sumi, K., Narita, M., Yokoyama, Y., Ashida, K., Kitamura, A., & Shinkai, S. (2017) · The journal of nutrition health & aging · doi:10.1007/s12603-017-0904-5 · Cited by 39
“A single session of resistance exercise (RE) increases MPS and MPB (3) and anabolic sensitivity to feeding (4).”
Williamson, E., & Moore, D. R. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.640621 · Cited by 42
“With the contraction-induced anabolic stimulus of resistance exercise there is an increase in MPB, although this primarily serves to provide AA precursors to support MPS in the fasted state (39, 40).”
BackgroundDavis, J.-K., Oikawa, S. Y., Halson, S. L., Stephens, J., O’Riordan, S. F., Luhrs, K., Sopeña, B. C., & Baker, L. B. (2021) · Sports Medicine · doi:10.1007/s40279-021-01606-7 · Cited by 82
“Exercise and protein ingestion are the two main anabolic stimuli responsible for increasing rates of MPS, where ingestion of protein in close temporal proximity to exercise results in greater stimulation of MPS than either stimulus independently [145].”
BackgroundExercise as an Anabolic Intervention in Patients With End-Stage Renal Disease
Ikizler, T. A. (2011) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2010.10.012 · Cited by 39
“Also, although exercise has a direct stimulatory effect on the rate of muscle protein synthesis, the rate of muscle protein breakdown is also increased as a consequence of exercise, thereby blunting the extent to which net balance between synthesis and breakdown is improved.(11,12) Multiple studies demonstrated that r…”
BackgroundEfficacy of strength training on tension-type headache: A randomised controlled study
Madsen, B. K., Søgaard, K., Andersen, L. L., Tornøe, B., & Jensen, R. (2017) · Cephalalgia · doi:10.1177/0333102417722521 · Cited by 37
In vivo muscle amino acid transport involves two distinct processes
Miller, S. L., Chinkes, D. L., MacLean, D. A., Gore, D. C., & Wolfe, R. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00092.2004 · Cited by 37
“Thus, after resistance exercise, muscle blood flow is increased and amino acid exchange between muscle and blood is also accelerated (3).”
BackgroundSelf-citationSupplements and the Endocrine System in Athletes
Di Luigi, L. (2008) · Clinics in Sports Medicine · doi:10.1016/j.csm.2007.09.003 · Cited by 43
Hayasaka, M., Tsunekawa, H., Yoshinaga, M., & Murakami, T. (2014) · Physiological Reports · doi:10.14814/phy2.12254 · Cited by 36
“Because protein synthesis has been shown to increase after a bout of exercise (Biolo et al. 1995), REDD1 could be a transient, yet potent inhibitor of mTORC1 during exercise.”
BackgroundEffects of aging and lifelong aerobic exercise on basal and exercise-induced inflammation in women
Lavin, K. M., Perkins, R. K., Jemioło, B., Raue, U., Trappe, S. W., & Trappe, T. A. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00655.2020 · Cited by 36
“Timely initiation and subsequent resolution of inflammation (7) facilitate protein accretion at the crux of long-term muscle hypertrophy (5, 53), a key outcome of resistance exercise training that may forestall or reverse the effects of aging.”
BackgroundSzewczyk, N. J., Peterson, B. K., & Jacobson, L. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4181-4188.2002 · Cited by 35
“Protein degradation in skeletal muscle is increased by heavy exercise (5, 12, 24, 36), which also promotes an increase in MAPK activation (40, 57, 58).”
BackgroundOlympic Textbook of Medicine in Sport
Schwellnus, M. P., Komitee, I. O., & International Federation of Sportive Medicine (2008) · Wiley eBooks · doi:10.1002/9781444300635 · Cited by 42
“Protein synthesis depends on amino acid availability and transport (Biolo et al. 1995), post-translational modifications (Jefferson & Kimball 2001), timing of intake (Tipton et al. 2001), insulin concentrations (Biolo et al. 1999), and other factors such as anabolic hormonal regulation (e.g.,…”
BackgroundThe Effects of Acute Passive Stretch on Muscle Protein Synthesis in Humans
Fowles, J. R., MacDOUGALL, J. D., Tarnopolsky, M. A., SALE, D. G., Roy, B. D., & Yarasheski, K. E. (2000) · Canadian Journal of Applied Physiology · doi:10.1139/h00-012 · Cited by 36
Kreider, R. B., Earnest, C. P., Lundberg, J., Rasmussen, C., Greenwood, M., Cowan, P., & Almada, A. L. (2007) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-4-18 · Cited by 35
“Others studies have reported that the provision of PRO or amino acids prior to and/or following exercise stimulates PRO synthesis [3,12,16-22].”
BackgroundDietary Protein for Muscle Hypertrophy
Tipton, K. D., & Phillips, S. M. (2013) · Nestlé Nutrition Institute Workshop Series · doi:10.1159/000350259 · Cited by 49
Self-citationMitigation of Muscle Loss in Stressed Physiology: Military Relevance
Church, D. D., Gwin, J. A., Wolfe, R. R., Pasiakos, S. M., & Ferrando, A. A. (2019) · Nutrients · doi:10.3390/nu11081703 · Cited by 35
“For example, resistance exercise increases protein turnover and results in a less negative NB in healthy, normal humans [21].”
BackgroundSelf-citationJoanisse, S., McKendry, J., Lim, C., Nunes, E. A., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Clinical Nutrition Open Science · doi:10.1016/j.nutos.2021.01.005 · Cited by 41
Aussieker, T., Hilkens, L., Holwerda, A. M., Fuchs, C. J., Houben, L. H. P., Senden, J. M., van Dijk, J., Snijders, T., & van Loon, L. J. C. (2023) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000003214 · Cited by 38
Amino Acid Supplementation Affects Hematological and Biochemical Parameters in Elite Rugby Players
Ohtani, M., Maruyama, K., Sugita, M., & Kobayashi, K. (2001) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.65.1970 · Cited by 36
Wall, B. T., Burd, N. A., Franssen, R., Gorissen, S. H. M., Snijders, T., Senden, J. M., Gijsen, A. P., & van Loon, L. J. C. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00325.2016 · Cited by 34
“A single bout of resistance-type exercise 54 increases both muscle protein synthesis and breakdown rates, albeit the latter to a lesser extent 55 (2, 31).”
BackgroundSynergistic effects of resistance training and protein intake: Practical aspects
Guimarães-Ferreira, L., Cholewa, J. M., Naimo, M. A., Zhi, X. I. A., Magagnin, D., Dal Ponte de Sá, R. B., Streck, E. L., da Silva Teixeira, T., & Zanchi, N. E. (2014) · Nutrition · doi:10.1016/j.nut.2013.12.017 · Cited by 34
Ivy, J. L., Ding, Z., Hwang, H., Cialdella-Kam, L. C., & Morrison, P. J. (2008) · Amino Acids · doi:10.1007/s00726-007-0620-2 · Cited by 52
Resistance Exercise’s Ability to Reverse Cancer-Induced Anabolic Resistance
Montalvo, R. N., Hardee, J. P., VanderVeen, B. N., & Carson, J. A. (2018) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000159 · Cited by 34
Equivalent Hypertrophy and Strength Gains in β-Hydroxy-β-Methylbutyrate- or Leucine-supplemented Men
JAKUBOWSKI, J. S., WONG, E. P. T., NUNES, E. A., NOGUCHI, K. S., VANDEWEERD, J. K., MURPHY, K. T., MORTON, R. W., MCGLORY, C., & PHILLIPS, S. M. (2019) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001752 · Cited by 34
Webster, J. M., Fenton, C. G., LANGEN, R. C. J., & Hardy, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225768 · Cited by 36
Okamura, K., Doi, T., Hamada, K., Sakurai, M., Matsumoto, K., Imaizumi, K., Yoshioka, Y., Shimizu, S., & Suzuki, M. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.272.6.e1023 · Cited by 34
Responses of Musculoskeletal Tissues to Disuse and Remobilization
Millis, D. L. (2004) · Elsevier eBooks · doi:10.1016/b978-0-7216-9555-6.50011-5 · Cited by 32
Fielding, R. A., & Parkington, J. D. (2002) · Nutrition in Clinical Care · doi:10.1046/j.1523-5408.2002.00606.x · Cited by 34
Hanson, E. D., Nelson, A. R., West, D. W. D., Violet, J. A., O’Keefe, L., Phillips, S. M., & Hayes, A. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3383 · Cited by 34
“Hyperaminoacidemia and testosterone independently increase MPS with no change in MPB (34, 35), whereas resistance exercise increases bothMPS andMBP (36).”
BackgroundProtein Intake Does Not Increase Vastus Lateralis Muscle Protein Synthesis during Cycling
HULSTON, C. J., WOLSK, E., GRØNDAHL, T. S., YFANTI, C., & VAN HALL, G. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31821661ab · Cited by 32
Exercise and Regulation of Protein Metabolism
Atherton, P. J., Phillips, B. E., & Wilkinson, D. J. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.06.015 · Cited by 36
Hendriks, F. K., Smeets, J. S. J., SANDE, F. M. V. D., Kooman, J. P., & van Loon, L. J. C. (2019) · Nutrients · doi:10.3390/nu11122972 · Cited by 35
“being elevated for up to 24 or even 48 h [76,77].”
BackgroundFarrell, P. A., Fedele, M. J., Vary, T. C., Kimball, S. R., & Jefferson, L. S. (1998) · Journal of Applied Physiology · doi:10.1152/jappl.1998.85.6.2291 · Cited by 32
“CONTROLLERS OF ANABOLIC PATHWAYS must be upregulated after resistance exercise, since rates of protein synthesis are elevated at this time (3, 10, 40, 41, 43).”
BackgroundBlomstrand, E., & Essén-Gustavsson, B. (2008) · Amino Acids · doi:10.1007/s00726-008-0182-y · Cited by 34
The metabolic and temporal basis of muscle hypertrophy in response to resistance exercise
Brook, M. S., Wilkinson, D. J., Smith, K., & Atherton, P. J. (2015) · European Journal of Sport Science · doi:10.1080/17461391.2015.1073362 · Cited by 36
Muscle proteins during 60‐day bedrest in women: Impact of exercise or nutrition
LeMoine, J. K., Haus, J. M., Trappe, S. W., & Trappe, T. A. (2009) · Muscle & Nerve · doi:10.1002/mus.21189 · Cited by 32
Morrison, P. J., Hara, D., Ding, Z., & Ivy, J. L. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01173.2007 · Cited by 32
“Whole body protein synthesis rates have been shown to increase by 200% with the infusion of amino acids after resistance-type exercise (4), much greater than the 100% increase found without amino acid supplementation (3).”
BackgroundEffect of Specific Resistance Training on Musculoskeletal Pain Symptoms
Pedersen, M. T., Andersen, L. L., Jørgensen, M. B., Søgaard, K., & Sjøgaard, G. (2012) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e3182541ceb · Cited by 31
“The doseresponse relationship found between dose of training and pain in this study may be attributable to the increased reserve capacity of muscle strength (5), a rebuilding of muscle cells by an increased protein synthesis and degradation (6), and a normalization of homeostasis because of an increased muscle tissue…”
The mechanistic and ergogenic effects of phosphatidic acid in skeletal muscle
Shad, B. J., Smeuninx, B., Atherton, P. J., & Breen, L. (2015) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2015-0350 · Cited by 33
“asmuscle atrophy (Biolo et al. 1995b).”
BackgroundDeane, C. S., Ely, I. A., Wilkinson, D. J., Smith, K., Phillips, B. E., & Atherton, P. J. (2020) · Proceedings of The Nutrition Society · doi:10.1017/s0029665120007879 · Cited by 38
“This is evidenced by the fact that exercise-induced increases in MPS in the absence of protein/EAA result in a prolonged elevation in MPB, therein contributing to an overall negative muscle protein balance((64)).”
BackgroundSmeuninx, B., Elhassan, Y., Sapey, E., Rushton, A. B., Morgan, P. T., Korzepa, M., Belfield, A. E., Philp, A., Brook, M. S., Gharahdaghi, N., et al. (2023) · The Journal of Physiology · doi:10.1113/jp285130 · Cited by 31
“RE can robustly increase aMyoPS in both the postabsorptive (Biolo et al., 1995; Kumar et al., 2012) and the postprandial state through increasing the utilization of dietary-derived amino acids (Pennings et al., 2011; Yang et al., 2012).”
Luiking, Y. C., Engelen, M. P. K. J., Soeters, P. B., Boirie, Y., & Deutz, N. E. P. (2011) · Clinical Nutrition · doi:10.1016/j.clnu.2010.06.012 · Cited by 30
“min)] and calculated according to formula (3) by multiplying the mean plasma flow (within the group) with the difference between venous and arterial plasma concentration across the organ, [V] and [A], respectively.”
MethodReitelseder, S., Agergaard, J., Doessing, S., Helmark, I. C., Schjerling, P., van Hall, G., Kjær, M., & Holm, L. (2013) · European Journal of Nutrition · doi:10.1007/s00394-013-0530-x · Cited by 32
“Several studies have documented that the positive regulation of muscle protein NB after exercise and amino acid/protein supplementation primarily are based on increased MPS with MPB being unchanged or only slightly elevated [1, 4, 9, 10, 30, 48, 49].”
BackgroundResultCan muscle typology explain the inter‐individual variability in resistance training adaptations?
Vossel, K. V., Hardeel, J., de Casteele, F. V., der Stede, T. V., Weyns, A., Boone, J., Blemker, S. S., Lievens, E., & Derave, W. (2023) · The Journal of Physiology · doi:10.1113/jp284442 · Cited by 35
“Post-exercise muscle blood flow is known to be an important contributor to muscle protein synthesis (Biolo et al., 1995; Fujita et al., 2006; Timmerman et al., 2010), and a suppressed post-exercise blood flow may lead to reduced resistance training adaptations as proposed by post-exercise muscle…”
BackgroundInfluentialLarsen, R. G., Befroy, D. E., & Kent‐Braun, J. A. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00409.2012 · Cited by 31
“Various modes of exercise training have been shown to elevate rates of muscle protein synthesis and breakdown (4, 5, 52, 67), suggesting that exercise may result in elevated ATP demand in resting tissue, which presumably would be reflected by increased oxidative ATP flux.”
BackgroundSnijders, T., Verdijk, L. B., McKay, B. R., Smeets, J. S. J., van Kranenburg, J. M. X., Groen, B. B. L., Parise, G., Greenhaff, P. L., & van Loon, L. J. C. (2013) · Journal of Nutrition · doi:10.3945/jn.113.183996 · Cited by 31
“During post-exercise recovery, dietary protein intake is essential to support the increase in myofibrillar muscle protein synthesis, thereby allowing net muscle protein accretion (10,12,18).”
BackgroundEynon, N., de Oliveira, J. J. F., Meckel, Y., Sagiv, M., Yamin, C., Sagiv, M. S., Amir, R., & Duarte, J. A. (2009) · Experimental Physiology · doi:10.1113/expphysiol.2008.045138 · Cited by 30
“Of particular interest is the influence that endurance exercise has on skeletal muscle metabolic pathways (Biolo et al. 1995), given that skeletal muscle contains 40% of all body protein stores (Rennie & Tipton 2000).”
BackgroundMonteyne, A. J., Coelho, M. O., Porter, C., Abdelrahman, D. R., Jameson, T. S., Finnigan, T. J., Stephens, F. B., Dirks, M. L., & Wall, B. T. (2020) · The Journal of Nutrition · doi:10.1093/jn/nxaa251 · Cited by 29
Escobar, K. A., VanDusseldorp, T. A., & Kerksick, C. M. (2016) · British Journal Of Nutrition · doi:10.1017/s0007114516003949 · Cited by 34
Protein for adaptations to exercise training
Tipton, K. D. (2008) · European Journal of Sport Science · doi:10.1080/17461390801919102 · Cited by 32
“The rate of breakdown of mixed muscle proteins is increased following resistance exercise and related to the increase in muscle protein synthesis (Biolo et al., 1995b; Phillips et al., 1997).”
BackgroundInfluentialSelf-citationCritical variables regulating age-related anabolic responses to protein nutrition in skeletal muscle
Deane, C. S., Cox, J., & Atherton, P. J. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1419229 · Cited by 36
Associations between muscle mass, physical activity and dietary behaviour in adolescents
Hao, G., Pollock, N. K., Harris, R. A., Gutin, B., Su, S., & Wang, X. (2018) · Pediatric Obesity · doi:10.1111/ijpo.12471 · Cited by 28
“Since muscle protein synthesis is accepted to be the dominant process of muscle remodelling (22), many studies investigating the role of dietary nutrients have focused on the effect of protein intake.”
BackgroundHannaian, S. J., Hodson, N. W., Sawan, S. A., Mazzulla, M., Kato, H., Matsunaga, K., Waskiw‐Ford, M., Duncan, J., Kumbhare, D. A., & Moore, D. R. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00241.2020 · Cited by 25
Protein Requirements for Master Athletes: Just Older Versions of Their Younger Selves
Moore, D. R. (2021) · Sports Medicine · doi:10.1007/s40279-021-01510-0 · Cited by 33
“Resistance exercise is an inherently anabolic exercise modality that has been consistently shown to increase muscle protein turnover and attenuate the otherwise negative net muscle protein balance in the rested fasted state [45, 83].”
BackgroundWest, S., Monteyne, A. J., Whelehan, G., van der Heijden, I., Abdelrahman, D. R., Murton, A. J., Finnigan, T. J. A., Stephens, F. B., & Wall, B. T. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00166.2023 · Cited by 33
The effects of short intensive exercise on plasma free amino acids in standardbred trotters
Hackl, S., van den HOVEN, R., Zickl, M., Spona, J., & Zentek, J. (2008) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/j.1439-0396.2007.00801.x · Cited by 29
“Anabolic effects of dietary AA supplementation have been documented in humans (Carli et al., 1992; Chandler et al., 1994; Hammarqvist et al., 1994; Pitkow et al., 1994; Biolo et al., 1995) and can favourably influence recovery after exercise (Carli et al., 1992; Chandler et al., 1994).”
BackgroundAge effect on myocellular remodeling: Response to exercise and nutrition in humans
Irving, B. A., Robinson, M. M., & Nair, K. S. (2011) · Ageing Research Reviews · doi:10.1016/j.arr.2011.11.001 · Cited by 31
“In the postabsorptive state, skeletal muscle protein synthesis is increased following both resistance (Biolo et al., 1995; Chesley et al., 1992; Dreyer et al., 2006; Dreyer et al.; Kim et al., 2005; Kumar et al., 2009b; Phillips et al., 1997; Phillips et al., 1999; Sheffield-Moore et al., 2005) and…”
BackgroundDrummond, M. J., Marcus, R. L., & LaStayo, P. C. (2012) · Journal of Aging Research · doi:10.1155/2012/486930 · Cited by 28
“Resistance exercise acutely stimulates muscle protein synthesis in healthy young human skeletal muscle [32, 33]; a response that has been shown to be elevated at least 48 hours after a single bout of exercise [34].”
BackgroundWhey Protein Ingestion Enhances Postprandial Anabolism during Short-Term Bed Rest in Young Men
Antonione, R., Caliandro, E., Zorat, F., Guarnieri, G., Heer, M. A., & Biolo, G. (2008) · Journal of Nutrition · doi:10.3945/jn.108.086462 · Cited by 30
“Synthesis rate of skeletal muscle protein is upregulated for several hours following exercise (7,8), leading to enhanced anabolic efficiency of dietary proteins (9,10).”
BackgroundInfluentialSelf-citationControl of Muscle Protein Breakdown: Effects of Activity and Nutritional States
Wolfe, R. R. (2001) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.11.s1.s164 · Cited by 28
Self-citationOrmsbee, M. J., Willingham, B. D., Marchant, T. P., Binkley, T. L., SPECKER, B. L., & Vukovich, M. D. (2018) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.2018-0036 · Cited by 29
Neck/shoulder function in tension-type headache patients and the effect of strength training
Madsen, B. K., Søgaard, K., Andersen, L. L., Skotte, J. H., Tornøe, B., & Jensen, R. (2018) · Journal of Pain Research · doi:10.2147/jpr.s146050 · Cited by 27
“The reduction in muscle pain through ST can be influenced by protein synthesis and degradation, which can lead to reconstruction of damaged muscle fiber.(17,19) Furthermore, the increased strength may reduce the relative workload on the muscle in daily life.”
BackgroundRoberson, P. A., Mobley, C. B., Romero, M. A., Haun, C. T., Osburn, S. C., Mumford, P. W., Vann, C. G., Greer, R. A., Ferrando, A. A., & Roberts, M. D. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2020.628405 · Cited by 28
António, J., Evans, C., Ferrando, A. A., Stout, J. R., Antonio, B. B., Cintineo, H. P., Harty, P. S., Arent, S. M., Candow, D. G., Forbes, S. C., et al. (2024) · Journal of the International Society of Sports Nutrition · doi:10.1080/15502783.2024.2341903 · Cited by 35
“…been demonstrated that the delivery matrix and pharmaco-kinetics of EAAs directly affect the stimulation of muscle protein turnover and MPS [208], with simpler administration formats such as free-form EAA and/or free-form protein combinations, resulting in greater EAA delivery and…”
BackgroundIs glucose/amino acid supplementation after exercise an aid to strength training?
Williams, A. G., van den Oord, M. H. A. H., Sharma, A. P., & Jones, D. A. (2001) · British Journal of Sports Medicine · doi:10.1136/bjsm.35.2.109 · Cited by 27
Metabolism of skin and muscle protein is regulated differently in response to nutrition
Zhang, X., Chinkes, D. L., Doyle, D. J., & Wolfe, R. R. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.274.3.e484 · Cited by 27
Self-citationVivo-Morpholinos Induced Transient Knockdown of Physical Activity Related Proteins
Ferguson, D. P., Schmitt, E. E., & Lightfoot, J. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061472 · Cited by 27
“We suspect that due to the high activity of the dopamine system in the brain [50,51,52], there may be a decreased protein turnover rate of Vmat2 in the brain as compared to skeletal muscle [50,53,54,55] resulting in a slower protein turnover rate leading to a slower knockdown time course of Vmat2 in the brain.”
BackgroundOkazaki, K., YAZAWA, D., Goto, M., Kamijo, Y., Furihata, M., Genno, H., Hamada, K., & Nosé, H. (2013) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12076 · Cited by 27
“It has been suggested that amino acid supplementation after exercise has a synergistic effect upon resistance exercise-induced augmentation of muscle protein synthesis when provided both intravenously (Biolo et al., 1995) and orally (Tipton et al.”
BackgroundResultHudson, J., Kim, J. E., Paddon‐Jones, D., & Campbell, W. W. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.158246 · Cited by 26
van der Heijden, I., Monteyne, A. J., West, S., Morton, J. P., Langan‐Evans, C., Hearris, M. A., Abdelrahman, D. R., Murton, A. J., Stephens, F. B., & Wall, B. T. (2024) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000003432 · Cited by 27
Gojda, J., Waldauf, P., Hrušková, N., Blahutová, B., Krajčová, A., Urban, T., Tůma, P., Řasová, K., & Duška, F. (2019) · PLoS ONE · doi:10.1371/journal.pone.0200228 · Cited by 28
Effects of resistance training and protein supplementation on bone turnover in young adult women
Mullins, N. M., & Sinning, W. E. (2005) · Nutrition & Metabolism · doi:10.1186/1743-7075-2-19 · Cited by 26
MacDOUGALL, J. D. (2003) · Wiley eBooks · doi:10.1002/9780470757215.ch13 · Cited by 25
Paoli, A., Cerullo, G., Bianco, A., Neri, M., Gennaro, F., Charrier, D., & Moro, T. (2024) · Journal of Human Kinetics · doi:10.5114/jhk/186660 · Cited by 29
Moon, J. M., Ratliff, K. M., Blumkaitis, J. C., Harty, P. S., Zabriskie, H. A., Stecker, R. A., Currier, B. S., Jagim, A. R., Jäger, R., Purpura, M., et al. (2020) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-020-00394-1 · Cited by 29
“In response to exercise and in the absence of feeding, rates of muscle protein synthesis (MPS) and muscle protein breakdown both increase with the overall net muscle protein balance remaining negative [4].”
BackgroundEven, P. C., Bertin, É., Gangnerau, M.-N., Roseau, S. M., Tomé, D., & Portha, B. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00268.2002 · Cited by 24
Casein Ingestion Does Not Increase Muscle Connective Tissue Protein Synthesis Rates
Trommelen, J., Holwerda, A. M., Senden, J. M., Goessens, J. P. B., van Kranenburg, J. M. X., Gijsen, A. P., Verdijk, L. B., & van Loon, L. J. C. (2020) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000002337 · Cited by 26
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
