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Recovery from the demands of daily training is an essential element of a scientifically based periodized program whose twin goals are to maximize training adaptation and enhance performance. Prolonged endurance training sessions induce substantial metabolic perturbations in skeletal muscle, including the depletion of endogenous fuels and damage/disruption to muscle and body proteins. Therefore, increasing nutrient availability (i.e., carbohydrate and protein) in the post-training recovery period is important to replenish substrate stores and facilitate repair and remodelling of skeletal muscle. It is well accepted that protein ingestion following resistance-based exercise increases rates of skeletal muscle protein synthesis and potentiates gains in muscle mass and strength. To date, however, little attention has focused on the ability of dietary protein to enhance skeletal muscle remodelling and stimulate adaptations that promote an endurance phenotype. The purpose of this review is to critically discuss the results of recent studies that have examined the role of dietary protein for the endurance athlete. Our primary aim is to consider the results from contemporary investigations that have advanced our knowledge of how the manipulation of dietary protein (i.e., amount, type, and timing of ingestion) can facilitate muscle remodelling by promoting muscle protein synthesis. We focus on the role of protein in facilitating optimal recovery from, and promoting adaptations to strenuous endurance-based training.
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Beyond muscle hypertrophy: why dietary protein is important
for endurance athletes
Daniel R. Moore, Donny M. Camera, Jose L. Areta, and John A. Hawley
Abstract: Recovery from the demands of daily training is an essential element of a scientifically based periodized program
whose twin goals are to maximize training adaptation and enhance performance. Prolonged endurance training sessions induce
substantial metabolic perturbations in skeletal muscle, including the depletion of endogenous fuels and damage/disruption to
muscle and body proteins. Therefore, increasing nutrient availability (i.e., carbohydrate and protein) in the post-training
recovery period is important to replenish substrate stores and facilitate repair and remodelling of skeletal muscle. It is well
accepted that protein ingestion following resistance-based exercise increases rates of skeletal muscle protein synthesis and
potentiates gains in muscle mass and strength. To date, however, little attention has focused on the ability of dietary protein to
enhance skeletal muscle remodelling and stimulate adaptations that promote an endurance phenotype. The purpose of this
review is to critically discuss the results of recent studies that have examined the role of dietary protein for the endurance
athlete. Our primary aim is to consider the results from contemporary investigations that have advanced our knowledge of how
the manipulation of dietary protein (i.e., amount, type, and timing of ingestion) can facilitate muscle remodelling by promoting
muscle protein synthesis. We focus on the role of protein in facilitating optimal recovery from, and promoting adaptations to
strenuous endurance-based training.
Key words: endurance exercise, cell signalling, training adaptation, muscle protein synthesis, dietary protein, remodelling,
Résumé : La récupération consécutive aux dépenses suscitées par l’entraînement quotidien est un élément essentiel d’un
programme scientifique de périodisation dont le double objectif est de maximiser l’adaptation a
`l’entraînement et d’améliorer
la performance. Les séances d’entraînement prolongé en endurance suscitent d’importantes perturbations métaboliques dans le
muscle squelettique notamment la déplétion des carburants endogènes et les lésions/dommages aux muscles et aux protéines
organiques. Il est donc important d’accroître la disponibilité des nutriments (hydrates de carbone et protéines) durant la période
de récupération postexercice afin de refaire les réserves de substrats et faciliter la réparation et le remodelage du tissu muscu-
laire squelettique. Il est généralement admis que l’ingestion de protéines après une séance d’exercices contre résistance accroît
le taux de synthèse des protéines du muscle squelettique et potentialise le gain de masse et de force musculaires. Jusqu’a
`ce jour,
cependant, il y a peu d’études sur le rôle des protéines alimentaires dans l’amélioration du remodelage du muscle squelettique
et la stimulation de l’adaptation a
`un phénotype d’endurance. Cette analyse documentaire se propose de traiter de façon critique
les résultats des études récentes sur le rôle des protéines alimentaires chez l’athlète d’endurance. Notre principal objectif est de
prendre en compte les résultats des recherches contemporaines qui ont amélioré nos connaissances sur l’utilisation des
protéines alimentaires (quantité, type et moment de l’ingestion) pour promouvoir la synthèse des protéines musculaires dans le
remodelage du muscle. On met l’accent sur le rôle des protéines pour faciliter la récupération optimale et favoriser les
adaptations a
`un entraînement intense en endurance. [Traduit par la Rédaction]
Mots-clés : exercice d’endurance, signalisation cellulaire, adaptation a
`l’entraînement, synthèse des protéines musculaires,
protéines alimentaires, remodelage, récupération.
Appropriate recovery from the stress of exercise is an essential
component of any periodized program aimed at maximizing
training-induced physiological adaptations and enhancing ath-
letic performance. Prolonged, sustained endurance training
sessions exert significant metabolic demands that include the de-
pletion of endogenous fuel stores (e.g., liver and muscle glycogen),
loss of body fluid and electrolytes, hormonal perturbations, and
damage/disruption to skeletal muscle and body proteins. As
such, recovery strategies for competitive athletes engaged in
endurance-based training typically focus on 3 inter-related ap-
proaches: refuelling, rehydration, and repair. Given the high en-
ergy demands of daily endurance training (Stepto et al. 2002),
many athletes recognize the importance of replenishing fuel
stores through suitable postexercise carbohydrate ingestion pro-
tocols (Burke et al. 2004). In addition, there is an awareness of the
role that hydration and rehydration play in optimizing training
outcomes and performance (Murray 2007;Sawka et al. 2007). As
Received 18 December 2013. Accepted 3 February 2014.
D.R. Moore. Faculty of Kinesiology and Physical Education, University of Toronto, Toronto ON, M5S 2W6, Canada.
D.M. Camera and J.L. Areta. Exercise and Nutrition Research Group, Department of Exercise Sciences, Australian Catholic University, Fitzroy,
Victoria, Australia.
J.A. Hawley. Exercise and Nutrition Research Group, Department of Exercise Sciences, Australian Catholic University, Fitzroy, Victoria, Australia;
Research Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool, UK.
Corresponding author: Daniel R. Moore (e-mail:
This paper is a part of a Special Issue entitled Nutritional Triggers to Adaptation and Performance.
Appl. Physiol. Nutr. Metab. 39: 987–997 (2014) Published at on 7 February 2014.
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such, many competitive endurance athletes already appreciate
the need to refuel and rehydrate after training. However, 1 aspect
of the recovery process that is often neglected is the role of dietary
protein in providing the “building blocks” (i.e., amino acids) to
repair and regenerate damaged proteins as well as synthesize a
variety of new proteins (including both contractile myofibrillar
and energy producing mitochondrial proteins and associated en-
zyme complexes). It is this repair and remodelling of muscle pro-
teins that provides the basis for many of the training-induced
adaptations that underpin the increases in muscle quality (i.e.,
mitochondrial density and (or) cross-sectional area) that ulti-
mately lead to improved performance.
The importance of adequate dietary protein to enhance recov-
ery from resistance-based exercise is well accepted and is a funda-
mental tenet of nutrition for muscle growth (Churchward-Venne
et al. 2012). Factors that influence the extent and magnitude of
muscle remodelling with resistance exercise include the amount,
type, and timing of protein ingestion (Burd et al. 2009). Only re-
cently, however, has it been recognized that the results from stud-
ies of resistance-trained athletes may have relevance to athletes
training for and competing in endurance events. Accordingly, the
general purpose of this review is to summarize recent informa-
tion on the importance of dietary protein for the endurance ath-
lete with a focus on the role of protein in facilitating optimal
recovery from, and adaptation to, strenuous endurance training
Although a brief overview of the protein requirements of the
endurance athlete will be provided, our primary focus will be to
discuss the results from recent research that has advanced our
knowledge of specific aspects of increased protein availability
that facilitate muscle remodelling by promoting muscle protein
synthesis. Given the current lack of evidence regarding the impact
of protein ingestion on postexercise muscle remodelling (i.e., in-
creasing muscle protein turnover) after endurance training, ap-
propriate studies that have utilized resistance-based training will
be highlighted and placed into the context for the endurance
Amino acids as a fuel
Carbohydrate (CHO)-based fuels (muscle and liver glycogen,
blood glucose, blood, muscle, and liver lactate) are the predomi-
nant energy for muscle contraction during continuous endurance
events lasting up to2h(Hawley and Hopkins 1995). In endurance
events lasting from 2–10 h (i.e., Ironman triathlon) there is still a
heavy reliance on CHO for oxidative metabolism, but fat-based
fuels (adipose and intramuscular triglycerides as well as blood-
borne free fatty acids) play an increasingly important role in en-
ergy provision (Jeukendrup 2011). Because endogenous CHO stores
are limited, nutritional strategies to either slow their rate of oxi-
dation during exercise and (or) increase their availability before
and (or) during exercise have received widespread scientific en-
quiry (Burke et al. 2011). However, amino acid oxidation (from free
amino acids in blood and liver pools as well as the protein stores
that are at equilibrium) can provide up to 10% of total energy
during endurance exercise (Tarnopolsky 2004). This enhanced ox-
idation arises to a significant extent from the breakdown of mus-
cle proteins into their constituent amino acids (Howarth et al.
2010), which are subsequently released from the muscle for he-
patic gluconeogenesis and (or) deaminated and oxidized within
the muscle mitochondria as a direct source of fuel (such is the
primary fate of the branched chain amino acids and especially
leucine) (Tarnopolsky 2004).
The oxidation of endogenous amino acids can be enhanced
by several factors, such as exercise intensity and (or) duration
(Haralambie and Berg 1976;Lamont et al. 2001), low muscle glyco-
gen availability (Howarth et al. 2010;Lemon and Mullin 1980), a
habitually high-protein diet (i.e., 1.8 g/(kg·day) (Bowtell et al.
1998), and sex (Phillips et al. 1993). Endurance training lowers the
maximal activity of branched-chain ketoacid dehydrogenase (the
rate-controlling enzyme for branched-chain amino acid oxida-
tion) during exercise while also blunting the exercise-induced
stimulation of leucine oxidation (McKenzie et al. 2000), suggest-
ing muscle from endurance-trained individuals has a refined
metabolism that can reduce its reliance on amino acids as an
alternative source of fuel. While the common practice of consum-
ing CHO during endurance exercise attenuates amino acid oxida-
tion, whole-body rates remain significantly elevated above rest
(Bowtell et al. 2000). Indeed, leucine, an amino acid with key
regulatory roles in protein metabolism (discussed subsequently),
can be oxidized at a rate of 8 mg/(kg·h) in endurance athletes
performing moderate-intensity (60% of maximal aerobic power
)) continuous exercise (Bowtell et al. 1998), resulting in an
estimated total body leucine loss of 1.2 g over 2 h. Assuming
muscle protein is 9% leucine (Burd et al. 2013), this could mean
the equivalent of 13 g of protein is catabolized during this type
of exercise. Paradoxically, despite an exercise-induced increase in
leucine oxidation, there is little effect of this extra protein de-
mand on 24-h net leucine balance during acute metabolic trials
(Forslund et al. 1999). These data suggest that over the course of a
day metabolic accommodation may occur to spare net leucine
loses, perhaps through an attenuated postexercise leucine oxida-
tion (Devlin et al. 1990). However, for the athlete who trains on a
daily basis (or on several occasions in a single day) and (or) who is
targeting an optimal recovery strategy that aims to meet or ex-
ceed net leucine (protein) balance, this potential accommodation
in protein metabolism may not be ideal to support their long-term
training goals. Given that oxidized amino acids (and especially the
essential amino acid leucine) are essentially lost from the body
and do not contribute to the increased muscle protein synthesis
observed during recovery, they must ostensibly be replaced
through dietary sources.
Protein requirements of endurance athletes
Energy balance
Current population requirements for protein to maintain ni-
trogen balance are set at 0.8 g/(kg·day). However, active persons,
particularly athletes involved in strenuous endurance and resis-
tance training, have a greater daily protein requirement than
their sedentary counterparts. As such, these individuals need to
ingest more dietary protein to reach nitrogen balance (Phillips
et al. 1993;Tarnopolsky et al. 1988). Indeed, it has been suggested
that the protein needs of such athletes may be 40%–100% greater
than the current recommended dietary allowance (Tarnopolsky
2004). This increased protein requirement is thought to reflect the
enhanced amino acid oxidation that occurs during exercise in
these athletes (Tarnopolsky 2004). However, the importance of
maintaining nitrogen balance in athletes has been questioned,
given that it has little direct link to any performance measure or
even lean muscle mass per se (Phillips 2006;Phillips et al. 2007;
Tipton and Witard 2007). Moreover, the majority of endurance-
trained athletes are likely meeting their total daily energy
requirements and therefore probably ingest protein in amounts
that are already higher than the minimal recommended levels
(Tarnopolsky 2004). As discussed subsequently, the type of protein
and the timing of intake are likely to play more important roles in
maximizing recovery from, and adaptation to, endurance train-
ing than merely meeting or exceeding current protein recommen-
dations on a daily basis (Tarnopolsky 2004)).
Negative energy balance
During periods of intensified training and (or) voluntary weight
loss (i.e., whole-body energy restriction), endurance athletes are
faced with a period of reduced energy availability (Loucks 2007).
The mismatch between energy intake and energy expenditure can
lead to a reduction in total body mass, especially lean body (i.e.,
988 Appl. Physiol. Nutr. Metab. Vol. 39, 2014
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muscle) mass. The implications of a loss of lean tissue on training
capacity and (or) performance outcomes are obvious. Further-
more if this reduced energy intake does not replenish muscle (and
liver) glycogen stores prior to subsequent training sessions, there
is likely to be an increased muscle catabolism and amino acid
oxidation during subsequent exercise (Howarth et al. 2010), which
would ultimately necessitate a greater dietary intake of the oxi-
dized amino acids (e.g., leucine) to replenish these amino acid
stores. Studies in nonathletic populations (Josse et al. 2011;
Pasiakos et al. 2013) and with different training modalities (i.e.,
resistance exercise) (Mettler et al. 2010) show that providing di-
etary protein at levels in excess of recommended dietary allow-
ances attenuates the loss of lean body mass during periods
of reduced energy availability; this strategy appears to have
preliminary support in athletes involved in endurance sports
(Haakonssen et al. 2013). While the protein requirements of en-
durance athletes during periods of deliberate negative energy bal-
ance has not been systematically investigated, it is likely that
these individuals would benefit from higher dietary protein avail-
ability (Tipton and Witard 2007), similar to resistance-trained ath-
letes (Helms et al. 2013). However, any additional dietary protein
intake should not be at the expense of achieving adequate CHO
goals, which are essential if an athlete aims to maintain training
quality (i.e., intensity) and performance (Jarvis et al. 2002;
Macdermid and Stannard 2006).
Exercise-induced skeletal muscle remodelling
Skeletal muscle is a highly plastic tissue undergoing constant
remodelling through the continuous and simultaneous processes
of muscle protein synthesis (MPS) and muscle protein breakdown.
The net balance between these 2 processes (“turnover”) ultimately
determines whether skeletal muscle tissue is increasing (hyper-
trophy) or decreasing (atrophy) total protein content (Rennie et al.
2004;Burd et al. 2009). In the case of athletes training for endur-
ance sports, muscle remodelling is essential to break down old
and (or) damaged protein and resynthesize new functional pro-
teins. Whether this energetically costly process represents a net
expansion of a specific protein pool may be of relative inconse-
quence (e.g., myofibrillar proteins) or may be a targeted training
outcome (e.g., increased mitochondrial biogenesis). Nevertheless,
the pre-eminence of the stimulation of muscle protein synthesis
is that qualitative changes in the synthesis of muscle protein
fractions (e.g., force-generating myofibrillar proteins vs. energy-
producing mitochondrial proteins) provides insight into the ulti-
mate adaptive response to training (e.g., larger vs. more fatigue
resistant muscles) (Wilkinson et al. 2008).
Numerous studies have reported increases in mixed muscle
protein synthesis following a single bout (Harber et al. 2010;
Mascher et al. 2011) of exercise, and both short-term (i.e., 4 weeks)
(Pikosky et al. 2006) and chronic (i.e., 4 months) (Short et al. 2004)
endurance training. Such increases in mixed muscle protein syn-
thesis likely reflect enhanced remodelling of muscle proteins that
may include mitochondrial-related proteins/enzymes, angiogenic
proteins (e.g., endothelial and smooth muscle cells within capil-
laries), and myofibrillar proteins. The cellular mechanism(s) un-
derlying the observed increases in muscle protein synthesis
following endurance exercise training have only recently begun
to be explored. In this regard, the downstream target of rapamy-
cin complex 1 (mTORC1) intracellular signalling cascade is an
important contraction- and nutrient-stimulated pathway that reg-
ulates translation initiation and subsequent protein synthesis in
skeletal muscle (Drummond et al. 2009;Dickinson et al. 2011).
Endurance exercise in the form of either prolonged, constant
loading, or higher intensity repeated sprints stimulates mTORC1
signalling independent of protein feeding (Benziane et al. 2008;
Coffey et al. 2011;Mascher et al. 2007). Indeed, we have previously
shown a similar time course for mTOR-mediated signalling during
the early (60-min) recovery period between resistance and endur-
ance exercise (Camera et al. 2010). Regardless, activation and sub-
sequent upregulation of aspects of the cell signalling machinery
regulating protein synthesis after endurance-based exercise is a
necessary prerequisite for the increased gene translation and
subsequent protein expression that ultimately generates the
exercise-induced phenotype associated with this type of training.
However, additional work is necessary to elucidate the appropri-
ate molecular “signature” that may translate into altered rates of
muscle protein synthesis, as there are some reports of a dissocia-
tion between these acute “snapshot” markers of kinase activity
and kinetic subsequent protein remodelling (Greenhaff et al.
2008;Wilkinson et al. 2008).
Dietary protein to enhance rates of muscle protein
The ingestion of dietary amino acids enhances muscle protein
synthesis during recovery from resistance-based exercise (Burd
et al. 2009). This enhanced exercise-induced increase in protein
synthesis, which may persist for up to 72 h (Cuthbertson et al.
2006;Miller et al. 2005), facilitates the skeletal muscle remodel-
ling process that can ultimately enhance training-induced gains
in lean body mass (Cermak et al. 2012). In addition, recent work
has demonstrated that protein ingestion can also increase the
rates of muscle protein synthesis after prolonged, strenuous
endurance exercise (Breen et al. 2011;Howarth et al. 2009;
Levenhagen et al. 2002;Lunn et al. 2012) (see Table 1). Therefore,
general nutritional guidelines to enhance recovery from exercise,
regardless of the modality, recommend the intake of protein to
maximize postexercise rates of muscle protein synthesis (Phillips
and van Loon 2011). In this regard, recent research has provided
specific information relating to the most effective nutritional
strategies that enhance muscle protein remodelling after exercise
and have determined that the amount, type, and timing of protein
ingestion can all impact the extent and magnitude of postexercise
skeletal muscle remodelling (Fig. 1); these tenants of periodized
protein ingestion are discussed subsequently. Given the lack of
studies that have directly evaluated the factors related to dietary
protein ingestion after endurance exercise, our discussion will
draw on the results from the resistance training literature and,
where appropriate, contrast them with the demands of the endur-
ance athlete.
Amount of protein
One of the most important nutritional considerations that fa-
cilitate an increase in the rates of muscle protein synthesis is the
amount of protein consumed. Both mixed muscle and myofibril-
lar protein synthetic rates are enhanced after resistance exercise
with small (5–10 g) amounts of protein (Moore et al. 2009;Tang
et al. 2007), but are further augmented after the ingestion of
larger (20 g) protein feedings (Moore et al. 2009;Witard et al. 2014).
Rates of MPS plateau at around 20 g of ingested protein with
additional quantities (up to 40 g) failing to stimulate protein syn-
thesis further, at least not statistically (Moore et al. 2009;Witard
et al. 2014). Rather, at these larger protein intakes, there are in-
creases in amino acid oxidation and urea production (Moore et al.
2009;Witard et al. 2014). While these data appear robust for ath-
letes in energy balance, we have preliminary data to suggest that
protein requirements to elicit maximal rates of muscle protein
synthesis may be higher (i.e., >20 g) for athletes in energy deficit
(Areta et al. 2014). To the best of our knowledge, no study has
systematically determined the dose–response characteristics to
protein ingestion following endurance exercise. However, muscle
protein synthesis can be increased after endurance exercise with
as little as 10 g of protein (Levenhagen et al. 2002), with the re-
peated ingestion of small (10 g) amounts of protein immediately
and 30 min after a single bout of endurance exercise enhancing
Moore et al. 989
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Table 1. Studies investigating the effects of protein ingestion on muscle protein synthesis after endurance or high-intensity sprint exercise.
(reference) Subjects
(mL/(kg·min)) Exercise stimulus
intervention Protein type Control condition Outcome MPS ES* (95% CI)
Mixed muscle and myofibrillar FSR
Breen et al. 2011 10 males,
66.5±5.1 1.5 h cycling at
70% V
10.2 g protein and
25.4 g CHO at 0
and 0.5 h of recovery
Whey 25.2 g CHO at 0 and
0.5 h of recovery
Myofibrillar FSR
(0–4 h recovery)
1.25 (0.25–2.15)
Camera et al.
8 males,
46.7±4.4 8×5 reps at 80% 1RM,
0.5 h cycling at 70%
25 g protein at
0 h of recovery
Whey Fasted
(no nutrition)
Myofibrillar FSR
(1–4 h recovery)
0.88 (−0.19–1.85)
Coffey et al. 2011 8 males,
51.3±5.6 10×6-s maximal
sprints, 54 s recovery
24 g protein,
4.8 g leucine,
50 g CHO
Whey Fasted
(no nutrition)
Myofibrillar FSR
(0–4 h recovery)
0.99 (−0.10–1.97)
Harber et al. 2010 8 males,
53 1 h cycling at 70%
27 g protein,
62 g CHO, and 2 g fat
Milk (20% whey,
80% casein)
(no nutrition)
Mixed muscle FSR
(2–6 h recovery)
0.49 (−0.53–1.46)
Howarth et al. 2009 6 males,
48.9±3.3 2 h variable intensity
cycling at 50%–80%
0.4 g/(kg·h) protein
and 1.2 g/(kg·h)
CHO (at 15-min intervals)
from 0–3 h recovery
Whey 1.6 g/(kg·h) CHO (at
15-min intervals)
from 0–3 h recovery
Mixed muscle FSR
(0–4 h recovery)
1.51 (0.13–2.65)
Lunn et al. 2012 8 males,
53.1±1.6 45 min treadmill at 65%
16 g protein/58 g CHO
at 0 h of recovery
Milk (20% whey,
80% casein)
Mixed muscle FSR
(0–3 h recovery)
0.79 (−0.27–1.76)
Mean ES (95% CI) 0.95 (0.53–1.38)
Mitochondrial fractional synthetic rate
Breen et al. 2011 10 males,
66.5±5.1 1.5 h cycling at 70%
10.2 g protein and
25.4 g CHO at 0 and
0.5 h of recovery
Whey 25.2 g CHO at 0 and
0.5 h of recovery
Mitochondrial FSR
(0–4 h recovery)
−0.15 (−1.02–0.74)
Camera et al.
8 males,
46.7±4.4 8×5 reps at 80% 1RM,
0.5 h cycling at 70%
25 g protein at
0 h of recovery
Whey Fasted
(no nutrition)
Mitochondrial FSR
(1–4 h recovery)
0.34 (−0.67–1.31)
Coffey et al. 2011 8 males,
51.3±5.6 10×6-s maximal
sprints, 54 s of recovery
24 g protein,
4.8 g leucine,
50 g CHO
Whey Fasted
(no nutrition)
Mitochondrial FSR
(0–4 h recovery)
0.08 (−0.91–1.05)
Mean ES (95% CI) 0.07 (−0.48–0.62)
Note: 1RM, 1-repetition maximum; CI, confidence interval; CHO, carbohydrate; FSR, fractional synthetic rate; V
, maximal aerobic capacity.
*MPS ES: muscle protein synthesis effect size of protein ingestion relative to control condition.
D.M Camera, D.W.D. West, S.M. Phillips, T. Rerecich, T. Stellingwerff, J.A. Hawley, and V.G. Coffey. Unpublished.
990 Appl. Physiol. Nutr. Metab. Vol. 39, 2014
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the rates of synthesis of the force-generating myofibrillar proteins
(Breen et al. 2011). Of note is that protein ingestion has little effect
on the ability to augment postexercise rates of mitochondrial
protein synthesis (Table 1), which is in contrast to the ability of
exogenous amino acid provision to upregulate the protein syn-
thetic machinery at rest (Bohe et al. 2003). Perhaps the pre-
eminence of energy provision to support cell function and
survival and the dependence on a constant supply of ATP dictates
that mitochondrial protein synthesis is prioritized in the postex-
ercise period with fasted levels of amino acid sufficient to support
the remodelling of this vital organelle (Moore and Stellingwerff
2012). Nevertheless, given that maximal rates of muscle protein
synthesis have been reported after the ingestion of 20–25 g of
protein both at rest and after resistance exercise (Cuthbertson
et al. 2005;Moore et al. 2009), it seems prudent to recommend
that similar amounts should also be consumed after endurance
exercise to facilitate postexercise muscle remodelling.
It is presently unclear whether exercise of longer duration (i.e.,
greater than 2 h) further increases the acute requirements of
protein at the whole-body level. However, given that there is sig-
nificant oxidation of amino acids (especially leucine) during pro-
longed endurance exercise, this would seem likely. Furthermore,
intense bouts of endurance exercise result in a redistribution of
cardiac output, with a shunting of blood away from the digestive
system, and a resultant hypoxia-mediated small intestinal injury
(van Wijck et al. 2011). Such effects are likely to be exacerbated
with longer duration exercise bouts, particularly those under-
taken in either hot/humid or hypoxic environments. Ultimately,
the net effect of any exercise-induced intestinal injury as well as
the increased protein catabolism and amino acid oxidation may
have on the acute protein requirements to whole-body protein
recovery is unclear. For example, in the study by Levenhagen et al (2002),
10 g of dietary protein was sufficient to enhance muscle protein
synthesis and induce a positive net muscle protein balance after
only 60 min of moderate intensity exercise, but failed to induce a
positive whole-body protein balance. This is similar to the obser-
vations of Lunn et al. (2012) who demonstrated that the ingestion
of 500 mL of chocolate-flavored milk (16 g of protein) enhanced
mixed muscle protein synthesis despite a negative whole-body
protein balance. Collectively, these results suggest that dietary
amino acids are preferentially utilized to support greater rates of
MPS in the immediate postexercise period with remodelling of
whole-body proteins (including the gut) occurring as a secondary
process. Therefore, it is currently unclear if either a slightly
greater amount of protein or perhaps a greater number of repeat
feedings is necessary to rapidly and fully restore whole-body pro-
tein balance after endurance exercise.
Timing of protein ingestion
Before and during exercise
Protein and amino acid ingestion prior to a bout of repeated
sprints has been shown to support greater postexercise rates of
Fig. 1. Overview of the potential effects of protein ingestion on supporting the recovery from endurance-based exercise as means to enhance
endurance capacity and performance. Potential metchanisms include (i) oxidation of amino acids to be used for hepatic gluconeogenesis and
(or) deaminiation, or as a fuel source by skeletal muscle mitochondria; (ii) increases in mitochondrial protein synthesis to enhance substrate
metabolism and utilization; (iii) promotion of myofibrillar remodelling to maintain muscle protein quality and function by removing old or
damaged proteins; (iv) stimulation of net myofibrillar protein synthesis to enable greater muscle force/power output; and (v) promotion of
glycogen resynthesis when co-ingested with carbohydrate (CHO). The capacity for protein ingestion to modulate such adaptive signals may be
influenced by peripheral factors such as the timing, amount and type of protein intake. MPB, muscle protein breakdown; MPS, muscle protein
synthesis; ?, speculative/requires further research.
Net Synthesis
Remodelling Glycogen
Amino Acid
Synthesis (?)
Typ e
Increased Recovery and
Endurance Adaptaon/ Performance ?
Enhanced muscle
power output?
Breakdown + Repair
of old/damaged
and/or direct
Co-ingeson with
CHO to increase
Increased energy
producon and
substrate ulizaon?
Before: Reduce MPB during exercise?
During: Posive whole body net protein
Aer: Increased MPS to facilitate
muscle remodelling
MPS: 20-25g
Whole body net balance: >20g?
Rapidly digested, leucine-enriched
proteins sources (whey)?
Mitochondria Myofibrils Energy storage
(Liver) (Muscle)
Moore et al. 991
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myofibrillar protein synthesis (Coffey et al. 2011), which is gener-
ally consistent with findings from studies employing a resistance-
exercise stimulus (Tipton et al. 2007). These results suggest that
the recovery from relatively short, high-intensity endurance-
based exercise can be enhanced with pre-exercise protein inges-
tion. However, prolonged endurance exercise stimulates the
increased oxidation of amino acids (especially the branched chain
amino acids) as an alternative fuel source and can depress normal
rates of protein synthesis as a means to prioritize muscle energy
stores towards fuelling contraction rather than the energetically
expensive process of protein synthesis (Rose and Richter 2009). As
such, the exercise period represents a net catabolic environment,
which can lead to the breakdown of skeletal muscle proteins and
net efflux of amino nitrogen from the muscle (Howarth et al. 2010;
van Hall et al. 1999). Endurance athletes who undertake pro-
longed (i.e., >1 h) training bouts or who train multiples times per
day (not always in a glycogen-replete state) could subject their
muscles to prolonged periods of net catabolism that presently has
unknown consequences on the optimal enhancement of muscle
protein synthesis and whole body and muscle protein balance
during the postexercise recovery period.
Koopman and colleagues (2004) were the first to demonstrate
that protein/CHO co-ingestion during prolonged endurance exer-
cise in trained athletes resulted in a greater whole-body protein
oxidation compared with CHO alone. At the time it was suggested
that the greater oxidation was reflective of a greater use of dietary
as compared with body amino acids as a source of fuel, which
ultimately resulted in a more positive whole-body net protein
balance during exercise (Koopman et al. 2004). With respect to
local effects within the muscle, protein/CHO co-ingestion may
attenuate the typical exercise-induced increase muscle protein
breakdown as reflected by a decrease in amino acid release from
the muscle and a subsequently less negative net muscle protein
balance during exercise (Hulston et al. 2011). Collectively these
data suggest that athletes performing prolonged, strenuous train-
ing could benefit from the co-ingestion of protein in their daily
nutrition plan to limit the catabolic environment of exercise,
which ultimately may position them in a greater nutritional po-
sition during the postexercise recovery period. However, protein
ingestion during exercise may be of limited ergogenic value (Betts
and Williams 2010;Saunders 2007). Therefore, additional research
is necessary to elucidate the potential advantage of an attenuated
endogenous protein catabolism (either of muscle or whole body
stores) on supporting long-term training goals that are dependent
on the remodelling of skeletal muscle tissue.
Immediate (<3 h) postexercise recovery
Consistent with reports from the resistance exercise literature
(Burd et al. 2009), dietary protein ingestion after endurance exer-
cise increases postexercise muscle protein synthesis, possibly as a
means to facilitate muscle remodelling and support the recovery
process (Breen et al. 2011;Howarth et al. 2009;Levenhagen et al.
2002;Lunn et al. 2012). This is evident in the moderate to large
effect sizes on mixed and myofibrillar (but not mitochondrial)
protein synthesis after protein ingestion compared with CHO
alone (Table 1). In contrast to the relatively prolonged (i.e., ≥24 h)
sensitivity of skeletal muscle to dietary amino acids induced by a
bout of resistance exercise (Burd et al. 2011), the immediate post-
exercise recovery period may be relatively important for enhanc-
ing muscle protein synthesis and net protein balance after
endurance compared with resistance exercise. For example, de-
laying the ingestion of 10 g of dairy-based protein by 3 h markedly
attenuates the anabolic effect of the dietary protein and fails
to enhance postexercise mixed muscle protein synthesis (Levenhagen
et al. 2001). Moreover, protein ingestion after training may be
especially important for athletes chronically consuming high-
protein diets (i.e., >1.8 g/(kg·day)) as postexercise rates of mixed
muscle protein synthesis in the fasted state have been reported to
be suppressed relative to lower protein diets (Bolster et al. 2005).
This lower protein synthetic response after exercise in the fasted
state may be secondary to a diet-induced upregulation of amino
acid oxidative capacity, which subsequently may result in a re-
duced intracellular availability of amino acids for the repair and
remodelling of muscle tissue in the absence of an exogenous di-
etary source (Bolster et al. 2005;Gaine et al. 2007). Therefore,
while additional studies need to address the importance of pro-
tein timing after endurance exercise, in light of current evidence
of an attenuation of protein synthesis when feeding is delayed by
several hours (Levenhagen et al. 2001) the ingestion of dietary
protein in the first 30–60 min after endurance exercise should be
recommended to maximize rates of skeletal muscle protein syn-
thesis and enhance recovery.
Prolonged (>3 h) postexercise recovery
In addition to the immediate postexercise recovery period
(i.e., ≤3 h), we have recently determined how feeding during a
prolonged (12 h) recovery period postexercise might further
support muscle remodelling. After a single bout of resistance ex-
ercise, undertaken in the morning, we found that rates of myofi-
brillar protein synthesis and whole-body net protein balance were
greater over a 12 h day when athletes consumed 20 g of protein
every4hascompared with isoenergetic amounts given as2×40g
every 6 h (typical of a 3-square meals approach) or multiple small
feeding8×10gofevery 1.5 h (typical of a “grazing” pattern of
eating) (Areta et al. 2013;Moore et al. 2012). These data clearly
show that it is not just the quantity of protein an athlete con-
sumes that is important for chronic muscle remodelling but the
pattern of protein ingestion. Given the importance of dietary pro-
tein for enhancing muscle protein synthesis after endurance-
based exercise (Table 1), it is likely that athletes training and
competing in these activities would also benefit from a balanced
daily protein ingestion (i.e., repeated meal feedings of 20gof
protein every 3–4 h) to maximize their postexercise recovery. In
fact, given that small 10-g protein feeding appears to have little
effect on enhancing muscle rates of protein synthesis and net
protein balance 3 h after endurance exercise (Levenhagen et al.
2001), the balanced ingestion of sufficient protein intake (i.e., sev-
eral 20-g feedings) may be even more critical to sustain maximal
rates of muscle protein remodelling in endurance athletes. This
pattern of meal-feeding to sustain daily rates of muscle protein
remodelling is likely also beneficial for athletes who are in nega-
tive energy balance and who wish to maintain lean mass while
losing fat mass, as has been suggested with other athletes during
periods of weight loss (Iwao et al. 1996).
Type of protein
Dietary proteins differ in their amino acid composition and
rates of digestion and absorption (i.e., the rate of appearance of
their constituent amino acids in the blood) (Boirie et al. 1997;
Pennings et al. 2011,2012), both of which have been reported to
have measurable effects on the ability to enhance postexercise
muscle protein synthesis (Burd et al. 2009). From the standpoint of
nutritional protein quality, as characterized by the current refer-
ence criteria of protein-digestibility corrected amino acid score
(PDCAAS; for overview of definition and limitations, see
Schaafsma 2000), commonly recommended proteins for athletes
such as the dairy proteins whey and casein and the plant-based
protein soy are all considered “high quality” proteins (i.e.,
PDCAAS >1). However, given that muscle protein synthesis is primarily
regulated by the EAA content of a protein (Tipton et al. 1999a,
1999b), it is becoming evident that subtleties of dietary protein
characteristics can lead to differences in their ability to support
maximal rates of MPS after exercise and ultimately adaptation to
training (Phillips et al. 2009). For example, compared with casein
and soy sources of protein, whey protein has distinct anabolic
characteristics that result in a greater feeding-induced stimula-
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tion of muscle protein synthesis: this premise is true when in-
gested both at rest and after resistance exercise (Tang et al. 2009),
although blends of these protein sources have also been shown to
have efficacy for supporting postexercise muscle protein synthe-
sis (Reidy et al. 2013). Nevertheless, a growing body of evidence has
implicated the essential amino acid leucine as a likely mediator of
this enhanced anabolic response with whey protein because of its
ability to “switch on” the cell signalling machinery governing
protein synthesis and serve as a substrate for protein synthesis
(Drummond et al. 2008;Phillips and van Loon 2011). Moreover,
independent of its amino acid profile, the rate at which a protein
is digested and its ability to induce rapid aminoacidemia and
leucinemia can modulate the extent of muscle remodelling as
evident by the greater stimulation of myofibrillar protein synthe-
sis after resistance exercise with ingestion of 25 g of whey protein
as a single bolus as compared with an equivalent amount of whey
protein ingested as multiple small repeated pulses (West et al.
2011). This greater stimulatory effect of rapid aminoacidemia
should be considered with athletes who wish to rapidly increase
muscle protein synthesis after an exercise bout with whole foods
as protein sources in liquid form are more rapidly digested than
those in solid food matrices (Burke et al. 2012). Therefore, al-
though studies directly comparing different protein sources dur-
ing the recovery from endurance exercise are currently lacking,
athletes who wish to enhance muscle protein synthesis during the
early recovery process would meet these goals with the ingestion
of rapidly digested, leucine-enriched proteins sources such as
whey (Breen et al. 2011).
Concurrent training
It is not uncommon for athletes training for endurance sports
to engage in resistance training to specifically enhance muscle
strength, power and (or) resistance to fatigue (Aagaard and
Andersen 2010). Conversely, athletes from the majority of team
sports often have physiological demands that require a combina-
tion of strength, a high lean mass, and superior endurance and
(or) sprint/power capacity to be successful in their discipline
(Bishop et al. 2011). As such, many athletes from a spectrum of
sports engage in concurrent training whereby both resistance and
endurance-based training sessions are performed either in a sin-
gle session or during separate sessions during the same day.
Classic early studies investigating adaptation responses to con-
current training clearly demonstrated an “interference” in train-
ing adaptation when resistance and endurance training were
combined compared with when the resistance or endurance
workouts were performed in isolation (Dudley and Djamil 1985;
Hickson 1980). Potential molecular mechanisms explaining these
attenuated anabolic/strength adaptations with concurrent train-
ing have centred on alterations in muscle glycogen availability
and (or) activation of the cellular energy sensor AMP kinase
(AMPK) (Hawley 2009). However, we have reported little effect of
AMPK on anabolic cell signalling and rates of myofibrillar protein
synthesis in either the fasted (placebo ingestion) or fed (2 bever-
ages at 0 and2hofrecovery containing 20 g whey and 40 g CHO
each) state when trained subjects commenced a single bout of
strenuous resistance exercise (8 × 5 repetitions at 80% 1 repetition
maximum) with low (50% of resting, fed levels) muscle glycogen
(Camera et al. 2012). Thus, a causal relationship for reduced glyco-
gen availability or AMPK-mediated attenuation of mTORC1 signal-
ling in a concurrent training paradigm has yet to be established in
vivo human muscle.
Little research to date has examined the effect of protein inges-
tion in a concurrent training setting. We recently observed that
rates of myofibrillar, but not mitochondrial protein synthesis
were enhanced when 25 g whey protein (compared with a nonen-
ergy placebo) was consumed following concurrent resistance and
endurance exercise (Camera et al., Table 1). Thus, protein inges-
tion may reduce the potential interference effect of endurance
exercise on skeletal muscle hypertrophy with chronic concurrent
training. Although less is known regarding the effects of protein
ingestion to augment endurance training-induced adaptations
(e.g., mitochondrial vs. myofibrillar protein synthesis) after con-
current training, whey protein has been shown to support rates of
mitochondrial protein synthesis following concurrent exercise
(Donges et al. 2012). However, in the absence of a protein-free
placebo in that study (Donges et al. 2012), it is unclear if the rates
of mitochondrial protein synthesis were indeed augmented by
protein ingestion or were simply enhanced by the exercise stim-
ulus itself, similar to previous reports after endurance exercise
(Breen et al. 2011;Coffey et al. 2011;Wilkinson et al. 2008). There-
fore, protein ingestion represents a practical means to increase
anabolic adaptations with concurrent exercise. Certainly increas-
ing protein availability in these situations will not lead to dimin-
ished response–adaptations, although this is clearly a fertile area
of future research. Based on the ability of postexercise protein
ingestion to support increased rates of muscle protein synthesis
after a variety of exercises and in the absence of any plausible
evidence against, it seems prudent to recommend that athletes
involved in concurrent training modes follow similar protein
guidelines as for those athletes training solely for resistance and
power sports.
Benefits beyond muscle protein synthesis with
protein ingestion
Glycogen synthesis
As previously noted, CHOs are an important fuel for oxidative
metabolism during both repeated sprint-type training sessions
and less intense, prolonged workouts. In these situations, and in
the absence of exogenous CHO intake, muscle and liver glycogen
are the primary sources of fuel to support CHO oxidation. Even
when ingested at high rates (>1 g/min) during submaximal endur-
ance exercise, the oxidation of blood glucose cannot be the sole
source of CHO by the working muscles (Coyle et al. 1986). As
endogenous CHO stores are limited to between 400–600 g of gly-
cogen (depending on the athletes’ body mass and nutritional sta-
tus), restoration of both muscle and liver glycogen is an important
consideration for the endurance athlete. Following prolonged en-
durance exercise, muscle glycogen is typically restored to pre-
exercise levels within 24 h (Burke et al. 1995;Costill et al. 1981)
provided adequate (i.e., 1.2 g/(kg·day)) postexercise carbohydrate
is ingested (Burke et al. 2011). However, for athletes who have do
not have access to adequate CHO and (or) have a smaller window
of opportunity in which refuelling can occur (i.e., multiple train-
ing sessions and (or) competitions in a day), alternate feeding
strategies have been explored to augment rates of glycogen resyn-
thesis. One approach has been to augment normal CHO replen-
ishment strategies with small amounts of protein as a means to
promote rapid rates of muscle glycogen resynthesis and maintain
subsequent exercise performance (Beelen et al. 2010).
It has been suggested that the increased insulin response with
the co-ingestion of protein and CHO may enhance glucose uptake
in the muscle via stimulation of glucose transporters, which ulti-
mately would translate into a greater rate of muscle glycogen
resynthesis (van Loon et al. 2000a,2000b). Indeed, leg glucose
uptake has been reported to be 3.5-fold higher following co-
ingestion of protein and carbohydrate compared with CHO only
(Levenhagen et al. 2002). However, studies that have shown pro-
tein co-ingestion with carbohydrate augments muscle glycogen
synthesis during recovery have used feeding strategies that fea-
tured carbohydrate intakes that are suboptimal (<0.8 g/(kg·h)) for
maximal rates of glycogen synthesis (van Loon et al. 2000a;
Zawadzki et al. 1992). Indeed, co-ingestion of protein with CHO
does not appear to augment postexercise muscle glycogen synthe-
sis rates when adequate amounts of carbohydrate (1.2 g/(kg·h)) are
Moore et al. 993
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consumed (Burke et al. 2011;Jentjens et al. 2001). Therefore, ath-
letes aiming to maximize fuel storage (i.e., muscle and liver gly-
cogen resynthesis) should focus on attaining sufficient CHO
intake. Nonetheless, the co-ingestion of protein with CHO as a
means to replenish muscle glycogen stores may be of practical
importance in situations in which CHO cannot be consumed to
the optimal level (e.g., gastrointestinal distress, inadequate access
to CHO, etc.). Additionally, athletes engaging in multiple training
sessions a day with limited recovery times (e.g., <4 h) could benefit
from the co-ingestion of protein with CHO as a means to optimize
muscle glycogen concentrations as well as to provide amino acids
for the repair of muscle proteins.
Immune function
Periods of intensified training have been reported to predispose
athletes to a greater risk of developing upper respiratory tract
infections (Gleeson 2007), which may impair training quality and
alter the ability to recovery from illness. This increased suscepti-
bility to opportunistic infection may be related in part to a
reduced immune surveillance characterized by attenuated circu-
lating viral antigen-targeting CD8
T-lymphocytes (Gleeson 2007;
Witard et al. 2012). However, a high (3 g/(kg·day)) but not a mod-
erate (1.5 g/(kg·day)) protein diet restores the circulating concen-
tration of these important immune cells to levels that are
comparable to those measured during normal training loads. Fur-
thermore, higher protein intakes are associated with a reduction
in the self-reported incidence of upper respiratory tract infections
in athletes when undertaking intensified training loads (Witard
et al. 2012,2013). In these studies (Witard et al. 2012,2013) CHO
intake was lower than recommended levels for intense training
periods (i.e., 6 vs >8 g/(kg·day), respectively) (Burke et al. 2011),
suggesting that in the absence of optimal CHO intake, protein
ingestion may improve markers of immune function (Nieman
1998) and help mitigate the risk of developing upper respiratory
infections in athletes. Future work is required to confirm these
initial positive findings and to elucidate their clinical significance in
maintaining athlete health.
Future perspectives
Dietary protein supplementation and muscle growth are inex-
tricably linked. This is the product of a strength training culture
that promotes the use of protein supplements and a body of re-
search that unequivocally supports increased protein availability
to enhance postexercise muscle protein synthesis and remodel-
ling (Burd et al. 2009). In addition, a recent meta-analysis demon-
strates that dietary protein supplementation is associated with
greater training-induced gains in lean mass growth and strength
increases (Cermak et al. 2012).
In contrast, our current understanding of the functional out-
come of enhancing muscle protein synthesis during recovery
from endurance-based exercise is in its infancy: the role dietary
protein in supporting enhanced skeletal muscle remodelling has
only received recent scientific inquiry. Therefore, fundamental
questions of how optimal protein ingestion (i.e., amount, type,
timing) during and after endurance exercise can enhance muscle
recovery and subsequent adaptation to training need to be ad-
dressed. For example, although protein is able to enhance muscle
protein synthesis after endurance exercise, especially of the force-
generating myofibrillar proteins (see Table 1), it is unclear if this
increased protein synthesis may translate into greater muscle
mass and (or) muscle power over a period of weeks to months;
such adaptations could be viewed as beneficial for endurance ath-
letes involved in nonweight-bearing sports such as cycling, where
success is generally linked to an ability to sustain high power
outputs (Hawley and Noakes 1992). In contrast, despite a lack of
stimulation of mitochondrial protein synthesis with physiologi-
cal (i.e., 20 g) protein ingestion, the results from a number of
chronic (i.e., 4–6 weeks) studies have reported enhanced aerobic
capacity after training with postexercise protein ingestion in
young (Ferguson-Stegall et al. 2011) and older adults (Robinson
et al. 2011). Replication of these results in well-trained endurance
athletes is warranted to elucidate the potential mechanisms for
these exercise-nutrient adaptations. Finally, although moderate
(i.e., 20 g) protein ingestion appears to have little effect on the
postexercise increase in mitochondrial protein synthesis (Breen
et al. 2011), supplementation of the branched chain amino acids
(i.e., the equivalent of 10 g/day) has been reported to increase
mitochondrial biogenesis and aerobic capacity in mice (D’Antona
et al. 2010). Whether similar results can be replicated in humans
remains to be determined. Preliminary evidence suggests that
high protein feeding (i.e., 64 g over 3 h, a level that would exceed
the requirement to enhance muscle protein synthesis) during re-
covery from intense endurance exercise may elicit a gene expres-
sion profile that could be conducive to enhancing cellular energy
pathways (Rowlands et al. 2011). Therefore, future studies are
needed to elucidate the effect of maximizing muscle protein syn-
thesis and the subsequent effects on altered gene expression pro-
files with optimal protein ingestion, and on the changes in muscle
mass, muscle quality, and (or) sports performance with prolonged
periods of supplementation (i.e., training). Additionally, the rele-
vance of appropriate protein supplementation during periods of
energy deficit (as compared with energy balance) needs system-
atic exploration given the potential ergogenic benefits (e.g., re-
duced muscle soreness, enhanced exercise performance) that may
occur with periodized protein feeding during this compromised
nutritional state (Pasiakos et al. 2014).
The prevailing paradigm for the majority of athletes is that
dietary protein is for building muscle (i.e., hypertrophy). While a
vast body of research supports this “hypertrophy-centric” view,
recent research highlights a critical role for dietary protein in
supporting the recovery from endurance exercise. In addition to
the elevated protein requirements in this population, periodized
protein ingestion has been shown to augment the remodelling of
muscle and whole body proteins with endurance training. This
protein remodelling, which is primarily determined by changes in
muscle protein synthesis, is an important aspect of the acute re-
covery process after exercise that ultimately underpins the adap-
tations (e.g., greater muscle power, aerobic capacity) that accrue
with endurance training. While future research is required to
elucidate the most effective protein ingestion strategies to sup-
port and promote endurance training adaptations, the fact that
dietary protein provides the requisite building blocks for muscle
protein synthesis positions this macronutrient as a vital, and per-
haps underappreciated, component of the endurance athlete’s
nutritional armour.
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... Therefore, guidelines should focus on optimal adaptation to specific sessions of a particular training programme or phase of the season, while taking into account the subject's experience, energy demand of the programme (higher or lower CHO demand) and body composition adequacy [10,96,97]. Recent reviews show positive effects of strength training programmes on throwing, isometric endurance, maximum strength and power in handball players [98], so we could speculate that intakes around the upper ranges of the recommendations could be necessary to improve skeletal muscle remodelling and stimulate adaptations during sessions or strenuous strength training programmes [99]. However, studies assessing the effects of dietary protein in strength training programmes in handball athletes are needed. ...
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Introduction: Modern handball was introduced as an Olympic sport in 1972 and is played by more than 19 million people worldwide. Beach handball was born as an adaptation of court handball in the 1990s. Both modalities are complex and multifactorial ball games characterised by a fast pace and variable game intensities, as well as the strong influence of tactical concepts, social factors and cognitive aspects. Objective: To analyse the nutritional status of both male and female players to assess whether it is in line with specific and general dietary intake demands. Methodology: A systematic search of databases was carried out using keywords with relevant Boolean operators. Results: A total of 468 studies was identified, of which 44 studies were included: 7 on hydration; 22 studies related to energy, macronutrient and fibre intake; 23 that assessed micronutrients; 4 studies on nutritional knowledge and information sources; and 2 articles on eating disorders. A further 85 articles were included in order to cross-check results. Discussion: The need for a state of euhydration and normal plasma electrolyte levels is clear. Adequate energy intake is the cornerstone of the handball athlete’s diet to support optimal body function. The ACSM sets daily recommendations of 6–10 g CHO/kg body weight for handball, and daily protein recommendations range from 1.2 to 2.0 g PRO/kg/day and 14 g dietary fibre per 1000 kcal. Conclusion: The nutritional habits of handball players do not seem to be adequate to the demands of the sport, although these demands are not clarified. The inclusion of nutrition professionals could be a key element in the performance of these athletes.
... In support, Breen and colleagues (2011) reported an approximate 35% increase in myofibrillar protein synthesis following CHO-P co-ingestion (50.8 g CHO and 20.4 g PRO) as compared to CHO alone (50.4 g) when consumed immediately and 30-min post high-intensity cycling in an equally divided dose 26 . Adding protein to a carbohydrate-based beverage immediately after high-intensity exercise may enhance muscle protein synthesis and thus promote the repair and remodeling of acutely damaged proteins to recover muscle functionality 26,27 . ...
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Introduction: The addition of protein to a carbohydrate solution has been shown to effectively stimulate glycogen synthesis in an acute setting and enhance exercise performance in a subsequent bout of exhaustive exercise. This study examined the effects of carbohydrate-protein (CHO-P), carbohydrate (CHO), and placebo (PLA) within a 2-hour recovery period on subsequent high-intensity exercise performance. Methods: This was a randomized, single-blind between-subject design. Participants (n = 25) were assigned to consume one of three beverages during a 2-hour recovery period: PLA, CHO (1.2 g/kg bm), or CHO-P (0.8 g/kg bm CHO + 0.4 g/kg bm PRO). During Visit#1, participants completed graded exercise testing (VO2peak; cycle ergometer). Familiarization (Visit#2) consisted of 5 x 4 min intervals at 70-80% of peak power output [PPO, watts] with two minutes of active recovery at 50W, followed by time to exhaustion [TTE] at 90% PPO. The same high-intensity interval protocol with TTE was conducted pre-and post-beverage consumption on Visit #3. Results: The ANCOVA indicated a significant difference among the group means for the posttest TTE (F2,21=8.248, p=.002, ƞ2=.440) and RER (F2,21=6.811, p=.005, ƞ2=.393) values after adjusting for the pretest differences. Conclusions: Carbohydrate-protein co-ingestion was effective in promoting an increase in TTE performance with limited time to recover.
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Branched-chain amino acids (BCAA: leucine, isoleucine, and valine) are three of the nine indispensable amino acids, and are frequently consumed as a dietary supplement by athletes and recreationally active individuals alike. The popularity of BCAA supplements is largely predicated on the notion that they can stimulate rates of muscle protein synthesis (MPS) and suppress rates of muscle protein breakdown (MPB), the combination of which promotes a net anabolic response in skeletal muscle. To date, several studies have shown that BCAA (particularly leucine) increase the phosphorylation status of key proteins within the mechanistic target of rapamycin (mTOR) signalling pathway involved in the regulation of translation initiation in human muscle. Early research in humans demonstrated that BCAA provision reduced indices of whole-body and MPB; however, there was no stimulatory effect of BCAA on MPS. In contrast, recent work has demonstrated that BCAA intake can stimulate postprandial MPS rates at rest and can further increase MPS rates during recovery after a bout of resistance exercise. The purpose of this evidence-based narrative review is to critically appraise the available research pertaining to studies examining the effects of BCAA on MPS, MPB, and associated molecular signalling responses in humans. Overall, BCAA can activate molecular pathways that regulate translation initiation, reduce indices of whole-body and MPB, and transiently stimulate MPS rates. However, the stimulatory effect of BCAA on MPS rates is less than the response observed following ingestion of a complete protein source providing the full complement of indispensable amino acids.
We identify novel epigenetically regulated genes associated with train-low sleep-low paradigms. Exercise under low-carbohydrate (CHO) energy-balance (high-fat) conditions elicited a more prominent DNA hypomethylation signature 30 minutes postexercise compared with low-CHO energy-deficit (low-fat) conditions. This was enriched within IL6-JAK-STAT signaling, metabolic processes, p53, cell cycle, oxidative phosphorylation, and fatty acid metabolism. Histone deacetylase (HDAC) family members 2, 4, 10, and 11 demonstrated hypomethylation, with HDAC2 and HDAC11 possessing alternative regulation of gene expression in energy balance versus deficit conditions.
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Background Carbohydrate (CHO) and carbohydrate-protein co-ingestion (CHO-P) have been shown to be equally effective for enhancing glycogen resynthesis and subsequent same-day performance when CHO intake is suboptimal (≤0.8 g/kg). Few studies have specifically examined the effect of isocaloric CHO vs CHO-P consumption on subsequent high-intensity aerobic performance with limited time to recover (≤2 hours) in masters class endurance athletes. Methods This was a randomized, double-blind between-subject design. Twenty-two male masters class endurance athletes (age 49.1 ± 6.9 years; height 175.8 ± 4.8 cm; body mass 80.7 ± 8.6 kg; body fat (%) 19.1 ± 5.8; VO2peak 48.6 ± 6.7 ml·kg·min⁻¹) were assigned to consume one of three beverages during a 2-hour recovery period: Placebo (PLA; electrolytes and water), CHO (1.2 g/kg bm), or CHO-P (0.8 g/kg bm CHO + 0.4 g/kg bm PRO). All beverages were standardized to one liter (~32 oz.) of total fluid volume regardless of the treatment group. During Visit #1, participants completed graded exercise testing on a cycle ergometer to determine VO2peak and peak power output (PPO, watts). Visit #2 consisted of familiarization with the high-intensity protocol including 5 × 4 min intervals at 70-80% of PPO with 2 min of active recovery at 50 W, followed by a time to exhaustion (TTE) test at 90% PPO. During Visit#3, the same high-intensity interval protocol with TTE was conducted pre-and post-beverage consumption. Results A one-way ANCOVA indicated a significant difference among the group means for the posttest TTE (F2,18 = 6.702, p = .007, ƞ² = .427) values after adjusting for the pretest differences. TTE performance in the second exercise bout improved for the CHO (295.48 ± 24.90) and CHO-P (255.08 ± 25.07 sec) groups. The water and electrolyte solution was not effective in restoring TTE performance in the PLA group (171.13 ± 23.71 sec). Conclusions Both CHO and CHO-P effectively promoted an increase in TTE performance with limited time to recover in this sample of masters class endurance athletes. Water and electrolytes alone were not effective for restoring endurance capacity during the second bout of exhaustive exercise.
Skeletal muscle is essential in locomotion and plays a role in whole-body metabolism, particularly during exercise. Skeletal muscle is the largest ‘reservoir’ of amino acids, which can be released for fuel and as a precursor for gluconeogenesis. During exercise, whole-body, and more specifically skeletal muscle, protein catabolism is increased, but protein synthesis is suppressed. Metabolism of skeletal muscle proteins can support energy demands during exercise, and persistent exercise (i.e. training) results in skeletal muscle protein remodelling. Exercise is generally classified as being either ‘strength’ or ‘aerobic/endurance’ in nature, and the type of exercise will reflect the phenotypic and metabolic adaptations of the muscle. In this chapter, we describe the impact of various exercise modes on protein metabolism during and following exercise.
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Background Systematic investigation of muscle protein synthesis (MPS) responses with or without protein ingestion has been largely limited to resistance training. Objective This systematic review determined the capacity for aerobic-based exercise or high-intensity interval training (HIIT) to stimulate post-exercise rates of MPS and whether protein ingestion further significantly increases MPS compared with placebo. Methods Three separate models analysed rates of either mixed, myofibrillar, sarcoplasmic, or mitochondrial protein synthesis (PS) following aerobic-based exercise or HIIT: Model 1 (n = 9 studies), no protein ingestion; Model 2 (n = 7 studies), peri-exercise protein ingestion with no placebo comparison; Model 3 (n = 14 studies), peri-exercise protein ingestion with placebo comparison. Results Eight of nine studies and all seven studies in Models 1 and 2, respectively, demonstrated significant post-exercise increases in either mixed or a specific muscle protein pool. Model 3 observed significantly greater MPS responses with protein compared with placebo in either mixed or a specific muscle fraction in 7 of 14 studies. Seven studies showed no difference in MPS between protein and placebo, while three studies reported no significant increases in mitochondrial PS with protein compared with placebo. Conclusion Most studies reporting significant increases in MPS were confined to mixed and myofibrillar PS that may facilitate power generating capacity of working skeletal muscle with aerobic-based exercise and HIIT. Only three of eight studies demonstrated significant increases in mitochondrial PS post-exercise, with no further benefits of protein ingestion. This lack of change may be explained by the acute analysis window in most studies and apparent latency in exercise-induced stimulation of mitochondrial PS.
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Background Engaging in both resistance and endurance exercise within the same training program, termed ‘concurrent exercise training,’ is common practice in many athletic disciplines that require a combination of strength and endurance and is recommended by a number of organizations to improve muscular and cardiovascular health and reduce the risk of chronic metabolic disease. Dietary protein ingestion supports skeletal muscle remodeling after exercise by stimulating the synthesis of muscle proteins and can optimize resistance exercise-training mediated increases in skeletal muscle size and strength; however, the effects of protein supplementation on acute and longer-term adaptive responses to concurrent resistance and endurance exercise are unclear. Objectives The purpose of this systematic review is to evaluate the effects of dietary protein supplementation on acute changes in muscle protein synthesis and longer-term changes in muscle mass, strength, and aerobic capacity in responses to concurrent resistance and endurance exercise in healthy adults. Methods A systematic search was conducted in five databases: Scopus, Embase, Medline, PubMed, and Web of Science. Acute and longer-term controlled trials involving concurrent exercise and protein supplementation in healthy adults (ages 18–65 years) were included in this systematic review. Main outcomes of interest were changes in skeletal muscle protein synthesis rates, muscle mass, muscle strength, and whole-body aerobic capacity (i.e., maximal/peak aerobic capacity [VO2max/peak]). The quality of studies was assessed using the National Institute of Health Quality Assessment for Controlled Intervention Studies. Results Four acute studies including 84 trained young males and ten longer-term studies including 167 trained and 391 untrained participants fulfilled the eligibility criteria. All included acute studies demonstrated that protein ingestion enhanced myofibrillar protein synthesis rates, but not mitochondrial protein synthesis rates during post-exercise recovery after an acute bout of concurrent exercise. Of the included longer-term training studies, five out of nine reported that protein supplementation enhanced concurrent training-mediated increases in muscle mass, while five out of nine studies reported that protein supplementation enhanced concurrent training-mediated increases in muscle strength and/or power. In terms of aerobic adaptations, all six included studies reported no effect of protein supplementation on concurrent training-mediated increases in VO2max/peak. Conclusion Protein ingestion after an acute bout of concurrent exercise further increases myofibrillar, but not mitochondrial, protein synthesis rates during post-exercise recovery. There is some evidence that protein supplementation during longer-term training further enhances concurrent training-mediated increases in skeletal muscle mass and strength/power, but not whole-body aerobic capacity (i.e., VO2max/peak).
Milk and dairy products with their distinct composition of carbohydrates, proteins, fats, and micronutrients are purported to have beneficial effects on human health. They have the potential to enhance exercise performance and recovery and are considered functional sport foods/beverages. This chapter summarizes the current evidence regarding the benefits of dairy products on endurance and resistance exercise, as well as the potential to augment health and performance in a variety of populations including team sport athletes, exercising children and adolescents, and aging adults. The impact of dairy products on weight loss and sleep quality is also discussed.
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The present study examined whether a high protein diet prevents the attenuated leukocyte redistribution in response to acute exercise caused by a large volume of high-intensity exercise training. Eight cyclists (VO2max: 64.2 ± 6.5 mL kg(-1)·min(-1)) undertook two separate weeks of high-intensity training while consuming either a high protein diet (3 g kg(-1) protein·BM(-1)·day(-1)) or an energy and carbohydrate-matched control diet (1.5 g·kg(-1) protein·BM(-1)·day(-1)). High-intensity training weeks were preceded by a week of normal-intensity training under the control diet. Leukocyte and lymphocyte sub-population responses to acute exercise were determined at the end of each training week. Self-reported symptoms of upper-respiratory tract infections (URTI) were monitored daily by questionnaire. Undertaking high-intensity training with a high protein diet restored leukocyte kinetics to similar levels observed during normal-intensity training: CD8(+)TL mobilization (normal-intensity: 29,319±13,130 cells/μL× ∼165 min vs. high-intensity with protein: 26,031±17,474 cells/μL× ∼165 min, P>0.05), CD8(+)TL egress (normal-intensity: 624 ± 264 cells/μL vs. high-intensity with protein: 597 ± 478 cells/μL, P>0.05). This pattern was driven by effector-memory populations mobilizing (normal-intensity: 6,145±6,227 cells/μL× ∼165 min vs. high-intensity with protein: 6,783±8,203 cells/μL× ∼165 min, P>0.05) and extravastating from blood (normal-intensity: 147±129 cells/μL vs. high-intensity with protein: 165±192 cells/μL, P>0.05). High-intensity training while consuming a high protein diet was associated with fewer symptoms of URTI compared to performing high-intensity training with a normal diet (P<0.05). To conclude, a high protein diet might reduce the incidence of URTI in athletes potentially mediated by preventing training-induced impairments in immune-surveillance.
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Caloric restriction occurs when athletes attempt to reduce body fat or make weight. There is evidence that protein needs increase when athletes restrict calories or have low body fat. The aims of this review were to evaluate the effects of dietary protein on body composition in energy-restricted resistance-trained athletes and to provide protein recommendations for these athletes. Database searches were performed from earliest record to July 2013 using the terms protein, and intake, or diet, and weight, or train, or restrict, or energy, or strength, and athlete. Studies (N = 6) needed to use adult (≥ 18 yrs), energy-restricted, resistance-trained (> 6 months) humans of lower body fat (males ≤ 23% and females ≤ 35%) performing resistance training. Protein intake, fat free mass (FFM) and body fat had to be reported. Body fat percentage decreased (0.5% to 6.6%) in all study groups (N = 13) and FFM decreased (0.3 to 2.7kg) in nine of 13. Four groups gained or did not lose FFM. They had the highest body fat, smallest magnitudes of energy restriction or underwent novel resistance training stimuli. Two groups lost non-significant amounts of FFM. The same conditions that existed in the groups that did not lose FFM existed in the first group. These conditions were not present in the second group, but this group consumed the highest protein intake in this review (2.5-2.6g/kg). Protein needs for energy-restricted resistance-trained athletes are likely 2.3-3.1g/kg of FFM scaled upwards with severity of caloric restriction and leanness.
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We aimed to produce intrinsically L-[1-(13)C]phenylalanine labeled milk and beef for subsequent use in human nutrition research. The collection of the various organ tissues after slaughter allowed for us to gain insight into the dynamics of tissue protein turnover in vivo in a lactating dairy cow. One lactating dairy cow received a constant infusion of L-[1-(13)C]phenylalanine (450 µmol/min) for 96 h. Plasma and milk were collected prior to, during, and after the stable isotope infusion. Twenty-four hours after cessation of the infusion the cow was slaughtered. The meat and samples of the various organ tissues (liver, heart, lung, udder, kidney, rumen, small intestine, and colon) were collected and stored. Approximately 210 kg of intrinsically labeled beef (bone and fat free) with an average L-[1-(13)C]phenylalanine enrichment of 1.8±0.1 mole percent excess (MPE) was obtained. The various organ tissues differed substantially in L-[1-(13)C]phenylalanine enrichments in the tissue protein bound pool, the highest enrichment levels were achieved in the kidney (11.7 MPE) and the lowest enrichment levels in the skeletal muscle tissue protein of the cow (between 1.5-2.4 MPE). The estimated protein synthesis rates of the various organ tissues should be regarded as underestimates, particularly for the organs with the higher turnover rates and high secretory activity, due to the lengthened (96 h) measurement period necessary for the production of the intrinsically labeled beef. Our data demonstrates that there are relatively small differences in L-[1-(13)C]phenylalanine enrichments between the various meat cuts, but substantial higher enrichment values are observed in the various organ tissues. We conclude that protein turnover rates of various organs are much higher when compared to skeletal muscle protein turnover rates in large lactating ruminants.
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The purpose of this work was to determine the effects of varying levels of dietary protein on body composition and muscle protein synthesis during energy deficit (ED). A randomized controlled trial of 39 adults assigned the subjects diets providing protein at 0.8 (recommended dietary allowance; RDA), 1.6 (2×-RDA), and 2.4 (3×-RDA) g kg(-1) d(-1) for 31 d. A 10-d weight-maintenance (WM) period was followed by a 21 d, 40% ED. Body composition and postabsorptive and postprandial muscle protein synthesis were assessed during WM (d 9-10) and ED (d 30-31). Volunteers lost (P<0.05) 3.2 ± 0.2 kg body weight during ED regardless of dietary protein. The proportion of weight loss due to reductions in fat-free mass was lower (P<0.05) and the loss of fat mass was higher (P<0.05) in those receiving 2×-RDA and 3×-RDA compared to RDA. The anabolic muscle response to a protein-rich meal during ED was not different (P>0.05) from WM for 2×-RDA and 3×-RDA, but was lower during ED than WM for those consuming RDA levels of protein (energy × protein interaction, P<0.05). To assess muscle protein metabolic responses to varied protein intakes during ED, RDA served as the study control. In summary, we determined that consuming dietary protein at levels exceeding the RDA may protect fat-free mass during short-term weight loss.-Pasiakos, S. M., Cao, J. J., Margolis, L. M., Sauter, E. R., Whigham, L. D., McClung, J. P., Rood, J. C., Carbone, J. W., Combs, G. F., Jr., Young, A. J. Effects of high-protein diets on fat-free mass and muscle protein synthesis following weight loss: a randomized controlled trial.
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Body composition in a female road cyclist was measured using Dual-energy X-ray absorptiometry (DXA; five occasions) and anthropometry (ten occasions) at the start of the season (Dec - Mar), during a period of chronic fatigue associated with poor weight management (Jun - Aug), and in the following months of recovery and retraining (Aug - Nov). Dietary manipulation involved a modest reduction in energy availability to 30 - 40 kcal·kg·FFM·d-1 and an increased intake of high quality protein, particularly following training (20 g). Through the re-training period, total body mass decreased (-2.82 kg), lean mass increased (+0.88 kg) and fat mass decreased (-3.47 kg). Haemoglobin mass increased by 58.7 g (8.4%). Maximal aerobic and anaerobic power outputs were returned to within 2% of pre-season values. The presented case shows that through a subtle energy restriction associated with increased protein intake and sufficient energy intake during training, fat mass can be reduced with simultaneous increases in lean mass, performance gains and improved health.
This review considers aspects of the optimal nutritional strategy for recovery from prolonged moderate to high intensity exercise Dietary carbohydrate represents a central component of post-exercise nutrition Therefore carbohydrate should be Ingested as early as possible in the post-exercise period and at frequent (i e 15- to 30-minute) intervals throughout recovery to maximize the rate of muscle glycogen resynthesis Solid and liquid carbohydrate supplements or whole foods can achieve this aim with equal effect but should be of high glycaemic index and Ingested following the feeding schedule described above at a rate of at least 1 g/kg/h in order to rapidly and sufficiently increase both blood glucose and insulin concentrations throughout recovery Adding >= 0 3 g/kg/h of protein to a carbohydrate supplement results in a synergistic increase in insulin secretion that can, in some circumstances, accelerate muscle glycogen resynthesis Specifically, if carbohydrate has not been ingested in quantities sufficient to maximize the rate of muscle glycogen resynthesis, the inclusion of protein may at least partially compensate for the limited availability of ingested carbohydrate Some studies have reported improved physical performance with ingestion of carbohydrate protein mixtures, both during exercise and during recovery prior to a subsequent exercise test While not all of the evidence supports these ergogenic benefits, there is clearly the potential for improved performance under certain conditions, e g if the additional protein increases the energy content of a supplement and/or the carbohydrate fraction is ingested at below the recommended rate The underlying mechanism for such effects may be partly due to increased muscle glycogen resynthesis during recovery, although there is varied support for other factors such as an increased central drive to exercise, a blunting of exercise-induced muscle damage, altered metabolism during exercise subsequent to recovery or a combination of these mechanisms
The myofibrillar protein synthesis (MPS) response to resistance exercise (REX) and protein ingestion during energy deficit (ED) is unknown. We determined, in young men (n=8) and women (n=7), protein signaling, resting post-absorptive MPS during energy balance [EB: 45 kcal•(kg FFM•d)(-1)] and after 5d of ED [30 kcal•(kg FFM•d)(-1)] as well as MPS while in ED after acute REX in the fasted state and with the ingestion of whey protein (15 and 30 g). Post-absorptive rates of MPS were 27% lower in ED than EB (P<0.001), but REX stimulated MPS to rates equal to EB. Ingestion of 15 and 30 g of protein after REX in ED increased MPS ~16 and ~34% above resting EB, (P<0.02). p70 S6K(thr389) phosphorylation increased above EB only with combined exercise and protein intake (~2-7 fold; P<0.05). In conclusion, short-term ED reduces post-absorptive MPS, however, a bout of REX in ED restores MPS to values observed at rest in EB. The ingestion of protein after REX further increases MPS above resting EB in a dose-dependent manner. We conclude that combining REX with increased protein availability after exercise enhances rates of skeletal muscle protein synthesis during short term ED and could, in the long term, preserve muscle mass.
Protein supplements are frequently consumed by athletes and recreationally-active individuals, although the decision to purchase and consume protein supplements is often based on marketing claims rather than evidence-based research. To provide a systematic and comprehensive analysis of literature examining the hypothesis that protein supplements enhance recovery of muscle function and physical performance by attenuating muscle damage and soreness following a previous bout of exercise. English language articles were searched with PubMed and Google Scholar using protein and supplements together with performance, exercise, competition and muscle, alone or in combination as keywords. Inclusion criteria required studies to recruit healthy adults less than 50 years of age and to evaluate the effects of protein supplements alone or in combination with carbohydrate on performance metrics including time-to-exhaustion, time-trial or isometric or isokinetic muscle strength and markers of muscle damage and soreness. Twenty-seven articles were identified of which 18 dealt exclusively with ingestion of protein supplements to reduce muscle damage and soreness and improve recovery of muscle function following exercise, whereas the remaining 9 articles assessed muscle damage as well as performance metrics during single or repeat bouts of exercise. Papers were evaluated based on experimental design and examined for confounders that explain discrepancies between studies such as dietary control, training state of participants, sample size, direct or surrogate measures of muscle damage, and sensitivity of the performance metric. High quality and consistent data demonstrated there is no apparent relationship between recovery of muscle function and ratings of muscle soreness and surrogate markers of muscle damage when protein supplements are consumed prior to, during or after a bout of endurance or resistance exercise. There also appears to be insufficient experimental data demonstrating ingestion of a protein supplement following a bout of exercise attenuates muscle soreness and/or lowers markers of muscle damage. However, beneficial effects such as reduced muscle soreness and markers of muscle damage become more evident when supplemental protein is consumed after daily training sessions. Furthermore, the data suggest potential ergogenic effects associated with protein supplementation are greatest if participants are in negative nitrogen and/or energy balance. Small sample numbers and lack of dietary control limited the effectiveness of several investigations. In addition, studies did not measure the effects of protein supplementation on direct indices of muscle damage such as myofibrillar disruption and various measures of protein signaling indicative of a change in rates of protein synthesis and degradation. As a result, the interpretation of the data was often limited. Overwhelmingly, studies have consistently demonstrated the acute benefits of protein supplementation on post-exercise muscle anabolism, which, in theory, may facilitate the recovery of muscle function and performance. However, to date, when protein supplements are provided, acute changes in post-exercise protein synthesis and anabolic intracellular signaling have not resulted in measureable reductions in muscle damage and enhanced recovery of muscle function. Limitations in study designs together with the large variability in surrogate markers of muscle damage reduced the strength of the evidence-base.
The intake of whey, compared with casein and soy protein intakes, stimulates a greater acute response of muscle protein synthesis (MPS) to protein ingestion in rested and exercised muscle. We characterized the dose-response relation of postabsorptive rates of myofibrillar MPS to increasing amounts of whey protein at rest and after exercise in resistance-trained, young men. Volunteers (n = 48) consumed a standardized, high-protein (0.54 g/kg body mass) breakfast. Three hours later, a bout of unilateral exercise (8 × 10 leg presses and leg extensions; 80% one-repetition maximum) was performed. Volunteers ingested 0, 10, 20, or 40 g whey protein isolate immediately (∼10 min) after exercise. Postabsorptive rates of myofibrillar MPS and whole-body rates of phenylalanine oxidation and urea production were measured over a 4-h postdrink period by continuous tracer infusion of labeled [(13)C6] phenylalanine and [(15)N2] urea. Myofibrillar MPS (±SD) increased (P < 0.05) above 0 g whey protein (0.041 ± 0.015%/h) by 49% and 56% with the ingestion of 20 and 40 g whey protein, respectively, whereas no additional stimulation was observed with 10 g whey protein (P > 0.05). Rates of phenylalanine oxidation and urea production increased with the ingestion of 40 g whey protein. A 20-g dose of whey protein is sufficient for the maximal stimulation of postabsorptive rates of myofibrillar MPS in rested and exercised muscle of ∼80-kg resistance-trained, young men. A dose of whey protein >20 g stimulates amino acid oxidation and ureagenesis. This trial was registered at as ISRCTN92528122.
Background: Protein induces an increase in insulin concentrations when ingested in combination with carbohydrate. Increases in plasma insulin concentrations have been observed after the infusion of free amino acids. However, the insulinotropic properties of different amino acids or protein (hydrolysates) when co-ingested with carbohydrate have not been investigated. Objective: The aim of this study was to define an amino acid and protein (hydrolysate) mixture with a maximal insulinotropic effect when co-ingested with carbohydrate. Design: Eight healthy, nonobese male subjects visited our laboratory, after an overnight fast, on 10 occasions on which different beverage compositions were tested for 2 h. During those trials the subjects ingested 0.8 g*kg(-)(1)*h(-)(1) carbohydrate and 0.4 g*kg(-)(1)*h(-)(1) of an amino acid and protein (hydrolysate) mixture. Results: A strong initial increase in plasma glucose and insulin concentrations was observed in all trials, after which large differences in insulin response between drinks became apparent. After we expressed the insulin response as area under the curve during the second hour, ingestion of the drinks containing free leucine, phenylalanine, and arginine and the drinks with free leucine, phenylalanine, and wheat protein hydrolysate were followed by the largest insulin response (101% and 103% greater, respectively, than with the carbohydrate-only drink; P < 0.05). Conclusions: Insulin responses are positively correlated with plasma leucine, phenylalanine, and tyrosine concentrations. A mixture of wheat protein hydrolysate, free leucine, phenylalanine, and carbohydrate can be applied as a nutritional supplement to strongly elevate insulin concentrations.