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Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men
Abstract
Signaling pathways sense local and systemic signals and regulate muscle hypertrophy. The effects of whey protein ingestion on acute and long-term signaling responses of resistance exercise are not well known. Previously untrained young men were randomized into protein (n = 9), placebo (n = 9), and control (n = 11) groups. Vastus lateralis (VL) muscle biopsies were taken before and 1 h and 48 h after a leg press of 5 x 10 repetitions [resistance exercise (RE)] and after 21 wk (2 times per week) of resistance training (RT). Protein (15 g of whey) or nonenergetic placebo was ingested before and after a single RE bout and each RE workout throughout the RT. The protein group increased its body mass and VL muscle thickness (measured by ultrasonography) already at week 10.5 (P < 0.05). At week 21, the protein and placebo groups had similarly increased their myofiber size. No changes were observed in the nonexercised controls. However, the phosphorylation of p70(S6K) and ribosomal protein S6 (rpS6) were increased at 1 h post-RE measured by Western blotting, the former being the greatest with protein ingestion. Mammalian target of rapamycin (mTOR) phosphorylation was increased after the RE bout and RT only in the protein group, whereas the protein ingestion prevented the post-RE decrease in phosphorylated eukaryotic initiation factor 4E binding protein 1 (p-4E-BP1). Akt phosphorylation decreased after RT, whereas no change was observed in phosphorylated eukaryotic elongation factor 2. A post-RE decrease in muscle myostatin protein occurred only in the placebo group. The results indicate that resistance exercise rapidly increases mTOR signaling and may decrease myostatin protein expression in muscle and that whey protein increases and prolongs the mTOR signaling response.
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“acute increases in mTOR signaling markers following one bout of resistance exercise are associated with muscle hypertrophy following weeks of resistance training (Terzis et al., 2008; Hulmi et al., 2009; Mayhew et al., 2009; Mitchell et al., 2013)”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Hulmi et al., 2009
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Cites
Durnin, J. V. G. A., & Womersley, J. (1974) · British Journal Of Nutrition · doi:10.1079/bjn19740060 · Cited by 6,343
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
A Critical Evaluation of Simple Methods for the Estimation of Free Testosterone in Serum
Vermeulen, A., Verdonck, L., & Kaufman, J. M. (1999) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.84.10.6079 · Cited by 3,824
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
Progression Models in Resistance Training for Healthy Adults
(2002) · Medicine and Science in Sports and Exercise · doi:10.1097/00005768-200202000-00027 · Cited by 2,979
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Pause, A., Belsham, G. J., Gingras, A., Donzé, O., Lin, T.-A., Lawrence, J. C., & Sonenberg, N. (1994) · Nature · doi:10.1038/371762a0 · Cited by 1,242
Skeletal muscle hypertrophy and atrophy signaling pathways
Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106 · cited 1×
“Muscle protein synthesis and hypertrophy are stimulated by the mammalian target of rapamycin (mTOR) pathway protein kinase enzymes that are activated or inactivated by phosphorylation or dephosphorylation at different amino acid sites (13, 28).”
BackgroundRibosomal protein S6 phosphorylation: from protein synthesis to cell size
Ruvinsky, I., & Meyuhas, O. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.04.003 · Cited by 800
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Morton, R. W., Murphy, K. T., McKellar, S. R., Schoenfeld, B. J., Henselmans, M., Helms, E., Aragon, A. A., Devries, M. C., Banfield, L., Krieger, J. W., et al. (2018) · British Journal of Sports Medicine · doi:10.1136/bjsports-2017-097608 · Cited by 1,269
Cermak, N. M., Res, P. T., de Groot, L. C., Saris, W. H., & van Loon, L. J. (2012) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.112.037556 · Cited by 827
Pekkala, S., Wiklund, P. K., Hulmi, J. J., Ahtiainen, J. P., Horttanainen, M., Pöllänen, E., Mäkelä, K. A., Kainulainen, H., Häkkinen, K., Nyman, K., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.263707 · Cited by 292
Myostatin decreases with aerobic exercise and associates with insulin resistance
HITTEL, D. S., AXELSON, M., SARNA, N., SHEARER, J., HUFFMAN, K. M., & KRAUS, W. E. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181e0b9a8 · Cited by 271
“AE and RE reduce muscle and circulating MSTN levels in human subjects whether acute or chronic (11,20,30).”
BackgroundRoberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214
Ribosome biogenesis: Emerging evidence for a central role in the regulation of skeletal muscle mass
Chaillou, T., Kirby, T. J., & McCarthy, J. J. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24604 · Cited by 211
Hulmi, J. J., Lockwood, C. M., & Stout, J. R. (2010) · Nutrition & Metabolism · doi:10.1186/1743-7075-7-51 · Cited by 238
“[20,37] has also reported that combined PRO ingestion and resistance training in previously untrained males, following an ad libitum diet, provides an augmented physiological adaptation to training.”
Sarcopenia in the elderly: basic and clinical issues
Wang, C., & Bai, L. (2012) · Geriatrics & Gerontology International · doi:10.1111/j.1447-0594.2012.00851.x · Cited by 170
Paulsen, G., Hamarsland, H., Cumming, K. T., Johansen, R. E., Hulmi, J. J., Børsheim, E., Wiig, H., Garthe, I., & Raastad, T. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.279950 · Cited by 148
Resistance 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
Exercise, Amino Acids, and Aging in the Control of Human Muscle Protein Synthesis
Walker, D. K., Dickinson, J. M., Timmerman, K. L., Drummond, M. J., Reidy, P. T., Fry, C. S., Gundermann, D. M., & Rasmussen, B. B. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318223b037 · Cited by 143
The search for exercise factors in humans
Catoire, M., & Kersten, S. (2015) · The FASEB Journal · doi:10.1096/fj.14-263699 · Cited by 137
Identification of atrogin-1-targeted proteins during the myostatin-induced skeletal muscle wasting
Lokireddy, S., Wijesoma, I. W., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00402.2011 · Cited by 135
Moore, D. R., Atherton, P. J., Rennie, M. J., Tarnopolsky, M. A., & Phillips, S. M. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02187.x · Cited by 122
Reidy, P. T., & Rasmussen, B. B. (2016) · The Journal of Nutrition · doi:10.3945/jn.114.203208 · Cited by 128
Characterization 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
West, D., Abou Sawan, S., Mazzulla, M., Williamson, E., & Moore, D. (2017) · Nutrients · doi:10.3390/nu9070735 · Cited by 112
Vissing, K., McGee, S. L., Farup, J., Kjølhede, T., Vendelbo, M. H., & Jessen, N. (2013) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/j.1600-0838.2011.01395.x · Cited by 111
Roberts, M. D., Haun, C. T., Mobley, C. B., Mumford, P. W., Romero, M. A., Roberson, P. A., Vann, C. G., & McCarthy, J. J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00834 · Cited by 107
Naclerio, F., & Larumbe-Zabala, E. (2016) · Sports Medicine · doi:10.1007/s40279-015-0403-y · Cited by 106
“These effects rely on the capacity to increase and prolong mammalian target of rapamycin signaling response to exercise and training [35] (for review see Vary and Lynch [36]).”
BackgroundImmune Responses to Resistance Exercise
Freidenreich, D. J., & Volek, J. S. (2026) · PubMed · doi:10.22029/eir.2012.1667 · Cited by 103
Heat stress enhances mTOR signaling after resistance exercise in human skeletal muscle
Kakigi, R., Naito, H., Ogura, Y., Kobayashi, H., Saga, N., Ichinoseki-Sekine, N., Yoshihara, T., & Katamoto, S. (2011) · The Journal of Physiological Sciences · doi:10.1007/s12576-010-0130-y · Cited by 95
“amino acid ingestion) during and after resistance exercise enhance the activation of mTOR signaling in skeletal muscle concomitant with an increase in the rate of muscle protein synthesis [24–27], leading to muscle hypertrophy.”
BackgroundGonzalez, A. M., Hoffman, J. R., Stout, J. R., Fukuda, D. H., & Willoughby, D. S. (2015) · Sports Medicine · doi:10.1007/s40279-015-0450-4 · Cited by 97
Resistance training induced increase in muscle fiber size in young and older men
Mero, A. A., Hulmi, J. J., Salmijärvi, H., Katajavuori, M., Haverinen, M., Holviala, J., Ridanpää, T., Häkkinen, K., Kovanen, V., Ahtiainen, J. P., et al. (2012) · European Journal of Applied Physiology · doi:10.1007/s00421-012-2466-x · Cited by 90
“…people consume adequate amounts of protein, some tend to have a reduced appetite and thus consume less protein than the recommended protein (Dalbo et al. 2011; Hulmi et al. 2007, 2008, 2009a, b; Kim et al. 2005a, 2007; Mascher et al. 2008), which likely results in an accelerated rate of sarcopenia.”
InfluentialApicella, J. M., Lee, E. C., Bailey, B. L., Sáenz, C., Anderson, J. M., Craig, S. A. S., Kraemer, W. J., Volek, J. S., & Maresh, C. M. (2012) · European Journal of Applied Physiology · doi:10.1007/s00421-012-2492-8 · Cited by 81
Hulmi, J. J., Silvennoinen, M., Lehti, M., Kivelä, R., & Kainulainen, H. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00398.2011 · Cited by 81
Considerations on mTOR regulation at serine 2448: implications for muscle metabolism studies
Figueiredo, V. C., Markworth, J. F., & Cameron‐Smith, D. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2481-5 · Cited by 88
Physical Activity and Sarcopenia
Pillard, F., Laoudj‐Chenivesse, D., Carnac, G., Mercier, J. G., RAMI, J., Rivière, D., & Rolland, Y. (2011) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2011.03.009 · Cited by 79
Hodson, N. W., West, D. W. D., Philp, A., Burd, N. A., & Moore, D. R. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00209.2019 · Cited by 82
Ryan, A. S., Li, G., Blumenthal, J. B., & Ortmeyer, H. K. (2013) · Obesity · doi:10.1002/oby.20216 · Cited by 74
Jespersen, J. G., Nedergaard, A., Andersen, L. L., Schjerling, P., & Andersen, J. L. (2009) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2009.01044.x · Cited by 67
Arciero, P. J., Baur, D., Connelly, S., & Ormsbee, M. J. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00152.2014 · Cited by 64
Symposium review: Amino acid uptake by the mammary glands: Where does the control lie?
Cant, J. P., Kim, J. J. M., Cieslar, S. R. L., & Doelman, J. (2018) · Journal of Dairy Science · doi:10.3168/jds.2017-13844 · Cited by 62
Mesquita, P. H. C., Vann, C. G., Phillips, S. M., McKendry, J., Young, K. C., Kavazis, A. N., & Roberts, M. D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.725866 · Cited by 62
Lueders, T. N., Zou, K., Huntsman, H. D., Meador, B. M., Mahmassani, Z. S., Abel, M., Valero, M. C., Huey, K. A., & Boppart, M. D. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00515.2010 · Cited by 60
“Active mTOR in 7Tg muscle cryosections was localized to the sarcolemma and cytoplasm of mature fibers, with intense staining around select nuclei inside or outside the fibers, consistent with previous findings (15) (Fig.”
ResultMolecular signaling in muscle is affected by the specificity of resistance exercise protocol
Hulmi, J. J., Walker, S., Ahtiainen, J. P., Nyman, K., Kraemer, W. J., & Häkkinen, K. (2010) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2010.01198.x · Cited by 62
Dietary protein considerations to support active aging
Wall, B. T., Cermak, N. M., & van Loon, L. J. C. (2014) · Sports Medicine · doi:10.1007/s40279-014-0258-7 · Cited by 56
Myostatin — From the Mighty Mouse to cardiovascular disease and cachexia
Dschietzig, T. B. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.03.021 · Cited by 55
Walker, S., Hulmi, J. J., Wernbom, M., Nyman, K., Kraemer, W. J., Ahtiainen, J. P., & Häkkinen, K. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2653-4 · Cited by 62
Doelman, J., Kim, J. J. M., Carson, M., Metcalf, J. A., & Cant, J. P. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9819 · Cited by 55
Post-absorptive muscle protein turnover affects resistance training hypertrophy
Reidy, P. T., Borack, M. S., Markofski, M. M., Dickinson, J. M., Fry, C. S., Deer, R., Volpi, E., & Rasmussen, B. B. (2017) · European Journal of Applied Physiology · doi:10.1007/s00421-017-3566-4 · Cited by 53
Whey for Sarcopenia; Can Whey Peptides, Hydrolysates or Proteins Play a Beneficial Role?
Gilmartin, S., O’Brien, N. M., & Giblin, L. (2020) · Foods · doi:10.3390/foods9060750 · Cited by 53
Rinnankoski‐Tuikka, R., Silvennoinen, M., Karvinen, S. M., Hulmi, J. J., Lehti, M., Kivelä, R., Reunanen, H., & Kainulainen, H. (2012) · Nutrition & Metabolism · doi:10.1186/1743-7075-9-53 · Cited by 49
“Western immunoblot analyses from the muscle lysates (samples containing 20 μg of total protein) were done as previously described [41,42].”
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Tagawa, R., Watanabe, D., Ito, K., Otsuyama, T., Nakayama, K., Sanbongi, C., & Miyachi, M. (2022) · Sports Medicine - Open · doi:10.1186/s40798-022-00508-w · Cited by 55
Hentilä, J., Ahtiainen, J. P., Paulsen, G., Raastad, T., Häkkinen, K., Mero, A. A., & Hulmi, J. J. (2018) · Acta Physiologica · doi:10.1111/apha.13069 · Cited by 50
“This may be explained by increased mTOR signalling that was previously observed in our subjects.(43) mTOR is known to inhibit autophagy by phosphorylating ULK1 at ser(757),(44) and there was a nonsignificant trend for increase in p-ULK1 content at 1 hour after the RE bout.”
BackgroundMethodNilsen, T. S., Thorsen, L., Fosså, S. D., Wiig, M., Kirkegaard, C., Skovlund, E., Benestad, H. B., & Raastad, T. (2015) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12543 · Cited by 46
Rahbek, S. K., Farup, J., Møller, A. B., Vendelbo, M. H., Holm, L., Jessen, N., & Vissing, K. (2014) · Amino Acids · doi:10.1007/s00726-014-1792-1 · Cited by 46
“2007), but not all studies (Hulmi et al. 2009) and may relate to the composition of amino acids (i.”
Hamarsland, H., Nordengen, A. L., Aas, S. N., Holte, K., Garthe, I., Paulsen, G., Cotter, M., Børsheim, E., Benestad, H. B., & Raastad, T. (2017) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-017-0202-y · Cited by 49
Doelman, J., Curtis, R. V., Carson, M., Kim, J. J. M., Metcalf, J. A., & Cant, J. P. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-9051 · Cited by 43
“The increase in protein synthesis in skeletal muscle following consumption of a meal is mediated by the mammalian target of rapamycin (mTOR) signaling cascade (Kimball et al., 2000; Hulmi et al., 2009).”
InfluentialIs 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
The influence of skeletal muscle on appetite regulation
Grannell, A., VITO, G. D., Murphy, J. C., & le Roux, C. W. (2019) · Expert Review of Endocrinology & Metabolism · doi:10.1080/17446651.2019.1618185 · Cited by 46
Hulmi, J. J., Myllymäki, T., Tenhumäki, M., Mutanen, N. E., Puurtinen, R., Paulsen, G., & Mero, A. A. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1360-7 · Cited by 41
“This study combines previously unpublished blood data results from separate studies of which we have previously reported muscle gene and protein expression (Hulmi et al. 2007, 2008a, b; 2009a, b), mTOR signaling ( Hulmi et al. 2009b ), and blood hormones (Hulmi et al. 2005, 2008a, b, 2009b).”
MethodResultNeuromuscular and Hormonal Responses to Constant and Variable Resistance Loadings
Walker, S., Taipale, R. S., Nyman, K., Kraemer, W. J., & Häkkinen, K. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181e71bcb · Cited by 41
Diel, P. R., Schiffer, T., Geisler, S., Hertrampf, T., Mosler, S., Schulz, S., Wintgens, K. F., & Adler, M. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.08.015 · Cited by 41
Protein Supplementation Does Not Affect Myogenic Adaptations to Resistance Training
Reidy, P. T., Fry, C. S., Igbinigie, S. N., Deer, R., Jennings, K., Cope, M. B., Mukherjea, R., Volpi, E., & Rasmussen, B. B. (2017) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001224 · Cited by 44
“In addition, studies using magnetic resonance imaging of the biceps (10) or latissimus dorsi (33) and ultrasound (3,4,22,23,48) of the thigh muscles have clearly shown the same pattern: no effect of protein supplementation (whey) to enhance vastus lateralis muscle hypertrophy.”
Bridge, A. D., Brown, J. A., Snider, H., Nasato, M., Ward, W. E., Roy, B. D., & Josse, A. R. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00055 · Cited by 41
Sedliak, M., Zeman, M., Buzgó, G., Cvečka, J., Hamar, D., Laczo, E., Okuliarová, M., Vanderka, M., Kampmiller, T., Häkkinen, K., et al. (2017) · Chronobiology International · doi:10.1080/07420528.2017.1411360 · Cited by 36
Dalbo, V. J., Roberts, M. D., Hassell, S., & Kerksick, C. M. (2013) · European Journal of Nutrition · doi:10.1007/s00394-012-0349-x · Cited by 35
Synergistic effects of resistance training and protein intake: Practical aspects
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Mobley, C. B., Fox, C. D., Thompson, R. M., Healy, J. C., Santucci, V., Kephart, W. C., McCloskey, A. E., Kim, M., Pascoe, D. D., Martin, J. S., et al. (2016) · Amino Acids · doi:10.1007/s00726-015-2121-z · 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
Irisin and myostatin responses to acute high-intensity interval exercise in humans
Kabak, B., Belviranlı, M., & Okudan, N. (2018) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2018-0008 · Cited by 33
Bagheri, R., Moghadam, B. H., Jo, E., Tinsley, G. M., Stratton, M. T., Ashtary‐Larky, D., Eskandari, M., & Wong, A. (2020) · British Journal Of Nutrition · doi:10.1017/s0007114520002238 · Cited by 36
“Our rationale for sample size was based on previous data (1,23,24) .”
Kazemi, F. (2015) · Journal of Endocrinological Investigation · doi:10.1007/s40618-015-0373-9 · Cited by 33
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Erceg, M., Velickovska, L. A., Gontarev, S., Naumovski, M., Kalac, R., Hristovski, R., Čular, D., Popovski, L., Dadasovic, M., Meshkovska, N., et al. (2013) · Cited by 31
Silvennoinen, M., Rinnankoski‐Tuikka, R., Vuento, M., Hulmi, J. J., Karvinen, S. M., Lehti, M., Kivelä, R., & Kainulainen, H. (2012) · Angiogenesis · doi:10.1007/s10456-012-9315-8 · Cited by 28
Mobley, C. B., Fox, C. D., Ferguson, B. S., Amin, R., Dalbo, V. J., Baier, S. M., Rathmacher, J. A., Wilson, J. M., & Roberts, M. D. (2014) · Journal of the International Society of Sports Nutrition · doi:10.1186/1550-2783-11-38 · Cited by 28
Gonzalez, A. M., Hoffman, J. R., Townsend, J. R., Jajtner, A. R., Wells, A. J., Beyer, K. S., Willoughby, D. S., Oliveira, L., Fukuda, D. H., Fragala, M. S., et al. (2015) · Physiological Reports · doi:10.14814/phy2.12268 · Cited by 26
Mäntyselkä, S., Kolari, K., Baumert, P., Ylä-Outinen, L., Kuikka, L., Lahtonen, S., Permi, P., Wackerhage, H., Kalenius, E., Kivelä, R., et al. (2024) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00151.2023 · Cited by 25
Omi, N., Shiba, H., Nishimura, E., Tsukamoto, S., Maruki‐Uchida, H., Oda, M., & Morita, M. (2019) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-019-0303-x · Cited by 25
McIntosh, M. C., Sexton, C. L., Godwin, J. S., Ruple, B. A., Michel, J. M., Plotkin, D. L., Ziegenfuss, T. N., Lopez, H. L., Smith, R. C., Dwaraka, V. B., et al. (2023) · Cells · doi:10.3390/cells12060898 · Cited by 28
Willoughby, D. S., Cardaci, T. D., Machek, S. B., Wilburn, D. T., & Heileson, J. L. (2022) · Journal of Sports Science and Medicine · doi:10.52082/jssm.2022.616 · Cited by 24
Binns, A., Gray, M., Henson, A. C., & Fort, I. L. (2017) · The journal of nutrition health & aging · doi:10.1007/s12603-017-0883-6 · Cited by 26
“Of specific interest, is the regulation of the mTOR pathway given its relation to muscle mass regulation with aging (35).”
Centner, C., Jerger, S., Mallard, A. R., Herrmann, A., Varfolomeeva, E., Gollhofer, S. M., Oesser, S., Sticht, C., Gretz, N., Aagaard, P., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.838004 · Cited by 27
Haun, C. T., Mobley, C. B., Vann, C. G., Romero, M. A., Roberson, P. A., Mumford, P. W., Kephart, W. C., Healy, J. C., Patel, R. K., Osburn, S. C., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29591-4 · Cited by 23
Edgett, B. A., Fortner, M. L., Bonen, A., & Gurd, B. J. (2013) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2012-0405 · Cited by 20
Muscle atrophy in immobilization and senescence in humans
Murton, A. J., & Greenhaff, P. L. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832f15e1 · Cited by 19
Paoli, A., Pacelli, Q. F., Neri, M., Toniolo, L., Cancellara, P., Canato, M., Moro, T., Quadrelli, M., Morra, A., Faggian, D., et al. (2014) · Journal of Medicinal Food · doi:10.1089/jmf.2014.0004 · Cited by 19
Effects of resistance training on expression of IGF‐I splice variants in younger and older men
Ahtiainen, J. P., Hulmi, J. J., Lehti, M., Kraemer, W. J., Nyman, K., Selänne, H., Alén, M., Komulainen, J., Kovanen, V., Mero, A. A., et al. (2016) · European Journal of Sport Science · doi:10.1080/17461391.2016.1185164 · Cited by 18
Tang, C., Xi, T., Zheng, J., & Cui, X. (2025) · Natural Product Communications · doi:10.1177/1934578x251326124 · Cited by 19
“Furthermore, the timing of whey protein ingestion can signi fi cantly impact its effectiveness in stimulating MPS. Recent studies have indicated that different types of whey protein, such as WPI and WPC, exhibit varying effects on MPS.”
InfluentialShirato, M., Tsuchiya, Y., Sato, T., Hamano, S., 具志堅武, Kimura, N., & Ochi, E. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0119-x · Cited by 18
Pekkala, S., Wiklund, P., Hulmi, J. J., Pöllänen, E., Marjomäki, V., Munukka, E., Pierre, P., Mouly, V., Mero, A. A., Alén, M., et al. (2015) · Peptides · doi:10.1016/j.peptides.2015.03.007 · Cited by 19
Angelica Sinensis promotes myotube hypertrophy through the PI3K/Akt/mTOR pathway
Yeh, T., Hsu, C.-C., Yang, S., Hsu, M., & Liu, J. (2014) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-14-144 · Cited by 19
Agergaard, J., Reitelseder, S., Pedersen, T. G., Doessing, S., Schjerling, P., Langberg, H., Miller, B. F., Aagaard, P., Kjær, M., & Holm, L. (2012) · Muscle & Nerve · doi:10.1002/mus.23667 · Cited by 17
Nissinen, T. A., Hentilä, J., Fachada, V., Lautaoja-Kivipelto, J. H., Pasternack, A. H., Ritvos, O., Kivelä, R., & Hulmi, J. J. (2021) · The FASEB Journal · doi:10.1096/fj.202002008r · Cited by 19
Čurović, I., Rhodes, D., Alexander, J., & Harper, D. J. (2024) · Sports Medicine · doi:10.1007/s40279-024-02039-8 · Cited by 14
“…the increased amino acid presence in 2 consecutive days, training of the contralateral arm may have benefitted from the previous day’s high-volume session via prolonged anabolic pathway signalling [136] and altered systemic metabolic state potentiating muscle stem cells [72] in the untrained arm.”
BackgroundHalonen, E. J., Gabriel, I., Kelahaara, M., Ahtiainen, J. P., & Hulmi, J. J. (2024) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.14739 · Cited by 19
Hulmi, J. J., Halonen, E. J., Sharples, A. P., O’Connell, T. M., Kuikka, L., Lappi, V., Salokas, K., Keskitalo, S., Varjosalo, M. T., & Ahtiainen, J. P. (2025) · The Journal of Physiology · doi:10.1113/jp288104 · Cited by 14
“Biopsies were taken from the VL at one-third of the length from the patella towards the greater trochanter, using local anaesthetic and a 5-mm Bergström biopsy needle with suction, as previously described (Hulmi et al., 2009).”
Ji, X., Ye, X., Ji, S., Zhang, S., Wang, Y., Zhou, Z., Xiang, D., & Luo, B. (2025) · Nutrients · doi:10.3390/nu17162579 · Cited by 12
“Among the 15 RCTs included in this meta-analysis, 11 included supplementation after exercise [17,19,20,23,25–31], 3 included supplementation before exercise [18,21,22], and 1 included supplementation both before and after exercise [24].”
Chan, K., Chen, Y., Lit, Y., Massaband, P., Kiratli, B. J., Rabkin, R., & MYERS, J. N. (2019) · Contemporary Clinical Trials Communications · doi:10.1016/j.conctc.2019.100365 · Cited by 12
Wang, W., Choi, R. H., Solares, G. J., Tseng, H.-M., Ding, Z., Kim, K., & Ivy, J. L. (2015) · Amino Acids · doi:10.1007/s00726-015-1972-7 · Cited by 12
Effects of time of day on resistance exercise-induced anabolic signaling in skeletal muscle
Sedliak, M., Zeman, M., Buzgó, G., Cvečka, J., Hamar, D., Laczo, E., Zelko, A., Okuliarová, M., Raastad, T., Nilsen, T. S., et al. (2012) · Biological Rhythm Research · doi:10.1080/09291016.2012.740314 · Cited by 14
Sun, J., He, M. T., Chen, M., Chen, Y., Yuan, W., Song, F., Ren, L., Shen, H., Zhang, J., Shen, X., et al. (2025) · Nutrition Journal · doi:10.1186/s12937-025-01244-z · Cited by 11
“Relevant mechanistic evidence supports this conclusion, as demonstrated by Juha J Hulmi et al., who reported that whey protein supplementation amplifies and prolongs mTOR signaling in the muscle protein synthesis pathway following exercise [45].”
Myostatin's marvels: From muscle regulator to diverse implications in health and disease
Sharma, S., & Patil, A. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.4106 · Cited by 12
Autophagy and Exercise: Current Insights and Future Research Directions
Botella, J., Shaw, C. S., & Bishop, D. J. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2153-9258 · Cited by 12
“The study of autophagy following RE is of interest given the important role of mTOR-regulated protein synthesis in the response to RE [70], and the negative regulation of autophagy by mTOR [71].”
BackgroundHaraguchi, F. K., Magalhães, C. L. D. B., Neves, L. X., dos Santos, R. C., Pedrosa, M. L., & Silva, M. E. (2013) · Nutrition · doi:10.1016/j.nut.2013.12.007 · Cited by 12
“WP induces mTOR phosphorylation to a greater extent than other protein sources, such as soy, in treadmill-exercised rats [9] and prolongs mTOR signaling in response to RE in humans [10].”
BackgroundGonzalez, A. M., Hoffman, J. R., Jajtner, A. R., Townsend, J. R., Boone, C. H., Beyer, K. S., Baker, K. M., Wells, A. J., Church, D. D., Mangine, G. T., et al. (2015) · Nutrition Research · doi:10.1016/j.nutres.2015.09.006 · Cited by 11
Aas, S. N., Tømmerbakke, D., Godager, S., Nordseth, M., Armani, A., Sandri, M., Benestad, H. B., & Raastad, T. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111122 · Cited by 10
Ono, K., Tanaka, M., Ikeji, T., Nakanishi, R., Hirabayashi, T., Tategaki, A., Kondo, H., Ishihara, A., & Fujino, H. (2020) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2020.1795810 · Cited by 8
Metadata
- Authors
- Hulmi, J. J., Tannerstedt, J., Selänne, H., Kainulainen, H., Kovanen, V., & Mero, A. A.
- Affiliations
- University of Jyväskylä (FI)
- Venue
- Journal of Applied Physiology
- Publisher
- American Physiological Society
- Published
- 2009-05
- Volume
- 106
- Issue
- 5
- Pages
- 1720-1729
- ISSN
- 0161-7567 (ISSN-L)
- 8750-7587
- 1522-1601
- OpenAlex
- W2095678778
- Cited by
- 163
- References
- 59
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 7 · 2023: 5 · 2022: 7 · 2021: 4 · 2020: 5 · 2019: 8 · 2018: 8 · 2017: 12 · 2016: 5 · 2015: 16 · 2014: 13 · 2013: 12 · 2012: 22
- FWCI
- 7.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Applied Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ellen ja Artturi Nyyssösen Säätiö
- Kela
- 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 › Orthopedics and Sports Medicine › Sports Performance and Training
- Keywords
- resistance training, mTOR signaling, myostatin, muscle hypertrophy, p70S6K phosphorylation, ribosomal protein S6, 4E-BP1, Akt phosphorylation, elongation factor 2, vastus lateralis, muscle fiber size, protein supplementation
- MeSH terms
- Whey Proteins, Dietary Proteins, Humans, Male, Milk Proteins, Phosphorylation, Protein Kinases, Signal Transduction, Exercise, Muscle Fibers, Skeletal, Ribosomal Protein S6, Ribosomal Protein S6 Kinases, 70-kDa, Oncogene Protein v-akt, Myostatin, TOR Serine-Threonine Kinases
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