Review 905

Muscle Protein Turnover in Endurance Training:

a Review

Authors T. Seene1, P. Kaasik2, K. Alev2

1
Affiliations Institute of Exercise Biology and Physiotherapy, University of Tartu, Estonia
2
Department of Functional Morphology, University of Tartu, Estonia

Key words Abstract capacity of muscle fibres. The turnover rate of

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●▶ endurance training
●▶ skeletal muscle
●▶ oxidative capacity
●▶ protein turnover
▼ myofibrillar proteins in the same muscle is dif-
There has been much debate about skeletal mus-
cle capacity to adapt to long-lasting endurance
exercise. Exercise in the aerobic zone of metabo-
lism does not result in hypertrophy of skeletal
muscle fibres but increases their oxidative capac-
ity. The duration and intensity of an exercise ses-
sion determines the time period of depressed
muscle protein synthesis and increased degrada-
tion rate during the recovery period after exer-
cise. Protein turnover characterizes the renewal
processes of muscle proteins and the functional
capacity of muscle. The turnover rate of myofi-
brillar proteins is slow in comparison with mito-
chondrial proteins and depends on the oxidative
ferent and is also different within the myosin
molecule between myosin heavy and light chain
isoforms. The turnover rate of muscle proteins
in endurance training shows the adaptation
of skeletal muscle to long-lasting exercise via
remodelling of muscle structures. Adaptational
coordination between myofibrillar and mito-
chondrial compartments shows the physiologi-
cal role and adaptational capacity of skeletal
muscle to endurance training. It is challenging
to use muscle protein turnover for the purposes
of monitoring the training process of endurance
athletes, optimizing training programs and pre-
venting overtraining.

Introduction protein, is the regulator in the conversion of

accepted after revision
June 07, 2011
Bibliography
DOI http://dx.doi.org/
10.1055/s-0031-1284339
Published online:
November 8, 2011
Int J Sports Med 2011; 32:
905–911 © Georg Thieme
Verlag KG Stuttgart · New York
ISSN 0172-4622
Correspondence
Prof. Teet Seene, PhD, DSci
Institute of Exercise Biology and
Physiotherapy
University of Tartu
Ülikooli 18
Tartu
Estonia 50090
Tel.: +372/7/375 364
Fax: +372/7/375 379
teet.seene@ut.ee
▼ chemical energy into mechanical activity. There
Adaptation of skeletal muscle to exercise training
depends on its character, oxidative capacity,
structural rearrangements of muscle fibres, the
turnover rate of proteins of the contractile appa-
ratus and fibre recovery from exercise-induced
injury [9, 21, 40, 63, 87, 90].
Endurance training does not result in hypertro-
phy of skeletal muscle fibres involved in the exer-
cise response because the level of force
production is relatively small compared to their
maximal force-generation [10]. This type of exer-
cise training results in the regulation of the
enzyme system of the Krebs cycle, electron trans-
port chain, capillary supply, changes in key meta-
bolic enzymes involved in fatty acid activation,
and increased oxygen uptake [40, 41, 101]. If
exercise training occurs mainly in the aerobic
zone of metabolism, it promotes a transition
from type II to type I fibres in skeletal muscle,
which occurs at the expense of type II fibre popu-
lation [100]. This process is related to the myofi-
brillar apparatus as myosin, the main contractile
is a clear relationship between myosin isoforms
and functional properties of the skeletal muscle.
Maximal shortening velocity is higher in muscle
fibres where myosin heavy chain (MyHC) fast
isoforms dominate as the rate of actomyosin
interaction is greater, because the size of the step
generated by single interactions is larger [15]. It
has been demonstrated that MyHC slow (I) iso-
form propelled actin filaments at a lower speed
than fast (IIb) isoforms [43].
Currently, the role of initial oxidative capacity of
muscle fibres in the development of endurance of
athletes via the turnover rate of muscle proteins
is not fully understood. There are no definite
answers to the questions where the border of
development of oxidative capacity of muscle
fibres during endurance training is and what the
limiting factors are [23]. Putative mechanisms for
the increase of muscle fibre oxidative capacity
and muscle protein turnover in parallel with
endurance development prove that there is no
1:1 relationship between these indicators. On the

Seene T et al. Muscle Protein Turnover in … Int J Sports Med 2011; 32: 905–911
906 Review
whole, the initial oxidative capacity of muscle fibres determines
the progress of endurance development in athletes but may not
guarantee the final result. The purpose of this review is to pro-
vide an overview of literature published relating to endurance
training and muscle fibre oxidative capacity and its relation to
myofibrillar protein turnover rate. This article highlights the
effects of endurance training on the renewal of the myofibrillar
apparatus, the accompanying rearrangements in the contractile
machinery and resulting skeletal muscle remodelling.
Effect of exercise intensity and duration on muscle
metabolism
Both low and high intensity exercise are important components
for endurance athletes’ training programs [53]. Endurance train-
ing programs, in a variety of forms, improve the energetic poten-
tial of muscle and result in the effective functioning of the
muscle contractile apparatus for longer periods of time
[35, 94, 109]. High intensity interval training supplemented into
the already high training volumes elicits improvements in both
short-lasting intense and prolonged exercise performance [54].
It has been shown that low volume high intensity interval train-
ing maintains an athlete′s endurance performance and muscle
oxidative potential and increases intense exercise performance
[46, 47].
Adaptation of skeletal muscle to exercise duration and intensity
changes muscle glycogen level [22] and protein synthesis rate
[72] within several hours after exercise. The post exercise
response is fundamentally more important to the state of pro-
tein metabolism changes that occur during exercise [102]. On
the other hand, the duration and intensity of an exercise session
determines the time period of depressed protein synthesis rate
and the rate of degradation of muscle protein after exercise
training, i. e. during the recovery period [49, 83, 87, 90]. It is well
known that protein synthesis is an energy consuming process
and as depicted in the context of sports performance and energy
metabolism, it is strongly related to implication recovery period.
Low cellular energy level induces in response to sustained con-
tractile process activation of the 5′adenosine monophosphate-
activated protein kinase (AMPK). AMPK reduces translational
processes and a low energy status is associated with a high rate
of protein turnover, which limits the increase of fibre size [105].
Lack of recovery also leads to changes in the skeletal muscle
myofibrillar apparatus, particularly the destruction of contrac-
tile proteins and decreased exercise performance [82, 83, 90].
Several studies have shown that in addition to type I fibres, type
II fibres, particularly IIA fibres, are also recruited during endur-
ance training [45, 82, 83, 85, 87, 88]. Due to the diversity of
molecular mechanisms in different fibre types, muscle functions
uniformly during intervention to exercise [5, 9, 31]. Changes in
myosin isoform composition during endurance training may be
qualified as qualitative remodelling of skeletal muscle by replac-
ing isoforms, which better suit the energetic adaptation to pro-
longed force-generation activity [9].
Muscle fibre oxidative capacity
The maximum rate of oxygen consumption (VO2max) per vol-
ume unit and the cross-sectional areas of striated myocytes
from different vertebrates vary across a 100-fold range [105].
Muscle fibres with high oxidative capacity are relatively small
compared to fibres with low oxidative capacity pointing to an
increase in relationships between fibre cross-sectional area and
VO2max [105]. It is necessary to mention that among striated
Seene T et al. Muscle Protein Turnover in … Int J Sports Med 2011; 32: 905–911
muscle cells, only cardiocytes have high oxidative capacity,
while skeletal muscle fibres have low (type IIB/X) and higher
oxidative capacity (type I and IIA) [76, 82, 87, 91].
VO2max is proportional to succinate dehydrogenase (SDH)
activity [12] or oxoglutarate dehydrogenase activity [13] and
consequently to the number of mitochondria [44, 71]. Muscle
fibres with a relatively large cross-sectional area had low SDH
activities and vice versa [50, 73].
It has been shown that muscle fibre can hypertrophy and
increase strength potential at the expense of endurance capacity
[105]. Type I and IIA muscle fibres have a relatively large oxida-
tive capacity and small fibre size compared to type IIB/IIX fibres.
Muscle fibre size, not necessarily the fibre type, is related to its
oxidative capacity [105]. The same authors raised the question
why high oxidative muscle fibres remain relatively small com-
pared to low oxidative muscle fibres.
It is well known that physiological function of muscle fibre type
is an outcome of MyHC isoform expressed within fibre. Some
fibres, the so-called hybrid fibres express a combination of 2 or
more MyHC isoforms [17, 93]. Laboratory animal experiments
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have shown that the relative proportions of hybrid fibres vary
significantly from muscle to muscle [17].
In human skeletal muscle, hybrid fibre types represent a signifi-
cant population of fibres, but the stability of this fibre pheno-
type is currently unclear. For example, electrical stimulation
increases the proportion of hybrid fibres [68] and mechanical
load and thyroid hormone changes the proportion of hybrid
fibres in skeletal muscle [18]. It has been shown that running
exercise declines the hybrid fibres in human skeletal muscle
[51], whereas muscle hybrid fibres are relatively refractory to
the effect of exercise in mice [32].
It is not clear yet what role hybrid fibres play in endurance train-
ing of athletes, particularly the role of these fibres in changes of
skeletal muscle oxidative capacity.
Protein synthesis and degradation in muscle fibres
It seems paradoxical that high oxidative fibres are relatively
small, but have a larger capacity for protein synthesis compared
to low oxidative fibres [105]. These fibres contain higher quanti-
ties of satellite cells, myonuclei, mitochondria, mRNA, and total
ribosomal RNA content (i. e., components of the transcription
machinery). IGF-1 expression, a stimulator of myofibrillar pro-
tein synthesis, is also higher in type I fibres [14, 96]. Myostatin,
expression inhibitor of muscle hypertrophy, is higher in type II
fibres [55, 110]. At the same time, the components of the degra-
dation machinery of muscle proteins, such as ubiquitin ligases
MAFbx and MuRF, are about 2-fold higher in fibres with higher
oxidative capacity [105]. The higher rate of protein degradation
in muscle fibres with higher oxidative capacity is balanced by a
high rate of synthesis. This may be an important factor limiting
the size of these fibres [105]. As a result of that steady state, pro-
tein turnover rate is faster in muscle fibres with higher oxidative
capacity. In these fibres, the half-life of mitochondrial protein is
the shortest although the turnover of cytochrome C is higher in
the low oxidative fibres [39].
The concept of protein turnover was described about 7 decades
ago [80]. All proteins are in a continous process of synthesis and
degradation and characterize renewal processes in the subse-
quent tissue (● ▶ Fig. 1). Amino acids that are released during
intracellular degradation of proteins are extensively reutilized
for protein synthesis within the cell or transported to other
organs where they enter intercellular recycling. The continuous

turnover of muscle proteins determines how the myofibrillar or
mitochondrial fractions balance change, and accordingly change
muscle functional capacity [64]. Muscle fibres with higher oxi-
dative capacity contain a higher level of cathepsin suggesting
that there is a higher potential for protein degradation in mus-
cles with high protein turnover [11].
The protein turnover rate in skeletal muscle fibres is very slow.
After an acute lesion or in chronic pathological conditions, satel-
lite cells are induced to proliferate and may change the protein
turnover [33].
Vertebrate skeletal muscle fibres are multinucleate cells [57]
with hundreds of thousands of myonuclei [34, 78]. Each myonu-
cleus regulates gene products within a finite volume called the
myonuclear domain [3] or DNA unit [20] and has been defined
as the theoretical volume of cytoplasm associated with a single
myonucleus [3, 4]. Cytoplasmic volume per myonucleus is
smaller in fibres expressing slow as compared to fast MyHC
[73, 103] or in fibres highly active in protein synthesis [29]. The
greater concentration of myonuclei in slow-twitch (ST) fibres
has been shown to be related to a higher rate of protein turnover
[103].
RNA and protein ratio called the RNA unit [58] and the protein
synthesis per RNA unit has been defined as the “activity” of RNA
[58] and shown as a stable indicator of protein synthesis or
effectiveness of the translation process in cell in physiological
conditions [61, 108].
About 4 decades ago, it was shown that the protein turnover rate
depends on the type of muscle [28] and even functionally related
proteins such as myofibrillar proteins have different speed of
renewal [79]. It was shown that a relationship exists between
the turnover rate of myofibrillar protein and quantity of mito-
chondria in muscle [28, 98].
The concept of plasticity of skeletal muscle [30, 65] enables
fibres to adapt themselves to different genetic and environmen-
tal influences on the cellular and molecular level, which in turn
lead to the changes in metabolic functions [31]. According to
contemporary understanding, muscle protein turnover rate may
be used for diagnostic purposes of muscle diseases and training
monitoring.
Changes in the turnover rate of myofibrillar proteins character-
ize the renewal processes in the contractile apparatus during
adaptation to increased functional activity [66, 67]. As muscle
fibres have limited capacity for hypertrophy and increase oxida-
Increase in DNA Unit Number
Hypertrophy
Increase in Protein Synthesis Rate Ratio
between
Protein
Muscle Fibre
Synthesis
Oxidative Capacity
Rate and
Nucleus RNA Protein
Protein
Degradation
Rate
Increase in Protein Degradation Rate
Atrophy
Decrease of DNA Unit Numbers
Review 907
tive capacity at the same time, it shows that a competition exists
between the turnover rate of myofibrillar and mitochondrial
proteins [105]. It has been demonstrated that the turnover rate
of MyHC isoforms does not only show differences between the
muscles of different twitch characteristics, but also between
fast-twitch (FT) muscles, and the turnover rate is faster in FT
muscles with a higher oxidative potential [82].
Faster myosin turnover rate supports qualitative remodelling FT
muscle with higher oxidative capacity so that the former pattern
of MyHC and myosin light chain (MyLC) isoforms changes. This
process shows that muscles with higher oxidative capacity adapt
faster to the new condition [30].
In the light of recent findings, the expression of specific contrac-
tile, regulatory and minor protein isoforms is a relevant, though
not the only mechanism of regulation of heterogeneity and plas-
ticity of skeletal muscle. The pattern of MyHC isoforms in skele-
tal muscle might change for several reasons.
Effect of endurance training on interaction between
mitochondria and sarcomeres
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Skeletal muscle oxidative capacity increases with endurance
training and the decline in oxidative capacity is related to the
reduction in fitness [74]. Endurance training stimulates mito-
chondrial biogenesis and improves their functional parameters
[42, 56]. Exhaustive endurance exercise produces undesired
effects and results in a marked decrease in cytochrome c/aa3
ratio by about 37 % in striated muscles with high oxidative
capacity (heart muscle), and the reason for the deficit of cyto-
chrome C is the disruption of the outer membrane [48]. Studies
in skeletal muscle have shown a potential role of mitochondrial
impairment during exhaustive exercise and subsequent muscle
fibre damage [87, 89].
It has been shown in striated muscles with high oxidative poten-
tial that intracellular phosphotransfer systems constitute a
major mechanism linking mitochondria and ATPases within
specific structures − intracellular energetic units [76, 92]. Mito-
chondria are precisely positioned between the myofilaments
throughout the whole muscle due to the fixed juxtaposition of
mitochondria with sarcomeres [104]. The effectiveness of meta-
bolic signalling strongly depends on structural-functional rela-
tionships of the interaction between mitochondria and
sarcomeres [91]. Under conditions of hypoxia, the connections
between mitochondria and sarcomeres are disturbed as sarcom-
Fig. 1 Protein turnover in muscle fibre. Protein
turnover is a continuous process determined by
the ratio between protein synthesis and degrada-
tion rate. Protein turnover rate is faster in muscle
fibres with higher oxidative capacity. Protein
turnover characterizes renewal processes in mus-
cle fibres and, accordingly, changes in muscle func-
tional capacity. Faster turnover of muscle proteins
Protein
also provides faster regeneration of fibres and their
Turnover
readiness for the next endurance training load.
Rate
Seene T et al. Muscle Protein Turnover in … Int J Sports Med 2011; 32: 905–911
908 Review
eric components disintegrate the muscle cell structure and
cause cell injury and death [91]. The activation of apoptosis may
be partly responsible for the initiation of protein degradation
and loss of muscle nuclei associated with local atrophy [27]. For
example, the disruption of desmin impairs the linking of mito-
chondria to Z-disc and skeletal muscle exhibits impaired oxida-
tive phosphorylation [75]. AMPK becomes activated in skeletal
muscle during acute bouts of exercise [8]. AMPK′s main function
is to monitor the energy status of muscle fibres and maintain
muscle energy homeostasis [62].
Long-lasting endurance exercise may lead to the depletion of the
energy system, neuromuscular fatigue and muscle damage [1].
Children have less muscle mass than adults and generate lower
absolute power during high-intensity exercise. Children′s mus-
cles are better equipped for oxidative than glycolytic pathways
during exercise and have a lower ability to activate their type II
muscle fibres [70]. Skeletal muscle oxidative capacity increases
with endurance training and an age-associated decline in oxida-
tive capacity is related to the reduction in fitness [74]. Aerobic
endurance training can positively influence structural changes
in capillarity [36].
Type IIB muscles exhibit increased ADP concentrations in
response to an increased workload, which conforms to the respi-
ratory control theory in skeletal muscle [75].
Exhaustive exercise and ROS
Exhaustive exercise stimulates the generation of reactive oxygen
species (ROS), which damage muscle cells, being side products of
oxidative phosphorylation, due to univalent reduction of molec-
ular oxygen by electrons leaking from the respiratory chain
[26, 69] and induce damage of this chain [59]. Mitochondria are
the source and target of ROS because complexes I and III of the
electron transport chain are the main sites of mitochondrial
superoxide production [38, 60]. The magnitude of changes in
exercise induced ROS depends on the type of muscle fibre [7] as
cellular Ca2+ overload activates the degradation of muscle pro-
teins and membrane phospholipids via Ca2+ dependent proteo-
lytic and phospholipolytic pathways [6]. Ca2+ overload results in
the uptake of Ca2+ into mitochondria [99], reduces mitochon-
drial capacity to synthesize ATP and causes damage of mito-
chondrial membranes.
Effect of endurance training on contractile protein
turnover
Changes in muscle protein turnover rate during endurance
training may be regarded as an adaptation of a tissue or cells to
long-lasting low intensity functional activity. This adaptation
provides a rapid means for the redistribution of amino acids into
new proteins as they are required because amino acids are
derived from protein breakdown and incorporated into the
newly synthesized protein. Aerobic exercise stimulates protein
turnover by increasing muscle protein degradation and synthe-
sis in the recovery phase after exercise [19]. The turnover rate of
MyHC and MyLC isoforms provides a mechanism by which the
type and amount of protein can be changed in accordance with
the needs of the contractile machinery during adaptation to
endurance training [2, 82].
Activity patterns of muscle fibres where MyHC I and IIa isoforms
are dominant have relatively high oxidative capacity and are
recruited during endurance exercise [85]. It has been shown that
in rat FT plantaris (Pla) and extensor digitorum longus (EDL)
muscles, the difference in oxidative capacity is about 10 % [82].
Seene T et al. Muscle Protein Turnover in … Int J Sports Med 2011; 32: 905–911
Endurance exercise training increased the oxidative capacity in
Pla muscle by 16 % and in EDL muscle by 12 % [82]. How much of
gene expression of MyHC isoforms is due to genetic predisposi-
tion and how much to the specificity of training is unresolved
[9]. Differences in MyHC isoforms turnover rate between FT
muscles show that the turnover rate is faster in muscles where
oxidative capacity is higher [82]. Changes in MyHC isoforms’
turnover rate in FT muscles during endurance training also char-
acterize changes in myofibrillar apparatus through protein
metabolism. The latitude of changes (increase, decrease) in
myosin isoforms turnover rate also shows the significance of
MyHC isoforms in the process of adaptation to endurance train-
ing. Although the exact role of MyLC isoforms in FT muscles dur-
ing endurance training is not fully known, changes in MyLC
isoforms’ relative content and their relation to the character of
training show that they play an important role in the process of
modulation of the contractile machinery during the increase of
oxidative capacity and degradation rate of contractile proteins
[2]. There is still no answer to the question whether other myofi-
brillar proteins can modulate the functional properties of
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myosin during endurance training and if it is dependent on the
training volume. C-protein, which binds either myosin and actin
or affects the mechanical properties of myosin cross-bridges by
linking the S2 segment of myosin to the backbone of the thick
filament [37], has shown to be very sensitive to high training
volume [83]. C-protein together with MyHC isoforms plays the
key role in changes of functional properties of the contractile
machinery during excessive increase in endurance training
volume [83].
Role of MyHC and MyLC Isoforms in endurance training
During the last 2 decades, it has been shown that among multi-
ple isoforms of muscle proteins MyHC and MyLC isoforms play
an important role in muscle function. These 2 isoforms of the
myosin molecule have a different turnover rate. MyLC isoforms
turnover is faster than MyHC and their recovery dynamics from
endurance exercise are also different [84]. Simultaneously with
increased contractile protein degradation, endurance training
also increased the degradation rate of MyHC isoforms [83, 87].
The degradation rate of MyHC isoforms increases in spite of the
increase of oxidative potential of FT skeletal muscle. The decrease
of expression of MyHC IIb isoform in FT muscles is caused by the
intensive degradation of the isoform during endurance training,
which is probably the main reason for unchanged turnover rate
of MyHC IIb isoform in endurance trained rats [77]. During the
adaptation to long-lasting endurance exercise, a decrease of
MyHC IIb isoform in FT skeletal muscle shows the transforma-
tion of muscle contractile apparatus in accordance with the
increase in muscle oxidative capacity and does not necessarily
show the decrease of muscle contraction speed.
It has been claimed that in order to better understand the role of
MyLC in skeletal muscle, it is necessary to study changes in MyLC
in parallel with the quantification of MyHC under the same con-
ditions [107]. During muscle atrophy of different genesis, it has
been shown that MyLC 1fast and 2fast isoforms increase in parallel
with the increase in the relative content of MyHC IIb isoforms
[25]. A decrease in the relative content of MyLC 1fast isoform is an
indicator of the slowing of muscle contraction [37]. This stand-
point has been supported in rat skeletal muscle by decreasing
MyLC 1fast isoform in the following direction EDL→Pla→ dia-
phragm (Dia) →soleus (Sol) muscle [2].

It has been demonstrated that a positive correlation exists
between MyHC IIb isoforms, MyLC 3fast isoform relative content
and muscle contraction speed [15]. In some studies, a positive
correlation was also found between MyLC 3fast/MyLC 1fast iso-
forms ratio and contraction speed [16, 97], but others did not
support this standpoint [52] or it was shown that the above-
mentioned relation only exists between ST and FT muscles but
not between different FT muscles [2]. Higher apparent affinities
were found between the MyLC 3fast isoform and MyHC IIb and IId
isoforms [95, 106].
The distribution of MyLC isoforms in different muscles has
shown that in ST muscle the distribution of dominating slow
isoforms is wider than that of fast isoforms, and this shows the
physiological role and adaptational capacity of MyLC isoforms in
skeletal muscle to everyday movement activity, and exercise
since ST muscle mainly participate in the process of slow move-
ments and keeping static position [2].
MyLC 3fast isoform has been shown to increase in rat Pla muscle
as well as in EDL muscle during endurance training. The MyLC
alkali isoforms content as well as MyLC regulatory isoforms con-
tent does not change in FT muscles during endurance training
[82]. The decrease of slow isoforms, both in alkali and in regula-
tory MyLC, during endurance training and the increase of MyLC
3fast isoform in FT muscle are at first glance not in agreement
with changes in MyHC isoforms pattern. However, the stoichom-
etry of these subunits and their association with each other do
not change [2, 82] and this shows that there are no definite adap-
tational borders between MyHC and MyLC isoforms in FT mus-
cles to endurance exercise [2, 81].
This adaptational process shows coordination between changes
in oxidative capacity and contractile machinery in skeletal mus-
cle during the adaptation to endurance exercise training mainly
in relation to muscle metabolism. Adaptational processes in FT
muscles during endurance training show the high potential of
recruiting these muscles in endurance training [82].
Effect of excessive volume of endurance training
Excessive volume of endurance training leads to exercise intoler-
ance. In skeletal muscle, decreased capillarization may impair
the exchange of oxygen between capillaries and muscle tissue
and this contributes to exercise intolerance [24] and explains
the changes in MyHC pattern in FT muscle during an excessive
increase of endurance training volume [85].
Chronic exhaustive endurance exercise leads to the decrease of
both DNA and RNA units in FT skeletal muscle [85]. Excessive
volume of endurance training and lack of recovery lead to the
decrease of physical work capacity [85]. There are several rea-
sons for the decrease of physical work capacity: training stimu-
lus lasts too long in each exercise session and is too frequent,
which interrupts the recovery phase and the necessary adapta-
tion does not occur [90]. The decrease of the DNA content, DNA
units and RNA units in skeletal muscle are typical for exercise
caused or glucocorticoid caused myopathic muscles [86, 90].
The decreased myofibrillar protein synthesis rate, increased
degradation rate, and slower turnover rate are indicators that
refer to excessive volume of endurance training and develop-
ment of myopathy [86, 87, 90]. In contrast, in myopathic muscles
heat shock protein synthesis rate increases, which shows the
increased stress tolerance of affected muscle fibres and cellular
repair process [77, 90].
Review 909
Conclusion
▼
Recent evidence suggests that a constant increase of endurance
training volume is not the only way to improve athletes’ com-
petitive results, but it is reasonable to assume that an increase of
muscle strength capacity is possible at the expense of endurance
capacity. Endurance training stimulates mitochondrial biogen-
esis and an increase of skeletal muscle oxidative capacity.
Exhaustive endurance exercise results in a marked decrease in
cytochrome C/aa3 ratio in skeletal muscle with higher oxidative
capacity. Disruption of minor muscle protein desmin impairs
the linking between mitochondria and myofibrils and muscle
exhibits impaired oxidative phosphorylation. Muscle protein
turnover demonstrates the continuous process of protein syn-
thesis and degradation, characterizing renewal processes, and
functional capacity of muscle. The turnover of contractile pro-
teins provides a mechanism by which the type and amount of
protein can be changed in accordance with the needs of the con-
tractile machinery during adaptation to endurance training. Aero-
bic exercise stimulates protein turnover by increasing muscle
Downloaded by: Florida International University. Copyrighted material.
protein degradation and synthesis in the recovery phase after
exercise, while exhaustive exercise conversely elicits slower turn-
over rate of contractile proteins. The turnover rate of contractile
proteins depends on the oxidative capacity of muscle fibre.
Changes in myofibrillar protein turnover rate may be regarded as
the remodelling of contractile machinery during endurance train-
ing supporting the energetic adaptation of muscle.
Muscle proteins turnover rate is applicable in monitoring the
training process of endurance athletes and enables to optimize
training programs and prevent overtraining.
Acknowledgements
▼
This study was supported by the funds of the Ministry of Educa-
tion and Research of the Republic of Estonia, research project
number SKKSB1787.
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