Skrevet av Emne: TestostroGrow 2 HP - testo-booster - noen som har prøvd det ?  (Lest 17487 ganger)

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En kompis av meg prøvde dette og var veldig fornøyd. Han merket tydelig fremgang i styrke !

Noen erfaringer ??

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jepp, det funker som rakkeren for meg. holder på med min andre omgang. øker både i størrelse og styrke.
men det skal sies at jeg tar kreatin ved side av.
absolutt verdt å prøve

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Så å si alle naturlige testo boostere er bare tull. Det finnes ikke noe god dokumentasjon på noen stoffer som øker testosteron nivåene. Det er greit at zink har vist seg å øke nivåene av testosteron hos folk som hadde lave sink nivåer, men ved optimale zink nivåer vil ikke det å ta zink gi økt testorstrone verdier. Også stoffer som Tribulus Terrestis, osv har ikke noen dokumentert virkning. Det skal visstnok finnes en bulgarsk studie på bulgarsk, men den er så å si umulig å finne.

Det beste du kan gjøre for testosteron verdiene, dine er å spise eggeplommer.  Smiley
Passion trumps fucking everything!

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Kompisen min tar bare proteinpulver ved siden av og merket tydlig at det funket. Kommer nok til å teste en boks, den koster ca 350 nok, og det er ikke noe man blir blakk av..hehe

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  • no retreat - no surrender!
Nok et eksempel på hvor mye bransjen tjener på placebo-effekten.. "TestostroGrow" høres jo unektelig kjempebra ut..
Si at dette tilskuddet virkelig funker på testo- nivåene, hvilken forskjell (etisk) vil dere da si at det er mellom dette og å innta testosteron/AAS..??
Bortsett fra lovligheten, ser jeg iallefall ingen forskjell i det å innta midler som booster din egenproduksjon eller å innta testosteron direkte..
If my mind can conceive it; and my heart can believe it - then I can achieve it.
- Muhammad Ali

Utlogget Geir M

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Hvis du først skal bruke penger på kosttilskudd så kjøp noe som har beviselige effekter.

Det jeg kan annbefale de som vil ha noe utover proteinpulver/karbopulver/gainer er BCAA. Ifølge en rekke forfattere på T-nation (f.eks. styrkeguru Charles Poliquin) så skal dette visstnok være særdeles effektivt å ta mens man trener siden det tar veldig kort tid for BCAA å bli absorbert i kroppen.
There are two novels that can change a bookish fourteen-year old's life: The Lord of the Rings and Atlas Shrugged. One is a childish fantasy that often engenders a lifelong obsession with its unbelievable heroes, leading to an emotionally stunted, socially crippled adulthood, unable to deal with the real world. The other, of course, involves orcs.

- Paul Krugman, Nobelprisvinner i økonomi

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Hmmm....BCAA har jeg ikke hørt om ?

Hva er det, og hvor får du kjøpt det ?


Testo-boostern selges på helsekosten i Sverige !
Det er jo en viss forskjell mellom å ta dette produktet, framfor å stikke ei sprøyte med "gosaker" i 2ern ...hehe :O)

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Det er aminosyrer i peptidform. Ikke noe hokus pokus.
There are two novels that can change a bookish fourteen-year old's life: The Lord of the Rings and Atlas Shrugged. One is a childish fantasy that often engenders a lifelong obsession with its unbelievable heroes, leading to an emotionally stunted, socially crippled adulthood, unable to deal with the real world. The other, of course, involves orcs.

- Paul Krugman, Nobelprisvinner i økonomi

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Hvordan funker det da ?

Styrke/pump....sov...

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Tror hyper testogainer 3000 max total muscle gain funker bedre. Har hatt strålende framgang med den.

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Hvordan funker det da ?

Styrke/pump....sov...
Ikke noe ekstra pump, og økningen i styrke er ikke umiddelbar. Aminosyrer er det stoffet som proteiner er bygget opp av. Grunnen til at det er bedre å ta aminosyrer mens man trener i forhold til vanlige proteiner er det faktum at det tas opp mye raskere. Man øker i volum og styrke fordi muskelen blir bedre restituert og blir hurtigere bygget opp igjen.  Noen vil også merke at man klarer å holde seg bedre gjennom treninga hvis man tar aminosyrer under selve økten. Altså hvis man vanligvis taper seg f.eks. 5 reps på siste settet fordi man er sliten så kanskje man bare taper 3 hvis man har tatt nok aminosyrer under trening.

Det skal imidlertid sies at det kan bli smådyrt siden man trenger relativt store doseringer (20g minst ifølge Charles Poliquin) men dyrt blir det fort med Super Xxtreme Pump-matrix Testo elite 5000 også.
There are two novels that can change a bookish fourteen-year old's life: The Lord of the Rings and Atlas Shrugged. One is a childish fantasy that often engenders a lifelong obsession with its unbelievable heroes, leading to an emotionally stunted, socially crippled adulthood, unable to deal with the real world. The other, of course, involves orcs.

- Paul Krugman, Nobelprisvinner i økonomi

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Ikke noe ekstra pump, og økningen i styrke er ikke umiddelbar. Aminosyrer er det stoffet som proteiner er bygget opp av. Grunnen til at det er bedre å ta aminosyrer mens man trener i forhold til vanlige proteiner er det faktum at det tas opp mye raskere. Man øker i volum og styrke fordi muskelen blir bedre restituert og blir hurtigere bygget opp igjen.  Noen vil også merke at man klarer å holde seg bedre gjennom treninga hvis man tar aminosyrer under selve økten. Altså hvis man vanligvis taper seg f.eks. 5 reps på siste settet fordi man er sliten så kanskje man bare taper 3 hvis man har tatt nok aminosyrer under trening.


Hehe har du heftige kilder på dette eller var det det han som solgte til deg sa?

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Tror hyper testogainer 3000 max total muscle gain funker bedre. Har hatt strålende framgang med den.

Hva er et samensatt av og hvor får man kjøpt det ?

Fin treningslogg du har, forresten :=)

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Hehe har du heftige kilder på dette eller var det det han som solgte til deg sa?
Kilde 1

http://www.t-nation.com/readArticle.do?id=1365045


Sitat
Today tip comes from David Barr:

Slam the BCAA's

Pound back the BCAA's. Unlike antioxidants, and most supplements for that matter, it seems that "more is better" when it comes to BCAA's. There are sure to be diminishing returns, in that 100g won't be twice as effective as half the dose, but if you're using quantities like that, then you have too much money anyway. About 0.2g/kilo bodyweight is a good place to start, and work up from there.

Kilde 2
http://www.t-nation.com/readArticle.do?id=459568

Sitat
I'd say that your best bet is to use branched-chain aminos while you train. I learned this trick from Dr. Serrano and Dr. DiPasquale and have been using it with athletes who have difficulty gaining size. What we've found is that there's a serious decrement in post-workout soreness when you use BCAA during the training session. I recommend taking 0.44 g per kg of bodyweight. In other words, if you weigh 90 kilograms (198 pounds), take 40 grams of branched-chain amino acids. If you're on a restricted budget, use at least 20 grams. If you can't afford that much, don't bother. Of course, you could save your BCAA loading for those days when you train your weakest body parts, and that'll allow you to save some money.

How does it work? Well, BCAAs consumed during training raise both growth hormone and insulin at the same time, hence the increased anti-catabolism and anabolism. Of course, the study by Carli et al. (1992) showed that supplementing with branched-chain amino acids prior to a workout not only prevents a decrease in post-workout testosterone levels, but actually allows testosterone levels to increase following exercise.

There are two ways to ingest them: tablets/capsules or powder. If you prefer to use tablets or capsules, I recommend that you use Muscle Mass from Beverley International. Swallow three to four capsules every time you sip water. If you'd rather take the powdered form, you can use Gluta Cene from Advanced Genetics. It contains both branched-chain amino acids and glutamine that's meant to be mixed in water and sipped throughout a workout. Since BCAAs are very disgusting in taste, the company has managed to mask the flavor quite adequately. My athletes agree that grape is the most palatable of all of the flavors. To contact Advanced Genetics, call 888-629-6277.
There are two novels that can change a bookish fourteen-year old's life: The Lord of the Rings and Atlas Shrugged. One is a childish fantasy that often engenders a lifelong obsession with its unbelievable heroes, leading to an emotionally stunted, socially crippled adulthood, unable to deal with the real world. The other, of course, involves orcs.

- Paul Krugman, Nobelprisvinner i økonomi

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Jess!

Det er endel studier som viser mulige effekter av BCAA. Tok fram noen studier jeg kom over ved et kjapt søk.
Merk deg i det minste det med fet skrift. Beklager avsnittsoppbygningen på mye av det der. Var ikke så lett å copy paste alt..

Bedret restitusjon ?

4th Amino Acid Assessment Workshop


Interrelationship between Physical Activity and Branched-Chain
Amino Acids1

Michael Gleeson2

School of Sport and Exercise Sciences, Loughborough University, Loughborough, Leicestershire, LE11 3TU,
England, UK

ABSTRACT Some athletes can have quite high intakes of branched-chain amino acids (BCAAs) because of their
high energy and protein intakes and also because they consume protein supplements, solutions of protein
hydrolysates, and free amino acids. The requirement for protein may actually be higher in endurance athletes than
in sedentary individuals because some amino acids, including the BCAAs, are oxidized in increased amounts
during exercise compared with rest, and they must therefore be replenished by the diet. In the late 1970s, BCAAs
were suggested to be the third fuel for skeletal muscle after carbohydrate and fat. However, the majority of later
studies, using various exercise and treatment designs and several forms of administration of BCAAs (infusion, oral,
and with and without carbohydrates), have failed to find a performance-enhancing effect. No valid scientific
evidence supports the commercial claims that orally ingested BCAAs have an anticatabolic effect during and after
exercise in humans or that BCAA supplements may accelerate the repair of muscle damage after exercise. The
recommended protein intakes for athletes (1.2 to 1.8 g . kg body mass–1 . d–1) do not seem to be harmful. Acute
intakes of BCAA supplements of about 10–30 g/d seem to be without ill effect. However, the suggested reasons
for taking such supplements have not received much support from well-controlled scientific studies. J. Nutr. 135:

1591S–1595S, 2005.


KEY WORDS: . exercise . branched-chain amino acids . supplements


Amino acids and endurance exercise.
Hargreaves MH, Snow R
.
School of Health Sciences, Deakin University, Burwood, 3125, Australia.

Although skeletal muscle is capable of oxidizing selected amino acids, exercise in the fed and carbohydrate-replete condition results in only a small increase in amino acid utilization. Nevertheless, it may be important to increase the dietary protein requirements of active individuals. There is ongoing debate as to whether the amino acids for oxidation are derived from the free amino acid pool, from net protein breakdown, or a combination of both. There has been interest in the potential ergogenic benefits of amino acid ingestion; however, BCAA ingestion does not appear to affect fatigue during prolonged exercise, there is little support from controlled studies to recommend glutamine ingestion for enhanced immune function, and although glutamine stimulates muscle glycogen synthesis, its addition to carbohydrate supplements provides no additional benefit over ingestion of carbohydrate alone.



Dette er en rewiev artikkel som tar for seg endel studier:

3rd Amino Acid Workshop


Exercise Promotes BCAA Catabolism: Effects of BCAA
Supplementation on Skeletal Muscle during Exercise1

Yoshiharu Shimomura,*2 Taro Murakami,* Naoya Nakai,y Masaru Nagasaki,* and
Robert A. Harris**

*Department of Materials Science and Engineering, Nagoya Institute of Technology, Nagoya 466-8555,
Japan; yDepartment of Biochemistry, Mie University School of Medicine, Tsu, Mie 514-8507, Japan;
and **Department of Biochemistry and Molecular Biology, Indiana University School
of Medicine, Indianapolis, IN 46202-5122, USA


ABSTRACT Branched-chain amino acids (BCAAs) are essential amino acids that can be oxidized in skeletal muscle.
It is known that BCAA oxidation is promoted by exercise. The mechanism responsible for this phenomenon is attributed
to activation of the branched-chain a-keto acid dehydrogenase (BCKDH) complex, which catalyzes the second-step
reaction of the BCAA catabolic pathway and is the rate-limiting enzyme in the pathway. This enzyme complex is
regulated by a phosphorylation-dephosphorylation cycle. The BCKDH kinase is responsible for inactivation of the
complex by phosphorylation, and the activity of the kinase is inversely correlated with the activity state of the BCKDH
complex, which suggests that the kinase is the primary regulator of the complex. We found recently that administration of
ligands for peroxisome proliferator-activated receptor-a (PPARa) in rats caused activation of the hepatic BCKDH
complex in association with a decrease in the kinase activity, which suggests that promotion of fatty acid oxidation
upregulates the BCAA catabolism. Long-chain fatty acids are ligands for PPARa, and the fatty acid oxidation is
promoted by several physiological conditions including exercise. These findings suggest that fatty acids may be one of
the regulators of BCAA catabolism and that the BCAA requirement is increased by exercise. Furthermore, BCAA
supplementation before and after exercise has beneficial effects for decreasing exercise-induced muscle damage and
promoting muscle-protein synthesis; this suggests the possibility that BCAAs are a useful supplement in relation to
exercise and sports. J. Nutr. 134: 1583S–1587S, 2004.


KEY WORDS: . exercise . branched-chain amino acids . branched-chain a-keto acid dehydrogenase
complex . peroxisome proliferator-activated receptor-a . rat

The branched-chain amino acids (BCAAs)3 leucine, iso-BCAAs is critically important for maintaining normal body
leucine, and valine are among the nine essential amino acids for conditions.
humans and account for ;35% of the essential amino acids in It is known that BCAAs can be oxidized in skeletal muscle,
muscle proteins and ;40% of the preformed amino acids whereas other essential amino acids are catabolized mainly in
required by mammals (1). Because animal and human cells liver (3). Exercise greatly increases energy expenditure and
have a tightly controlled enzymatic system for BCAA promotes oxidation of BCAAs (3). It is believed that BCAAs
degradation, BCAAs that are ingested in excess are quickly contribute to energy metabolism during exercise as energy
disposed of (2). Although BCAAs are absolutely required for sources and substrates to expand the pool of citric acid–cycle
protein synthesis, some intermediates formed in their catabo-intermediates (anaplerosis) and for gluconeogenesis. In conlism [e.g., branched-chain a-keto acids (BCKA)] can be toxic trast, leucine is special among the BCAAs, because it promotes
at high concentrations (1). Therefore, the disposal of excess muscle-protein synthesis in vivo when orally administered to

animals (4). As a consequence of these findings, BCAAs are
receiving considerable attention as potentially helpful dietary

1

Presented at the conference ‘‘The Third Workshop on the Assessment of

supplements for individuals who enjoy exercise and participate

Adequate Intake of Dietary Amino Acids’’ held October 23–24, 2003 in Nice,
France. The conference was sponsored by the International Council on Amino in sports. We describe here what is known about the
Acid Science. The Workshop Organizing Committee included Vernon R. Young, mechanism responsible for the promotion of BCAA oxidation
Yuzo Hayashi, Luc Cynober, and Motoni Kadowaki. Conference proceedings were

by exercise and summarize the effects of BCAA supplementa

published as a supplement to The Journal of Nutrition. Guest editors for the
supplement publication were Vernon R. Young, Dennis M. Bier, Luc Cynober,

tion (as a dietary supplement) in relation to exercise.

Yuzo Hayashi, and Motoni Kadowaki.

2

To whom correspondence should be addressed. E-mail: shimomura.
yoshiharu@nitech.ac.jp.

3

Regulation of BCAA catabolism

Abbreviations used: BCAA, branched-chain amino acid; BCKA, branched-
chain a-keto acid; BCKDH, branched-chain a-keto acid dehydrogenase; CoA,

Enzymes regulating the BCAA catabolism. The entire

coenzyme A; HIByl-CoA, b-hydroxyisobutyryl-coenzyme A; KIC, a-ketoisocaproate; PPARa, peroxisome proliferator-activated receptor-a. catabolic pathway for BCAAs is located in mitochondria. The

0022-3166/04 $8.00 . 2004 American Society for Nutritional Sciences.

1583S

Downloaded from jn.nutrition.org by on August 3, 2007


1584S SUPPLEMENT

first two steps are common to all three BCAAs and have
characteristic features of catabolism. The first reaction in the
pathway is the reversible transamination of BCAA to produce
BCKA, which is catalyzed by branched-chain aminotransferase.
The second reaction is the irreversible oxidative decarboxylation of BCKA to form coenzyme A (CoA) compounds, which
is catalyzed by the branched-chain a-keto acid dehydrogenase
(BCKDH) complex (Fig. 1). The latter reaction is the rate-
limiting step of BCAA catabolism and is therefore understandably subject to tight regulation (2,5).

The catabolic pathway of BCAAs has been most intensively
studied in rats. Many studies have focused on regulation of the
activity state of the BCKDH complex in rat liver. The BCKDH
complex is regulated by a phosphorylation-dephosphorylation
cycle. BCKDH kinase is responsible for inactivation of the
complex by phosphorylation of the E1 component of the
complex (6,7), and BCKDH phosphatase is responsible for
reactivation of the complex by dephosphorylation (8). Much
evidence suggests that the BCKDH kinase primarily regulates
the activity state of the complex (7). The BCKDH phosphatase
may also be important, but very limited information about the
phosphatase is available, although purification of the phosphatase from bovine kidney has been reported (8).

Regulation of the activity state of BCKDH complex by
a-ketoisocaproate derived from leucine. Many reports show
that the activity of BCKDH kinase is inversely correlated with
the activity state of the BCKDH complex in vivo, which
suggests that the kinase may regulate BCAA catabolism (7). It
was demonstrated (9) that a-ketoisocaproate (KIC; formed by
transamination of leucine) is a potent inhibitor of the kinase.
a-Keto-b-methylvalerate and a-ketoisovalerate, which are
derived from isoleucine and valine, respectively, have an effect
similar to that of KIC but with greatly reduced potency (9).
Therefore, when KIC has accumulated in tissues under some
physiological conditions, BCAA catabolism is promoted by
activation of the BCKDH complex.

It was reported that feeding rats a leucine-rich diet decreases
plasma concentrations of isoleucine and valine (10) and
activates the hepatic BCKDH complex (11). This indicates

that administration of leucine alone induces BCAA imbalance
presumably because of inhibition of BCKDH kinase by KIC.

Effect of exercise on BCAA catabolism and
its regulation

Activation of BCKDH complex by exercise. Endurance
exercise increases energy expenditure and promotes protein
and amino acid catabolism (3). BCAAs can be oxidized in
skeletal muscles, and their oxidation is enhanced by exercise
(3). It was reported that endurance exercise activates the
BCKDH complex in human and rat skeletal muscles (12,13)
and rat liver (14). We showed that BCKDH kinase activity in
rat liver is decreased significantly by 85 min of running exercise
(14), which may be a main factor contributing to activation of
the hepatic BCKDH complex. Although the detailed mechanism is not known, it is unlikely that altered gene expression of
the kinase can be responsible for the decrease in kinase activity
caused by such a short period of exercise. In our study using an
electrically stimulated muscle-contraction model, increases in
leucine and KIC concentrations in the muscle are suggested to
be one of the factors responsible for the muscle BCKDH
activation (15). We also demonstrated that the amount of the
kinase bound to the complex is reduced by exercise (16).

In addition to the acute effects of exercise as described, it
was reported that exercise training (repeated exercise bouts)
decreases the kinase protein in rat skeletal muscle and thereby
results in greater activation of the BCKDH complex in skeletal
muscle of trained rats by acute exercise (17).

It is well known that feeding a low-protein diet (or protein
starvation) inactivates the BCKDH complex by phosphorylation of the enzyme in rat liver (1,2). The activity of BCKDH
kinase and the amount of the kinase bound to the complex are
inversely correlated with the activity state of the complex (18).
Inactivation of the BCKDH complex provides a mechanism for
conservation of BCAAs for protein synthesis under BCAA-
deficient conditions. When the rats fed the low-protein diet
performed running exercise, hepatic BCKDH complexes were
significantly increased (14), which suggests that BCAA

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FIGURE 1 The BCAA catabolic pathway, which occurs within mitochondria, includes two primary reactions: the reversible
transamination of BCAAs and the irreversible
decarboxylation of BCKA to form CoA compounds. The latter reaction is the rate-limiting
step of BCKA catabolism. TCA, tricarboxylic
acid cycle; KIV, a-ketoisovalerate; KMV, a-
keto-b-methylvalerate; CoA-SH, reduced
form of CoA; IB-CoA, isobutyryl-CoA; MB-
CoA, a-methylbutyryl-CoA; IV-CoA, isovaleryl-CoA; R-CoA, acyl-CoA.


BRANCHED-CHAIN AMINO ACIDS AND EXERCISE 1585S

catabolism is promoted by exercise even in rats that are
deficient in BCAA.

Effects of stimulation of the fatty acid oxidation on the
BCKDH complex activity. A number of physiological conditions including exercise stimulate fatty acid oxidation as well as
BCAA oxidation (1,14). It is interesting to consider the
relationship between the two catabolic systems. Clofibric acid
is well known as a hyperlipidemic drug that stimulates fatty acid
oxidation. It was reported that this compound also stimulates
BCAA catabolism and causes muscle wasting upon long-term
treatment of animals with the drug (19,20). Studies examining
the long-term effects of clofibric acid on BCKDH kinase expression in rat liver revealed decreases in kinase activity, protein,
and message in response to the treatment (21). It is believed that
clofibric acid exerts many of the long-term effects by activation
of peroxisome proliferator-activated receptor-a (PPARa).
Starvation also stimulates fatty acid oxidation. Because
starvation increases free fatty acid levels in the circulation and
fatty acids are naturally occurring ligands for PPARa, the
increase in free fatty acid levels caused by starvation may
downregulate kinase expression in rat liver (22). Because fatty
acid oxidation is also promoted by exercise, the hypothesis of
activation of the BCKDH complex in association with increased
fatty acid oxidation might be applicable to the mechanisms for
promotion of BCAA oxidation by exercise training.

Effect of BCAA supplementation on muscle
performance in sport and exercise

Effects of BCAA supplementation on muscle protein
metabolism in relation to exercise. The effects of BCAA
supplementation before and after exercise on muscle-protein
metabolism and exercise-induced muscle damage were examined in humans. It was reported (23) that an oral supplement of
BCAAs (77 mg/kg body wt) before exercise increased intracellular and arterial BCAA levels during exercise and
resulted in suppression of endogenous muscle-protein breakdown. It was also reported that oral BCAA administration

(12 g/d for 2 wk and an additional 20 g each before and after
the exercise test) suppressed the rise in serum creatine kinase
activity for several days after exercise (24). Similar effects were
also observed in a study in which subjects ingested an amino
acid mixture (that contained 3.6 g of amino acids with 37%
BCAAs) before and after the exercise test and 2 doses/d of the
amino acid mixture for 4 d after the exercise test (25). The
amino acid supplement also diminished muscle soreness that
usually follows exercise. Although the mechanism responsible
for the protective effects of BCAA supplementation against
exercise-induced muscle damage and soreness have not been
elucidated, it is presumed that stimulation of protein synthesis
by leucine and suppression of exercise-induced protein
breakdown by BCAAs may be involved. Furthermore, the
most effective ratio of the three BCAAs for the beneficial
effects is not known. Clearly these interesting observations
should be followed up with studies designed to elucidate the
mechanisms responsible for the phenomena and to clarify the
most effective composition of BCAAs.

Specific features of valine catabolism. Valine catabolism is
unique compared with the other BCAAs. The potentially toxic
compound methacrylyl-CoA is formed in the middle of the
valine catabolic pathway (Fig. 2). It was suggested that
methacrylyl-CoA is a particularly reactive compound with
considerable potential for cytogenic and mutagenic actions,
because it is a thiol-reactive molecule through nonenzymatic
Michael addition reactions (26). Crotonase and b-hydroxyisobutyryl-CoA (HIByl-CoA) hydrolase activities are critically
important for rapid disposal of methacrylyl-CoA in cells. Furthermore, methacrylyl-CoA is generated during valine catabolism in the mitochondrial matrix space, where it can react with
glutathione and thereby potentially interfere with the mechanism that protects mitochondria against damage by reactive
oxygen species. Although methacrylyl-CoA has not been
established to cause damage during exercise, stimulation of
BCAA catabolism during exercise results in production of
additional methacrylyl-CoA that must be rapidly destroyed by
the combined actions of crotonase and HIByl-CoA hydrolase to
prevent irreversible mitochondrial damage.

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FIGURE 2 The valine catabolic pathway is unique when compared with other
BCAAs in that the potentially toxic methacrylyl-CoA is formed in the middle of the
pathway. Stimulation of BCAA catabolism
during exercise results in production of
additional methacrylyl-CoA that is rapidly
destroyed by the combined actions of crotonase and HIByl-CoA hydrolase. BCAT,
branched-chain aminotransferase; HIBA,
b-hydroxyisobutyric acid; and MMS, methyl-
malonic acid semialdehyde.


1586S SUPPLEMENT

We purified the HIByl-CoA hydrolase from rat livers and
established a method for measurement of this enzyme activity
in a coupled reaction with crotonase (26,27). The activities of
both crotonase and HIByl-CoA hydrolase are extremely high
compared to the activity of the BCKDH complex in the
mammalian tissues examined [skeletal muscle of rat (26), dog
(27), and human (28)]. Therefore, methacrylyl-CoA is rapidly
degraded to the free acid and reduced form of CoA by the high
activities of two enzymes. As a consequence, methacrylyl-CoA
and HIByl-CoA are not detectable in liver cells even when
incubated under conditions that should maximize the concentrations of valine pathway intermediates (29). These
findings suggest that a supplement of valine as the BCAA
mixture for sports should not be toxic for humans under normal
conditions although exercise promotes valine catabolism.

Toxicity of BCAA. Acute and subacute toxicity studies of
BCAAs using mice and rats (30) and a chronic toxicity study
using rats (31) were reported. The BCAA composition used in
these studies was a 2.1:1:1.2 leucine:isoleucine:valine ratio. No
animals died from the single dose of 10 g of BCAA/kg body wt
in the acute toxicity study, and the half-maximal lethal
dose was estimated as .10 g/kg body wt. No toxic effects of
BCAAs were observed at a dose of 2.5 gkg21d21 for 3 mo or

d21 

1.25 gkg21 for 1 y. There are no reports concerning
BCAA toxicity in relation to exercise and sports.
Concluding remarks

It is clear that exercise promotes degradation of BCAAs.
Promotion of fatty acid oxidation appears to be associated with
greater rates of BCAA oxidation, which suggests that fatty
acids may be regulators of BCAA oxidation. Furthermore,
muscle-protein synthesis is enhanced after exercise. From these
findings, it may be concluded that the BCAA requirement is
increased by exercise. BCAA supplementation before and after
exercise has beneficial effects for decreasing exercise-induced
muscle damage and promoting muscle-protein synthesis; this
suggests that BCAAs may be a useful supplement in relation to
exercise and sports. Although in many human exercise studies,
a dose of .5 g of BCAA was used as a supplement, the
minimum dose to produce the beneficial effects of BCAA
supplementation remains to be established. Furthermore, the
most effective ratio of the three BCAAs is unclear. Toxicity
studies of BCAAs using animals showed that BCAAs are
quite safe amino acids when the three BCAAs are provided
in a ratio similar to that of animal protein (e.g., a 2:1:1
leucine:isoleucine:valine ratio). Although leucine is the most
potent amino acid among the BCAAs for stimulating protein
synthesis, supplementation of leucine alone may cause BCAA
imbalance via the activating effect of its keto acid on the
BCKDH complex. A number of research groups examined
whether BCAA supplementation might have a beneficial effect
on endurance performance (32–36), but the results are
inconsistent. Additional studies are required to clarify the
appropriate amount of BCAA supplementation for beneficial
effects and the responsible mechanisms.

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