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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Self-citationHuman soleus muscle protein synthesis following resistance exercise
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Pasiakos, S. M., & Carbone, J. W. (2014) · IUBMB Life · doi:10.1002/iub.1291 · Cited by 79
“Similar acute proteolytic responses to resistance exercise have been reported by others using the AV balance approach (52,53).”
Serra, C., Sandor, N. L., Jang, H., Lee, D. C., Toraldo, G., Guarneri, T., Wong, S., Zhang, A., Guo, W., Jasuja, R., et al. (2013) · Endocrinology · doi:10.1210/en.2013-1004 · Cited by 75
“Anabolic stimuli, such as mechanical loading and nutrient supplementation, increase muscle mass by augmenting net protein balance (3), whereas catabolic stimuli, such as starvation (4) and mechanical unloading (5), induce rapid muscle atrophy, which is mediated by the ubiquitin (Ub)-proteasome system (UPS) and by the…”
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“160 The oxidation rate of branched-chain amino acids in elderly individuals is also increased by endurance 161–163 and resistance exercise, 164,165 as is the anabolic response to leucine, again suggesting that both anabolic and catabolic stimuli are necessary to obtain maximum benefit from…”
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Optimizing the Benefits of Exercise on Physical Function in Older Adults
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“Acute bouts of resistance exercise indeed stimulate muscle protein synthesis [68]; however, in the absence of postexercise feeding, myofibrillar synthesis is minimized due to concomitant increases in protein degradation [69].”
BackgroundFerrando, A. A., Wolfe, R. R., Hirsch, K. R., Church, D. D., Kviatkovsky, S. A., Roberts, M. D., Stout, J. R., Gonzalez, D. E., Sowinski, R. J., Kreider, R. B., et al. (2023) · Journal of the International Society of Sports Nutrition · doi:10.1080/15502783.2023.2263409 · Cited by 69
“When the same resistance exercise was performed without amino acid administration, there was both an increase in inward transport of amino acids as well as muscle protein synthesis; however, net muscle balance remained negative [66].”
Self-citationTipton, K. D., Jeukendrup, A. E., & Hespel, P. (2007) · Journal of Sports Sciences · doi:10.1080/02640410701607205 · Cited by 56
Self-citationMechanisms of malnutrition in uremia
Guarnieri, G., Antonione, R., & Biolo, G. (2003) · Journal of Renal Nutrition · doi:10.1053/jren.2003.50020 · Cited by 55
Self-citationMorgan, P. T., Harris, D. O., Marshall, R. N., Quinlan, J. I., Edwards, S. J., Allen, S., & Breen, L. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab055 · Cited by 57
“(1) Data were uploaded into RevMan (Review Manager, v5.”
MethodImpact of protein coingestion on muscle protein synthesis during continuous endurance type exercise
Beelen, M., Zorenc, A., Pennings, B., Senden, J. M., Kuipers, H., & van Loon, L. J. C. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00446.2010 · Cited by 54
“muscle protein synthesis (4, 32, 36, 41) and breakdown (4, 32,”
BackgroundMaking muscles "stronger": exercise, nutrition, drugs.
Aagaard, P. (2004) · PubMed · Cited by 53
Lang, F., Khaghani-Razi-Abad, S., Türk, C., Wiederstein, J. L., Hölper, S., Piller, T., Nogara, L., Blaauw, B., Günther, S., Müller, S., et al. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00093 · Cited by 54
Effects of voluntary wheel running and amino acid supplementation on skeletal muscle of mice
Pellegrino, M. A., Brocca, L., Dioguardi, F. S., Bottinelli, R., & D’Antona, G. (2004) · European Journal of Applied Physiology · doi:10.1007/s00421-004-1237-8 · Cited by 56
“…and both oral (Tipton et al. 1999) and intravenous (Biolo et al. 1997) amino acid supplementation during the early recovery from resistance exercise promotes muscle hypertrophy (Biolo et al. 1995; Rasmussen et al. 2000; Blomstrand and Saltin 2001; Esmarck et al. 2001; Levenhagen et al. 2002).”
BackgroundInsulin but not growth hormone stimulates protein anabolism in skin wound and muscle
Zhang, X., Chinkes, D. L., Wolf, S. E., & Wolfe, R. R. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.276.4.e712 · Cited by 54
“The same mechanism may be applicable to leg Phe uptake, as in our previous studies in resting human volunteers we have found significant correlations between leg blood low and inward AA transport and between blood flow and protein synthesis (6, 7).”
ResultSelf-citationUse of stable isotopically labeled tracers for studies of metabolic kinetics: An overview
Patterson, B. W. (1997) · Metabolism · doi:10.1016/s0026-0495(97)90260-2 · Cited by 54
Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism
McKendry, J., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200029 · Cited by 78
Pasiakos, S. M., & McClung, J. P. (2011) · Nutrition Reviews · doi:10.1111/j.1753-4887.2011.00420.x · Cited by 53
Tessari, P., Zanetti, M., Barazzoni, R., Vettore, M., & Michielan, F. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118923 · Cited by 53
Alcantara, J. M. A., Sanchez-Delgado, G., Martinez-Tellez, B., Labayen, I., & Ruiz, J. R. (2019) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-019-0288-5 · Cited by 47
“When the rates of muscle protein synthesis and degradation increase [6, 7], an adequate nutrition is required [8– 10] to facilitate the recovery process.”
BackgroundDietary protein and exercise training in ageing
Koopman, R. (2011) · Proceedings of The Nutrition Society · doi:10.1017/s0029665110003927 · Cited by 50
“Muscle protein breakdown is also stimulated following exercise, albeit to a lesser extent than protein synthesis((52,55)), and results in an improved net muscle protein balance that persists for up to 48 h in untrained individuals((52)).”
Parise, G., & Yarasheski, K. E. (2000) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200011000-00012 · Cited by 51
Forslund, A. H., Hambræus, L., van Beurden, H., Holmbäck, U. C., El-Khoury, A. E., Hjorth, G., Olsson, R., Stridsberg, M., WIDE, L. E., Åkerfeldt, T., et al. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.5.e857 · Cited by 52
“Finally, resistance exercise, at least, accelerates amino acid transport (5), and it is possible that the 24-h plasma amino acid patterns observed here were modulated by the exercise periods that each subject experienced during the six days before and on day 7 of the 24-h metabolic study.”
BackgroundDietary protein requirements in athletes
Lemon, P. W. R. (1997) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(97)00007-7 · Cited by 50
Fedele, M. J., Hernandez, J. M., Lang, C. H., Vary, T. C., Kimball, S. R., Jefferson, L. S., & Farrell, P. A. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.1.102 · Cited by 50
“Elevations in rates of protein synthesis are consistently observed using not only our model (16–18, 21, 22) but also other models of resistance exercise (7, 8, 53, 54).”
BackgroundSpecificity and context in post-exercise recovery: it is not a one-size-fits-all approach
Minett, G. M., & Costello, J. T. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00130 · Cited by 49
“…resistance training stresses different pathways, maladaptation reported could be resultant of delayed amino acid delivery with blood flow changes (Biolo et al., 1995), or altered macrophage activity and a lesser growth factor concentrations as a result of cold training stimulus and recovery…”
BackgroundAbe, T., Beekley, M. D., Hinata, S., Koizumi, K., & Sato, Y. (2005) · International Journal of KAATSU Training Research · doi:10.3806/ijktr.1.71 · Cited by 49
“However, a single bout of high intensity resistance exercise in humans results in small but significant increases in synthesis of muscle protein, i.e. a hypertrophic response [Biolo et al., 1995; Phillips et al., 1999].”
BackgroundMethodHolm, L., Esmarck, B., Mizuno, M., Hansen, H., Suetta, C., Hölmich, P., Krogsgaard, M. R., & Kjær, M. (2006) · Journal of Orthopaedic Research® · doi:10.1002/jor.20147 · Cited by 50
“Studies have shown that the muscle appear to favor the synthetic processes if amino acids are supplied in demanded amounts.(46,47) Hence, muscles with higher turnover rates are more susceptible for changes in amino acid availability during recovery than muscles with lower turnover rates.”
BackgroundAttenuating Muscle Mass Loss in Critical Illness: the Role of Nutrition and Exercise
Chapple, L. S., Parry, S. M., & Schaller, S. J. (2022) · Current Osteoporosis Reports · doi:10.1007/s11914-022-00746-7 · Cited by 50
Understanding Muscle Protein Dynamics: Technical Considerations for Advancing Sarcopenia Research
Kim, I., Park, S., Jang, J., & Wolfe, R. R. (2020) · Annals of Geriatric Medicine and Research · doi:10.4235/agmr.20.0041 · Cited by 49
Self-citationStefanetti, R. J., Zacharewicz, E., Gatta, P. A. D., GARNHAM, A. P., Russell, A. P., & Lamon, S. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00030 · Cited by 48
“However, MPB also increases following RE, albeit to a lesser extent and of a shorter-lived duration than MPS (Biolo et al., 1995; Phillips et al., 1997).”
BackgroundInfluentialCarbone, J. W., Pasiakos, S. M., Vislocky, L. M., Anderson, J. M., & Rodriguez, N. R. (2014) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2013-0433 · Cited by 49
“2010a), it has been repeatedly shown that acute exercise induces a net catabolic effect in terms of muscle protein turnover (Biolo et al. 1995; Norton and Layman 2006; Tipton et al. 1999).”
BackgroundEffects of Amino Acid Intake on Anabolic Processes
Wolfe, R. R. (2001) · Canadian Journal of Applied Physiology · doi:10.1139/h2001-056 · Cited by 46
Self-citationMacronutrient intake and whole body protein metabolism following resistance exercise
Roy, B. D., Fowles, J. R., Robert, H. I. L. L., & Tarnopolsky, M. A. (2000) · Medicine & Science in Sports & Exercise · doi:10.1097/00005768-200008000-00009 · Cited by 46
“net protein balance in individuals in the fasted state (4,23).”
BackgroundWhey Protein Does Not Enhance the Adaptations to Elbow Flexor Resistance Training
ERSKINE, R. M., FLETCHER, G., HANSON, B., & FOLLAND, J. P. (2012) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318256c48d · Cited by 45
Herndon, D. N., Dasu, M. R. K., Wolfe, R. R., & Barrow, R. E. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00508.2002 · Cited by 44
“The blood levels of unlabeled phenylalanine and its isotope were determined by gas chromatography-mass spectrometry as previously described (6, 7).”
MethodSelf-citationMcKendry, J., Coletta, G., Nunes, E. A., Lim, C., & Phillips, S. M. (2024) · Experimental Physiology · doi:10.1113/ep091937 · Cited by 47
Dickinson, J. M., Lee, J. D., Sullivan, B. E., Harber, M. P., Trappe, S. W., & Trappe, T. A. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00905.2009 · Cited by 45
“Monitoring changes in the rate of muscle protein synthesis in response to a given stimulus can provide important insight into the adaptive state of skeletal muscle (5, 21).”
BackgroundResultRen, G., Yi, S., Zhang, H., & Wang, J. (2017) · Food & Function · doi:10.1039/c6fo01692h · Cited by 46
Vangsoe, M., Joergensen, M., Heckmann, L.-H., & Hansen, M. (2018) · Nutrients · doi:10.3390/nu10030335 · Cited by 44
Wilborn, C., Taylor, L. W., Outlaw, J. J., Williams, L., Campbell, B. I., Foster, C. A., Smith‐Ryan, A. E., Urbina, S. L., & Hayward, S. E. (2013) · PubMed Central · Cited by 45
ENGELEN, M. P. K. J., Deutz, N. E. P., Mostert, R., Wouters, E. F. �., & Schols, A. M. W. J. (2003) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/77.4.868 · Cited by 44
“resulted from an increased transport of amino acids into skeletal muscle (29) and to skeletal muscle proteolysis immediately after exercise (29, 34).”
BackgroundMuscle wasting and protein metabolism1
Castañeda, C. (2002) · Journal of Animal Science · doi:10.2527/animalsci2002.80e-suppl_2e98x · Cited by 45
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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