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To cite this article: H. J. Green (1997) Mechanisms of muscle fatigue in intense exercise, Journal of Sports
Sciences, 15:3, 247-256, DOI: 10.1080/026404197367254
To link to this article: http://dx.doi.org/10.1080/026404197367254
The manifestations of fatigue, as observed by reductions in the ability to produce a given force or power, are
readily apparent soon after the initiation of intense activity. M oreover, following the activity, a sustained
weakness may persist for days or even weeks. The mechanism s responsible for the impairment in performance
are various, given the severe strain imposed on the multiple organ systems, tissues and cells by the activity.
At the level of the muscle cell, ATP utilization is dramatically accelerated in an attempt to satisfy the energy
requirements of the major processes involved in excitation and contraction, namely sarcolemm al Na + /K +
exchange, sarcoplasmic reticulum Ca 2 + sequestration and actomyosin cycling. In an attempt to m aintain ATP
levels, high-energy phosphate transfer, glycolysis and oxidative phosphorylation are recruited. W ith intense
activity, ATP production rates are unable to match ATP utilization rates, and reductions in ATP occur
accom panied by accumulation of a range of metabolic by-products such as hydrogen ions, inorganic
phosphate, AM P, ADP and IM P. Selective by-products are believed to disturb Na + /K + balance, C a2 + cycling
and actomyosin interaction, resulting in fatigue. Cessation of the activity and normalization of cellular energy
potential results in a rapid recovery of force. This type of fatigue is often referred to as metabolic.
Repeated bouts of high-intensity activity can also result in depletion of the intracellular substrate, glycogen.
Since glycogen is the fundamental fuel used to sustain both glycolysis and oxidative phosphorylation, fatigue
is readily apparent as cellular resources are exhausted.
Intense activity can also result in non-m etabolic fatigue and weakness as a consequence of disruption in
internal structures, m ediated by the high force levels. This type of impairment is most conspicuous following
eccentric muscle activity; it is characterized by myo brillar disorientation and damage to the cytoskeletal
framework in the absence of any m etabolic disturbance. The speci c mechanism s by which the high force levels
prom ote muscle damage and the degree to which the damage can be exacerbated by the metabolic effects of
the exercise rem ain uncertain.
Given the intense nature of the activity and the need for extensive, high-frequency recruitment of muscle
bres and motor units in a range of synergistic m uscles, there is limited opportunity for compensatory
strategies to enable perform ance to be sustained. Increased fatigue resistance would appear to depend on
carefully planned programm es designed to adapt the excitation and contraction processes, the cytoskeleton and
the metabolic systems, not only to tolerate but also to minimize the changes in the intracellular environment
that are caused by the intense activity.
K eywords : Calcium, cytoskeleton, eccentric activity, bre types, m uscle damage, potassium.
Introduction
C hest heaving and recoiling in uncontrolled pitch.
Lungs locked in a desperate struggle for oxygen. Heart
pounding in incessant rhythm. Skin ushed and blanketed by sweat; legs unresponsive to higher authority;
m ind tormented by pain; the joy of effort denied.
To the participant who has engaged in intense and
sustained exercise, the sym ptom s described represent a
hum iliating and distasteful experience, vividly etched
into the deepest recesses of the m ind. To the physiolo0264 -0414/97
gist, however, this behaviour is intriguing and challenging. It is intriguing because of the severe insult im posed
by this form of exercise on a wide range of physiological
system s. It is challenging because of the dif culty in
isolating the m echanisms for the inability to sustain
perform ance am ong a com plexity of changes in the
m ultiple systems, organs, tissues and cells of the
body.
In this review, a prim ar y objective is to provide
insights into the possible causes of the rapid and profound fatigue which results from participation in
248
Green
expends energy in the form of ATP to pum p both N a +
and K + against their concentration gradients. The
enzym e involved, for hydrolysing the AT P and producing the necessary energy for this process, is embedded
in the m embrane and is called the N a + /K + -AT Pase
(Clausen and N ielsen, 1994). It is apparent that if the
sarcolem m a and the T-tubule m embranes are to conduct action potentials at a high rate, necessary for the
m axim al activation of the bre, the pum p m ust possess
a high AT Pase activity, and a high capacity for rapid
AT P hydrolysis and rapid production of free energy.
O nce the excitation is inside the cell, it m ust also be
rapidly conducted from the T-tubule m embrane to the
sarcoplasm ic reticulum and speci cally the region of
the calcium release channel, located prim arily in the
term inal cisternae and in apposition to the T-tubules
(M elzer et al., 1995). The speci c m echanisms involved
in the transm ission of the excitation signal from the Ttubule to the term inal cisternae are not yet fully understood. Recent developm ents suggest that receptors
located in the T-tubule m em brane, labelled dihydropyridine receptors, are capable of conducting a charge and
initiating m ovem ent of speci c m olecules. The m ovem ent of these m olecules is believed to unblock the calcium release channel in the sarcoplasm ic reticulum ,
allowing calcium (C a 2 + ) to escape to the surrounding
cytoplasm and resulting in an increase in the levels of
free Ca (C a 2f + ). As with sarcolem m a and T-tubules,
excitation -contraction coupling m ust rem ain responsive to elevate C a 2f + for m axim al activation of the myo brillar apparatus. In most skeletal m uscles,
approximately a 100-fold increase is necessary (M elzer
et al., 1995).
T he generation of high force levels depends on the
Ca 2 + signal begin translated via the regulatory proteins,
troponin and tropom yosin, leading to a transform ation
of actomyosin from a weak binding to a dominant
strong binding, force-generating state (M oss et al.,
1995). Weak to strong binding is mediated via activation of an AT Pase, located in the myosin heavy chains
(myosin ATPase), which allows for generation of free
energy via ATP hydrolysis and the release of the m etabolic by-products AD P and inorganic phosphate. H igh
levels of myosin ATPase (actomyosin) are essential for
work perform ed at high velocities (M oss et al., 1995).
T he generation of high force levels by m uscle bres
also depends on the ability to control Ca 2 + removal
from the cytoplasm rapidly. This property prim arily
resides in the sarcoplasm ic reticulum and predominantly in the longitudinal reticulum of the sarcoplasmic
reticulum where an enzym e, the C a 2 + AT Pase, is
located. This enzym e, as with the other major enzym es
involved in excitation and contraction, is capable of
hydrolysing ATP for the production of the energy necessary to pum p the cytosolic Ca 2 + against a concentra-
249
supply the energy for restoring N a + /K + gradients across
the sarcolem m a and T-tubules, re-sequestering Ca 2 +
into the sarcoplasm ic reticulum and for the actomyosin
power stroke. T he energy supplying system s, oxidative
phosphorylation, glycolysis and high-energy phosphate
transfer, m ust be precisely geared to regenerate ATP at
a rate necessary to prevent any substantial depletion of
AT P, which exists only in low concentration in the
m uscle. T hese m etabolic pathways differ widely in the
rate at which ATP can be synthesized and consequently
are specialized to subserve the energy requirem ents of
speci c m echanical tasks. D uring single repetitions of
intense contractile activity, for exam ple, the hydrolysis
of phosphocreatine serves as a prim ar y source of regeneration of ATP from AD P. The rate at which this system
can regenerate AT P is far in excess of that w hich can be
hydrolysed by the m ajor AT Pase enzym es involved in
supplying energy for speci c excitation and contraction
functions (C onnett et al., 1990; Hochachka, 1994).
M oreover, given the equilibrium nature of the creatine
phosphokinase reaction, the ux is intim ately sensitive
and protective of reductions in AT P concentration
(Connett et al., 1990). D epending on the tem poral
characteristics of the intense contractile cycle, glycolysis may also contribute extensively to the stabilization
of AT P levels. This system , although possessing a lower
capability for peak AT P production than the highenergy phosphate transfer system , is also capable of
being
rapidly
activated
and
generating AT P
(Hochachka, 1994). According to current thinking,
AT P production is com partmentalized with the synthesis located near the ATP hydrolysing enzym es (K orge,
1995). According to this concept, both phosphocreatine and glycolysis serve to regenerate AT P via enzym es
which are bound to structures in close proximity to the
site of AT P utilization. In this model, oxidative phosphorylation is viewed as a m eans of synthesizing phosphocreatine via AT P production, which then diffuses to
the site of utilization (Korge, 1995). Indeed, the mitochondria them selves also appear to be strategically
positioned in different regions to the cell (Howald,
1982).
M uscle bre types differ dram atically in the expression of the m etabolic pathways used for AT P production (Hochachka, 1994). Fast-twitch bres, for
exam ple, given their high capability for AT P utilization,
also possess a high potential for high-energy phosphate
transfer and glycolysis. In contrast, slow-tw itch bres
possess m etabolic pathway specialization geared to
aerobic ATP production. T hese bres are invariably
characterized by a low potential for high-energy phosphate transfer and glycolysis and a high potential for
oxidation phosphorylation. A population of the fasttwitch bres may also possess a high m itochondrial
content and, consequently, a high potential for the
250
aerobic synthesis of ATP (G reen, 1995b). Although
preferential recruitm ent of fast-twitch bres m ay be
desirable during intense exercise, given the specialized
capability for high rates of ATP synthesis, this does not
appear to be the case. The recruitment of slow-twitch
bres within a m uscle appears to be invariable regardless of the force generated (Deluca, 1985).
Green
propriate response from the sarcoplasmic reticulum .
The inappropriate response could result from reductions in Ca 2 + release or from reductions in Ca 2 +
sequestration. D irect m easurem ent of cytosolic Ca 2 +
levels with repetitive activity is not possible in situ, but
these m easurem ents can be m ade in single intact bre
preparations w ith the use of uorescent dyes (Allen et
al., 1995). These studies have found depressions in
cytosolic C a 2f + in conjunction with depressed force levels, the reduction in Ca 2f + being prim arily attributed
to a reduction in C a 2 + release from the sarcoplasm ic
reticulum (Allen et al., 1995). At high force levels and
high excitation levels, the reduction in Ca 2 + release has
been attributed not so m uch to a problem at the level of
the Ca 2 + release channel itself, but to a failure in excitation (Allen et al., 1995). Although there is minim al
experim ental evidence, excitation -contraction coupling
is not considered lim iting (Fitts, 1994). Single bre
studies are m ore conclusive in attributing a failure at
the level of the sarcoplasm ic reticulum to less intense
schedules of contractile activity (Allen et al., 1995).
However, the lim itation in single bre experim ents with
an im posed and stereotyped activation pattern cannot
provide for possible accom m odation strategies. Evidence has been provided (Bigland-R itchie and Woods,
1984), although still som ewhat controversial (Enoka
and Stuart, 1992), using needle electrodes inserted into
the m uscle, of a reduction in ring frequency coinciding with a prolongation of relaxation tim e. The lower
ring frequency m inim izes excitation failure while still
retaining the minim al frequency necessar y to activate
fully the partially fatigued muscle. U nder these circum stances, the loss of force that occurs could well reside in
the sarcoplasm ic reticulum or som e process m ore distal
to the sarcoplasm ic reticulum , such as the myo brillar
com plex.
O ther evidence of sarcoplasm ic reticulum dysfunction, albeit indirect, com es from in vitro studies. In
these studies, sam ples of the m uscle tissue are harvested after the exercise and sarcoplasm ic reticulum function is studied in hom ogenates or fractions highly
enriched with sarcoplasm ic reticulum m embrane.
Under such conditions, high-intensity exercise has
been shown to depress C a 2 + uptake and Ca 2 + AT Pase
activity in both horses (Byrd et al., 1989) and hum ans
(Gollnick et al., 1991). The depression in Ca 2 + sequestering abilities, m easured under supposedly optim al
conditions, suggests a persistent change in the Ca 2 +
AT Pase enzym e, possibly at the adenine nucleotide
binding site (G reen, 1995a), which renders part of the
Ca 2 + AT Pase population dysfunctional and incapable
of accum ulating Ca 2 + into the lum en of the sarcoplasm ic reticulum . There is a possibility also that the Ca 2 +
release channel m ay be adversely affected in intense
exercise. Prolonged running in rats has been shown to
251
tim es during the activity by superim posing a brief, electrical stim ulus to the m otor nerve or muscle directly
(Bigland-R itchie and Woods, 1984; Enoka and Stuart,
1992; G andevia, 1992). T he fact that the m uscle can
demonstrate som e positive response under these circum stances has been used as evidence for a failure in
central com m and. M ore recent work, using direct
transm agnetic stimulation to the m otor areas of the
brain, has also identi ed a central com ponent contributing to the fatigue observed during intense, small
m uscle group activity (G andevia et al., 1996).
T he peripheral mechanism s underlying the fatigue
obser ved during repetitive, high force-generating activity appear to have both non-m etabolic and m etabolic
com ponents (Davies and W hite, 1981; M oussavi et al.,
1989). T he non-m etabolic com ponent of fatigue
appears to exist independently of a disturbance in the
energetic potential of the m uscle bre. This type of
fatigue appears to be m ediated as a result of the high
repetition forces that are generated and which results in
m uscle dam age (Newham et al., 1983; Byrnes et al.,
1985; Frid e n and L eiber, 1992). Although concentric
activity can produce som e degree of damage to the
m uscle cell (Frid e n and Ekblom , 1988), eccentric exercise, m ost probably because of the m uch higher force
levels that can be generated, have the m ost lethal effect.
At various tim es, the damage has been characterized by
sarcoplasm ic sarcolemm a disruption, Z-band stream ing, myo brillar disorganization, leukocyte and phagocyte in ltration, central nuclei, loss of cytoskeletal
proteins such as desm in and bre necrosis (Arm strong
et al., 1991; Frid e n and Leiber, 1992; Leiber et al.,
1996). Such exercise-induced muscle dam age is also
comm only associated with soreness and swelling of the
tissue.
T he post-exercise degenerative changes are believed
to be exacerbated by one or m ore of several potential
m echanism s, including activation of proteolytic
enzym es such as calpain, generation of oxygen free
radicals and an autophagic response resulting from the
invasion of phagocytes and increases in lysosom al acid
hydrolysis in the injured m uscle cell (Arm strong et al.,
1991; Frid e n and Leiber, 1992).
Regardless of the m echanism , the dam age appears to
result in a pronounced weakness, the recovery of
which, at least in unconditioned individuals, m ay take
several days or even weeks (Newham et al., 1983;
Clarkson and Trem blay, 1988). D uring high-intensity
activity, this non-m etabolic com ponent would be
expected to be progressive w ith the duration of the
activity and, in fact, m ay represent a m ajor aspect of
the fatigue observed. High-intensity exercise perform ance is impaired if attempted before recovery from this
form of weakness is com plete (Sargeant and D olan,
1987). Since the activity is at near m axim al levels, there
252
rem ains only a lim ited ability to increase ring frequency or recruit other motor units and synergistic
m uscles.
M etabolic fatigue or fatigue associated with the energetic changes in the m uscle would appear to be intim ately involved in the ability to sustain high-intensity
exercise. The actual manifestation and progression of
fatigue depend to a large extent on the ratio of the time
of contraction to the tim e of relaxation or recovery.
T his ratio, de ned as the duty cycle, is m ost conspicuous during dynam ic activity, where a period of m uscle
shortening is characteristically followed by a period of
m uscle relaxation w hen the m uscle is returned to its
original position by antagonistic m uscles, before the
beginning of the next repetition. In cycling, the m uscles of the opposite leg perform this function, such that
the m uscles of the thrust leg are only on duty for a
m axim um period of 50% of the tim e. In actual fact, the
duty cycle for each of the m uscles appears to be m uch
less than 50% (G reen and Patla, 1992). T he duty cycle
is a m ajor factor in the relative im portance of m etabolic
pathways used for AT P supply.
As previously emphasized, a single m ovement, even
at m axim al force levels, can be perform ed without serious threat to ATP levels by using phosphocreatine to
regenerate AT P. However, as the num ber of repetitions
increases and depending on the duty cycle, activation
of both glycolysis and oxidative phosphorylation is
essential in m aintaining adequate levels of AT P. D uring
the recover y phase, replenishm ent of phosphocreatine
stores depends on the AT P regenerated from aerobic
processes, a process that even at peak levels of oxidative
2 m ax) takes m inutes to com plete
phosphorylation ( VO
(H arris et al., 1976). As a consequence, glycolysis generally assum es increasing im portance as the number of
repetitions is increased. D uring this period, the m itochondria are also increasingly activated and the ATP
supplied by oxidative phosphorylation becom es progressively m ore im portant both during the contractile
and recovery phases.
Following a period of repetitive, high-intensity activity, the m uscles and muscle bres are characterized by
extrem e m etabolic perturbations. T hese m uscles display reductions in AT P which m ay approach 40%
(M cCartney et al., 1986; H ultm an et al., 1991; Gaitanos et al., 1993) and near com plete reductions in phosphocreatine. The metabolic by-products generated
from the high-energy phosphate reactions result in
large increases in inorganic phosphate, creatine, free
AD P and free AM P. Activation of AMP deam inase also
occurs, leading to increases in inosine m onophosphate
and am m onia (NH +4 ). These changes are accom panied
by large increases in lactic acid generated by the
increase in glycolytic ux. The increase in lactic acid in
com bination with the hydrogen ions generated by ATP
Green
hydrolysis, produces a profound m uscle acidosis which
m ay decrease pH to below 6.4 (G reen, 1995b).
According to current thinking, it is not the reduction
in AT P that is the prim ary cause of force failure in
itself, since the concentration of AT P rem ains well in
excess of that needed to saturate the AT Pase enzym es
(Korge, 1995). Rather, it is the accumulation of selected m etabolic by-products that precipitates the fatigue
process. Accum ulation of AD P, inorganic phosphate
and H 2 + , for exam ple, serves not only to reduce the
free energy liberated by ATPase hydrolysis, but also to
cause a profound dow n-regulation in ATPase activity
(Korge, 1995). This dow n-regulation has been dem onstrated not only for the sarcoplasm ic reticulum Ca 2 +
AT Pase, but for C a 2 + release channel function, using
an arti cial m icroenvironm ent with speci c m anipulation of selected m etabolites either alone or in combination (Zhu and N osek, 1991). Skinned bre
preparations have also been used to demonstrate the
effect of changes in speci c m etabolites on myosin
AT Pase activity and actomyosin function (C ooke and
Pate, 1990). Interestingly, the effect of changes in speci c m etabolites is, to som e degree, speci c to the
velocity of contraction. Skinned bre studies have also
been com plem ented by in vitro studies in w hich the
behaviour of either the sarcoplasm ic reticulum Ca 2 +
AT Pase (W illiam s and Klug, 1995) or the myo brillar
AT Pase (Parkhouse, 1992) is exam ined at different
background concentrations of m etabolites, typical of
those found in heavy exercise. T he results are generally
consistent and show a dom inant effect of selected
m etabolites such as inorganic phosphate, AD P and H +
on the regulation of AT Pase activity and the liberation
of energy.
T he down-regulation of AT Pase is viewed as protective, allowing relatively tight regulation of ATP levels
(Korge, 1995). By reducing ATP utilization, a better
balance can be achieved with the AT P synthesizing
pathways. T he penalty, however, for the dow n-regulation is fatigue, prom oted by a loss in the ability to use
AT P at high rates. At present, it is not possible to im plicate a speci c excitation or contraction process as the
de nitive weak link, since all processes appear to be
disturbed by the adverse m icroenvironm ent created by
intense exercise. It is possible that metabolite levels
m ay be different in the different com partments separating the m ajor ATPase enzym es. Since AT P synthesis is
believed to be locally regulated (Korge, 1995), an
im balance between ATP utilization and AT P synthetic
rates m ay be m ore pronounced in one com partment
than another.
T he high glycolytic rate induced by intense activity
also results in the predom inant utilization of carbohydrate and, in particular, the glycogen reserves in the
working m uscle. Even short periods of repetitive activ-
253
invoked by repeated, high force generation would
appear to be one area where dram atic im provem ent is
possible. Follow ing a schedule of acute concentric or
eccentric contractions, the repair and rem odelling of
the dam age m ay take several days and, depending on
the severity, up to 2 weeks (Newham et al., 1983;
Frid e n and Leiber, 1992). After the repair period, the
m uscle appears to be able to tolerate the same exercise
task not only with less dam age but also w ith a faster
recovery and consequently less weakness and soreness
(Byrnes et al., 1985; C larkson and Trem blay, 1988).
M oreover, it appears that the protective effect m ay
extend for at least a period of a week (Clarkson and
Trem blay, 1988). Consequently, a planned preparatory
program m e should include periodic and system atic
exposure to activities demanding the generation of
large forces to stim ulate adaptations in the cytoskeletal
fram ework. For this type of adaptation to be signi cantly transferable to a speci c task, care m ust be taken
to incorporate high force activities that fully exploit the
m uscles and m otor units, the range of motion and the
contraction velocity typical of the task. An inviting but
unproved possibility is that eccentric activity, given the
sm all insult needed to induce damage and adaptation
(Frid e n and Leiber, 1992), m ay have a valuable role to
play. If this is the case, it m ay not be necessary to concentrate exclusively on intense and sustained training
activities, w ith the accom panying and diverse physiological strain that results, to prom ote increased resistance to m uscle dam age.
Adaptations in energy m etabolic potential are
undoubtedly crucial to im proving fatigue resistance.
Since high-intensity activity results in an im balance
between ATP regeneration and ATP utilization,
resulting in a reduction in AT P of as m uch as 40%
(M cCartney et al., 1986; Gaitanos et al., 1993), m ajor
bene ts would result from increasing AT P synthetic
rates. M oreover, since the greatest imbalance occurs
during the rest to work transitions, im provem ents in
the ability to increase ux rates of the AT P supplying
pathways rapidly, particularly where repetitive,
dynam ic activity is involved, would be particularly signi cant. Although high-energy phosphate transfer
potential appears relatively insensitive to further adaptation, the metabolic pathways and segm ents involved
in glycogenolysis, glycolysis and oxidative phosphorylation can change m arkedly if appropriately stim ulated
(Holloszy and Coyle, 1984; C adefau et al., 1990).
High-intensity activity appears to represent a potent
stim ulus for eliciting increases in the m axim al activities
of a wide range of enzymes involved in these pathways
and segm ents (Dudley et al., 1982; Cadefau et al.,
1990). In the case of glycolysis, greater ux would be
expected at a given effector concentration or, alternatively, a given ux could be sustained at a lower effector
254
concentration (C onnett et al., 1990; Spriet, 1995).
Increases in buffer capacity should also prom ote an
im proved work perform ance given the need to m inim ize the drastic changes in H + concentration which
occurs w ith repeated stim ulation of glycolysis (Sharp et
al., 1986). Im provements in oxidative phosphor ylation
could effectively lower the dependency on high-energy
phosphate transfer and glycolysis at a given AT P
requirem ent and, consequently, reduce m etabolic byproduct accum ulation and glycogen dependency (Connett et al., 1990).
VO
2 during the non-steady-state (Hagberg et al., 1980;
Phillips et al., 1995) as well as providing for a faster rate
of phosphocreatine synthesis during the rest and recovery intervals. Since phosphocreatine re-synthesis is an
aerobic-dependent process (H arris et al., 1976), ensuring that tissue oxygen tension rem ains high during the
recovery period could prom ote a faster norm alization
of the by-products of high-energy phosphate reactions
and quicker restoration of energy potential. In the long
term , im provem ents in O 2 availability would appear to
depend on increases in capillar y density (Hudlicka et
al., 1992). O xygen kinetics m ay also be im proved inde
pendent of changes in VO
2 m ax of m itochondrial
potential. Recent evidence indicates that alterations in
blood ow may provide an early adaptation to shortterm training, leading to an increase in ATP supplied
by mitochondrial respiration and a lowering of byproduct accum ulation (G reen, 1996).
Im portant adaptations are not only lim ited to the
ATP synthesizing m achinery. T he AT Pase enzym es
involved in ATP hydrolysis m ay also be altered. T he
sarcolemm a N a + -K + ATPase, for exam ple, has been
shown to be quickly up-regulated with sprint activity
(M cK enna et al., 1993) and there is evidence that these
adaptations result in an improvem ent in N a + and K +
hom eostasis (M cKenna, 1995). If an im proved ability
to re-establish N a + and K + gradients occurs, the sarcolem m a should allow for a m ore rapid re-establishm ent
of the resting m embrane potential and an improved
ability to conduct action potentials at a high frequency
(C lausen and N ielsen, 1994).
W hether adaptations elicited by high-intensity activity include increased activity of the other m ajor ATPases, the sarcoplasm ic reticulum ATPase and the
actomyosin AT Pase rem ain unclear. It is well know n
that extensive m odi cations can be elicited by extrem e
non-p hysiological patterns of contractile activity (Pette
and D usterh oft, 1992), but w hether an up-regulation
in the m axim al activity of these pum ps can be induced
by voluntary training to m eet the requirem ents of
intense, dynam ic activity remains to be determ ined. At
least for the myosin AT Pase (actomyosin), pronounced
Green
changes would not be exp ected, given the ability of
sprint training to induce only m inor changes in bre
types (Sim oneau et al., 1985).
Particularly noteworthy are the increases that result
to the areas of all bre types and subtypes with
dynam ic training in general and high-resistance training in particular (Howald, 1982). The increase in crosssectional area should have the effect of delaying fatigue
by allowing a sm aller num ber of m otor units to be initially recruited at a given force level, or by allowing a
subm axim al activation of the bres where recruitm ent
of the motor neuron pool rem ains xed. It would
appear, however, that for increases in bre size to be a
m eaningful adaptation in sustained, high-intensity
effort, capillary density should also be increased. M oreover, training routines should also address the velocity
requirem ents of the task, so that neural recruitm ent
patterns and m uscular contractile properties are developed in a m anner consistent with what is desired.
O verview
In sum mar y, pronounced im provem ents in exercise
perform ance are attainable with regular and system ic
training routines. Extensive adaptations are possible at
a variety of levels of organization. T he real challenge is
to devise appropriate strategies so that adaptations can
result in desired outcom es. For the participant, exp eriencing the joy of effort, at least in part, rem ains a
possibility.
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