Are BCAA's better than Whey Protein--Bobo and thegame?

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    Are BCAA's better than Whey Protein--Bobo and thegame?


    I have a question for Bobo and the game that I need clarified. With the popularity of BCAA's, I conducted a home experiement.

    20 grams of Whey concentrate 10 minutes pre workout or 10 grams of BCAA's. I am convinced that pre workout Protein or BCAA's increases exercise endurance.

    I failed to "Feel" the difference between 20 grams of whey concentrate or 10 grams of BCAAs.

    General feedback is wanted!

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    Oh man...what a loaded question.

    Did you not know Nandi was against BCAA's?
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    I won't even try to make a educated statement but my personal experience has been that I get the best effect from whatever i'm lacking most in my diet. If that makes any sense whatsoever.
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    Quote Originally Posted by Bobo
    Oh man...what a loaded question.

    Did you not know Nandi was against BCAA's?
    Loaded question..nah.

    I would pay for the answer. Nandi loved to experiment and BCAAs was not on the list. He recomended whey instead, but He did like leucine.

    I had alot of BCAA's gifted so I tested both approaches.

    Do you use BCAA's?
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    Quote Originally Posted by USPLabs
    Loaded question..nah.

    I would pay for the answer. Nandi loved to experiment and BCAAs was not on the list. He recomended whey instead, but He did like leucine.

    I had alot of BCAA's gifted so I tested both approaches.

    Do you use BCAA's?
    I know you would! I still won't do it! lol

    This is what Nandi had to say when asked this:

    "So lots of peopel our builiding up ICE and rightfully so, it is a very good product. The thing is though...it seems that loading up on BCAA's would be awesome for dieting, their anti-catabloic /anabolic actions would make it great to take in between meals and keep muscle wasting at an absolute minimum. However with BCAA's increasing Insulin release, wouldn't they be counter productive to fat loss goals...just looking for others thoughts.."

    Quite possibly. Amino acid infusions produce insulin resistance:

    " A approximately 2.1-fold elevation of plasma anabolic steroids [amino acids] reduced whole-body glucose disposal by 25% (P < 0.01). Rates of muscle glycogen synthesis decreased by 64% (180--315 min, 24 plus minus 3; control, 67 plus minus 10 micromol center dot l(-1) center dot min(-1); P < 0.01), which was accompanied by a reduction in G6P starting at 130 min (DeltaG6P(260--300 min), 18 plus minus 19; control, 103 plus minus 33 micromol/l; P < 0.05). In conclusion, plasma amino acid elevation induces skeletal muscle insulin resistance in humans by inhibition of glucose transport/phosphorylation, resulting in marked reduction of glycogen synthesis. (1)

    The resulting insulin resistance would be expected to lead to hyperinsulinemia and impaired lipolysis.

    An even more interesting question ( in my mind ) is to what extent the resulting insulin resistance affects protein metabolism. If a person is insulin resistant with respect to glucose, are they also insulin resistant with respect to the anabolic effects of insulin? The answer may be yes, at least somewhat.

    Resistance to glucose uptake evidently does not affect amino acid uptake; the transport systems are different (2). So amino acid transport seems to be the same in normal and insulin resistant people, and the stimulatory effect of hyperaminoacidemia on protein synthesis is the same as well. However, what appears to be different is that in insulin resistance, the antiproteolytic effect of insulin is lost, at least in the research presented here:

    "In conclusion, insulin resistance is a common feature of both glucose and protein metabolism in obesity. The defect in protein metabolism is characterized by an impairment of the ability of insulin to inhibit proteolysis; the stimulatory effect of hyperaminoacidemia on protein synthesis is intact in obesity." (3)

    So it seems, ironically, that a high protein diet could actually lead to a catabolic state. This is especially true in light of the fact that a high protein diet induces subclinical metabolic acidosis, which raises cortisol levels."

    (1) Diabetes 2002 Mar;51(3):599-605

    Mechanism of amino acid-induced skeletal muscle insulin resistance in humans.

    Krebs M, Krssak M, Bernroider E, Anderwald C, Brehm A, Meyerspeer M, Nowotny P, Roth E, Waldhausl W, Roden


    (2) Diabetes 1993 Dec;42(12):1868-77

    Different sensitivity of glucose and amino acid metabolism to insulin in NIDDM.

    Luzi L, Petrides AS, De Fronzo RA


    (3) Am J Physiol 1996 Feb;270(2 Pt 1):E273-81

    Insulin and hyperaminoacidemia regulate by a different mechanism leucine turnover and oxidation in obesity.

    Luzi L, Castellino P, DeFronzo RA




    "Most athletes take in more protein than they need. Especially without a buffering protocol, the resulting acidosis is quite catabolic. The insulin resistance only adds insult to injury. This is especially true in AAS using athletes who are already experiencing some degree of AAS induced insulin resistance. Moreover, there is evidence that AAS users require LESS protein than non users becuase the cells become much more efficient at recycling amino acids.

    BCAA supplementation is a waste of money, IMHO, and probably detrimental as well."


    Consdering you asked this, I remember this from years ago.
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    **slightly off topic but within that statement**

    That made my brain hurt but I will echo something that I noticed by accident cause I was broke. A decrease in my whey intake and over all protein intake yielded better strength and muscle gains. I was seriously over doing the protein.
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    Quote Originally Posted by USPLabs
    He recomended whey instead, but He did like leucine.

    I had alot of BCAA's gifted so I tested both approaches.

    Do you use BCAA's?
    I did in moderation but never megadosed it (consistently). I tried it, dind't work out too well.

    Lecine is differnet because of its signialling properties.
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    I've often wondered about BCAA's hindering fatloss as well because of their effects on insulin but i see TONS of ppl still using them while dieting so i guess not.
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    Well I think in moderation they can be beneficial but considering how straight aminos are metabolized there is just so much your body can utilize at once point before it gets "flushed". Whey protein even though fast absorbing has much more of a time release then straight amino's.

    I think a lot of people that megadose don't understand the majority of it isn't getting used for what they bought it for.
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    Quote Originally Posted by Bobo
    Well I think in moderation they can be beneficial but considering how straight aminos are metabolized there is just so much your body can utilize at once point before it gets "flushed". Whey protein even though fast absorbing has much more of a time release then straight amino's.

    I think a lot of people that megadose don't understand the majority of it isn't getting used for what they bought it for.
    The endurance effect is probably from gluconeogenisis.
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    instead of taking it throughout the day, it might be beneficial to only taking it during the workout when your body can utilize it the most no?
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    Quote Originally Posted by Bobo
    Well I think in moderation they can be beneficial but considering how straight aminos are metabolized there is just so much your body can utilize at once point before it gets "flushed". Whey protein even though fast absorbing has much more of a time release then straight amino's.

    I think a lot of people that megadose don't understand the majority of it isn't getting used for what they bought it for.
    please explain something

    how do bcaas turn into glucose via glycolosis even when supplemented during exercise?

    i was under the impression that they werent converted...please explain when they are megadosed as well

    thanks!!
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    Quote Originally Posted by ECTOmorph
    please explain something

    how do bcaas turn into glucose via glycolosis even when supplemented during exercise?

    i was under the impression that they werent converted...please explain when they are megadosed as well

    thanks!!
    I didn't say BCAA specfically, I said amino's. Genernally the oxidation of BCAA's usually correlates to increased gluconeogensis (leucine will be oxidized as a fuel source to spare glucose for use elsewhere). This condition is usually only relevant when dieting. You can eliminate this simply by adding a carb.

    As for megadosing, I just don't feel the body can utilize large amounts effectively. A small amount of carbs couple wiht a small amount of BCAA's make the most sense IMO.
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    I thought aminos would have the best effect when taken on an empty stomach? so if you were to take bcaas, what is the best scenario for taking them? During the workout/post workout/in the morning or when?
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    I think if you get a decent protein additinoal AA content is a waste of $$, if you are going to add AA content there is only three I would add. Leucince, Isoluecine, and Valine, which have been shown to be key factors in hypertrophy. The rest of the AA content you need can easily be found in a good protein powder.
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    Quote Originally Posted by RunMav
    I thought aminos would have the best effect when taken on an empty stomach? so if you were to take bcaas, what is the best scenario for taking them? During the workout/post workout/in the morning or when?
    Absorption will be quicker on an empty stomahce but you still need to add carbs. Just limit the fat or slow digesting protriens.

    If you are going to take a straight BCAA mix I would go mid workout with some carbs in water.
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    Quote Originally Posted by TheGame46
    I think if you get a decent protein additinoal BCAA content is a waste of $$, if you are going to add BCAA content there is only three I would add. Leucince, Isoluecine, and Valine, which have been shown to be key factors in hypertrophy. The rest of the BCAA content you need can easily be found in a good protein powder.

    Huh? BCAA's ARE Leucine, Isoleucine and Valine.
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    Quote Originally Posted by RunMav
    I thought aminos would have the best effect when taken on an empty stomach? so if you were to take bcaas, what is the best scenario for taking them? During the workout/post workout/in the morning or when?
    Take them with a small form of carbohydrate during workout. YOu can take the pre workout just take half pre and half during. IF you have adequate carbs before workout then you can just take them with water.
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    Quote Originally Posted by Beth1971
    and then?
    and then what?
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    Quote Originally Posted by Bobo
    Huh? BCAA's ARE Leucine, Isoleucine and Valine.
    These are the only 3 amino acids I would add to my shake. Leucine is the only one I actaully do!

    Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise.

    * Blomstrand E,
    * Eliasson J,
    * Karlsson HK,
    * Kohnke R.

    Department of Surgical Science, Karolinska Institutet, Stockholm, Sweden. eva.blomstrand@gih.se

    BCAAs (leucine, isoleucine, and valine), particularly leucine, have anabolic effects on protein metabolism by increasing the rate of protein synthesis and decreasing the rate of protein degradation in resting human muscle. Also, during recovery from endurance exercise, BCAAs were found to have anabolic effects in human muscle. These effects are likely to be mediated through changes in signaling pathways controlling protein synthesis. This involves phosphorylation of the mammalian target of rapamycin (mTOR) and sequential activation of 70-kD S6 protein kinase (p70 S6 kinase) and the eukaryotic initiation factor 4E-binding protein 1. Activation of p70 S6 kinase, and subsequent phopsphorylation of the ribosomal protein S6, is associated with enhanced translation of specific mRNAs. When BCAAs were supplied to subjects during and after one session of quadriceps muscle resistance exercise, an increase in mTOR, p70 S6 kinase, and S6 phosphorylation was found in the recovery period after the exercise with no effect of BCAAs on Akt or glycogen synthase kinase 3 (GSK-3) phosphorylation. Exercise without BCAA intake led to a partial phosphorylation of p70 S6 kinase without activating the enzyme, a decrease in Akt phosphorylation, and no change in GSK-3. It has previously been shown that leucine infusion increases p70 S6 kinase phosphorylation in an Akt-independent manner in resting subjects; however, a relation between mTOR and p70 S6 kinase has not been reported previously. The results suggest that BCAAs activate mTOR and p70 S6 kinase in human muscle in the recovery period after exercise and that GSK-3 is not involved in the anabolic action of BCAAs on human muscle.

    Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise.

    * Karlsson HK,
    * Nilsson PA,
    * Nilsson J,
    * Chibalin AV,
    * Zierath JR,
    * Blomstrand E.

    Univ. College of Physical Education and Sports, Box 5626, S-114 86 Stockholm, Sweden.

    The aim of the study was to investigate the effect of resistance exercise alone or in combination with oral intake of branched-chain amino acids (BCAA) on phosphorylation of the 70-kDa S6 protein kinase (p70(S6k)) and mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK1/2), and p38 MAPK in skeletal muscle. Seven male subjects performed one session of quadriceps muscle resistance training (4 x 10 repetitions at 80% of one repetition maximum) on two occasions. In a randomized order, double-blind, crossover test, subjects ingested a solution of BCAA or placebo during and after exercise. Ingestion of BCAA increased plasma concentrations of isoleucine, leucine, and valine during exercise and throughout recovery after exercise (2 h postexercise), whereas no change was noted after the placebo trial. Resistance exercise led to a robust increase in p70(S6k) phosphorylation at Ser(424) and/or Thr(421), which persisted 1 and 2 h after exercise. BCAA ingestion further enhanced p70(S6k) phosphorylation 3.5-fold during recovery. p70(S6k) phosphorylation at Thr(389) was unaltered directly after resistance exercise. However, during recovery, Thr(389) phosphorylation was profoundly increased, but only during the BCAA trial. Furthermore, phosphorylation of the ribosomal protein S6 was also increased in the recovery period only during the BCAA trial. Exercise led to a marked increase in ERK1/2 and p38 MAPK phosphorylation, which was completely suppressed upon recovery and unaltered by BCAA. In conclusion, BCAA, ingested during and after resistance exercise, mediate signal transduction through p70(S6k) in skeletal muscle.

    Branched-chain amino acids improve glucose metabolism in rats with liver cirrhosis.

    * Ni****ani S,
    * Takehana K,
    * Fujitani S,
    * Sonaka I.

    Pharmaceutical Research Laboratories, Ajinomoto Co., Inc., Kawasaki-ku, Kawasaki-shi, Japan. shinobu_ni****ani@ajinomoto.co m

    It is well established that impaired glucose metabolism is a frequent complication in patients with hepatic cirrhosis. We previously showed that leucine, one of the branched-chain amino acids (BCAA), promotes glucose uptake under insulin-free conditions in isolated skeletal muscle from normal rats. The aim of the present study was to evaluate the effects of BCAA on glucose metabolism in a rat model of CCl(4)-induced cirrhosis (CCl(4) rats). Oral glucose tolerance tests were performed on BCAA-treated CCl(4) rats. In the CCl(4) rats, treatment with leucine or isoleucine, but not valine, improved glucose tolerance significantly, with the effect of isoleucine being greater than the effect of leucine. Glucose uptake experiments using isolated soleus muscle from the CCl(4) rats revealed that leucine and isoleucine, but not valine, promoted glucose uptake under insulin-free conditions. To clarify the mechanism of the blood glucose-lowering effects of BCAA, we collected soleus muscles from BCAA-treated CCl(4) rats with or without a glucose load. These samples were used to determine the subcellular location of glucose transporter proteins and glycogen synthase (GS) activity. Oral administration of leucine or isoleucine without a glucose load induced GLUT4 and GLUT1 translocation to the plasma membrane. GS activity was augmented only in leucine-treated rats and was completely inhibited by rapamycin, an inhibitor of mammalian target of rapamycin. In summary, we found that leucine and isoleucine improved glucose metabolism in CCl(4) rats by promoting glucose uptake in skeletal muscle. This effect occurred as a result of upregulation of GLUT4 and GLUT1 and also by mammalian target of rapamycin-dependent activation of GS in skeletal muscle. From these results, we consider that BCAA treatment may have beneficial effects on glucose metabolism in cirrhotic patients.
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    Umm...yeah thats all good and everything but there are only 3 to begin with.

    You do know there are only 3 right?




    Quote Originally Posted by TheGame46
    These are the only 3 I would add to my shake.

    Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise.

    * Blomstrand E,
    * Eliasson J,
    * Karlsson HK,
    * Kohnke R.

    Department of Surgical Science, Karolinska Institutet, Stockholm, Sweden. eva.blomstrand@gih.se

    BCAAs (leucine, isoleucine, and valine), particularly leucine, have anabolic effects on protein metabolism by increasing the rate of protein synthesis and decreasing the rate of protein degradation in resting human muscle. Also, during recovery from endurance exercise, BCAAs were found to have anabolic effects in human muscle. These effects are likely to be mediated through changes in signaling pathways controlling protein synthesis. This involves phosphorylation of the mammalian target of rapamycin (mTOR) and sequential activation of 70-kD S6 protein kinase (p70 S6 kinase) and the eukaryotic initiation factor 4E-binding protein 1. Activation of p70 S6 kinase, and subsequent phopsphorylation of the ribosomal protein S6, is associated with enhanced translation of specific mRNAs. When BCAAs were supplied to subjects during and after one session of quadriceps muscle resistance exercise, an increase in mTOR, p70 S6 kinase, and S6 phosphorylation was found in the recovery period after the exercise with no effect of BCAAs on Akt or glycogen synthase kinase 3 (GSK-3) phosphorylation. Exercise without BCAA intake led to a partial phosphorylation of p70 S6 kinase without activating the enzyme, a decrease in Akt phosphorylation, and no change in GSK-3. It has previously been shown that leucine infusion increases p70 S6 kinase phosphorylation in an Akt-independent manner in resting subjects; however, a relation between mTOR and p70 S6 kinase has not been reported previously. The results suggest that BCAAs activate mTOR and p70 S6 kinase in human muscle in the recovery period after exercise and that GSK-3 is not involved in the anabolic action of BCAAs on human muscle.

    Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise.

    * Karlsson HK,
    * Nilsson PA,
    * Nilsson J,
    * Chibalin AV,
    * Zierath JR,
    * Blomstrand E.

    Univ. College of Physical Education and Sports, Box 5626, S-114 86 Stockholm, Sweden.

    The aim of the study was to investigate the effect of resistance exercise alone or in combination with oral intake of branched-chain amino acids (BCAA) on phosphorylation of the 70-kDa S6 protein kinase (p70(S6k)) and mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK1/2), and p38 MAPK in skeletal muscle. Seven male subjects performed one session of quadriceps muscle resistance training (4 x 10 repetitions at 80% of one repetition maximum) on two occasions. In a randomized order, double-blind, crossover test, subjects ingested a solution of BCAA or placebo during and after exercise. Ingestion of BCAA increased plasma concentrations of isoleucine, leucine, and valine during exercise and throughout recovery after exercise (2 h postexercise), whereas no change was noted after the placebo trial. Resistance exercise led to a robust increase in p70(S6k) phosphorylation at Ser(424) and/or Thr(421), which persisted 1 and 2 h after exercise. BCAA ingestion further enhanced p70(S6k) phosphorylation 3.5-fold during recovery. p70(S6k) phosphorylation at Thr(389) was unaltered directly after resistance exercise. However, during recovery, Thr(389) phosphorylation was profoundly increased, but only during the BCAA trial. Furthermore, phosphorylation of the ribosomal protein S6 was also increased in the recovery period only during the BCAA trial. Exercise led to a marked increase in ERK1/2 and p38 MAPK phosphorylation, which was completely suppressed upon recovery and unaltered by BCAA. In conclusion, BCAA, ingested during and after resistance exercise, mediate signal transduction through p70(S6k) in skeletal muscle.

    Branched-chain amino acids improve glucose metabolism in rats with liver cirrhosis.

    * Ni****ani S,
    * Takehana K,
    * Fujitani S,
    * Sonaka I.

    Pharmaceutical Research Laboratories, Ajinomoto Co., Inc., Kawasaki-ku, Kawasaki-shi, Japan. shinobu_ni****ani@ajinomoto.co m

    It is well established that impaired glucose metabolism is a frequent complication in patients with hepatic cirrhosis. We previously showed that leucine, one of the branched-chain amino acids (BCAA), promotes glucose uptake under insulin-free conditions in isolated skeletal muscle from normal rats. The aim of the present study was to evaluate the effects of BCAA on glucose metabolism in a rat model of CCl(4)-induced cirrhosis (CCl(4) rats). Oral glucose tolerance tests were performed on BCAA-treated CCl(4) rats. In the CCl(4) rats, treatment with leucine or isoleucine, but not valine, improved glucose tolerance significantly, with the effect of isoleucine being greater than the effect of leucine. Glucose uptake experiments using isolated soleus muscle from the CCl(4) rats revealed that leucine and isoleucine, but not valine, promoted glucose uptake under insulin-free conditions. To clarify the mechanism of the blood glucose-lowering effects of BCAA, we collected soleus muscles from BCAA-treated CCl(4) rats with or without a glucose load. These samples were used to determine the subcellular location of glucose transporter proteins and glycogen synthase (GS) activity. Oral administration of leucine or isoleucine without a glucose load induced GLUT4 and GLUT1 translocation to the plasma membrane. GS activity was augmented only in leucine-treated rats and was completely inhibited by rapamycin, an inhibitor of mammalian target of rapamycin. In summary, we found that leucine and isoleucine improved glucose metabolism in CCl(4) rats by promoting glucose uptake in skeletal muscle. This effect occurred as a result of upregulation of GLUT4 and GLUT1 and also by mammalian target of rapamycin-dependent activation of GS in skeletal muscle. From these results, we consider that BCAA treatment may have beneficial effects on glucose metabolism in cirrhotic patients.
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    Quote Originally Posted by Bobo
    Umm...yeah thats all good and everything but there are only 3 to begin with.

    You do know there are only 3 right?
    Ok I'm out of it I meant to say leucine is the only "1" lol that I would add in bulk. Damn that early morning cardio stealing blood from my brain!
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    Quote Originally Posted by TheGame46
    I if you are going to add BCAA content there is only three I would add. Leucince, Isoluecine, and Valine, which have been shown to be key factors in hypertrophy. The rest of the BCAA content you need can easily be found in a good protein powder.
    I don't understand that either.
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    Quote Originally Posted by Bobo
    I don't understand that either.
    Did I not just calrify I meant to say AA?
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    Uh, no.
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    Quote Originally Posted by Bobo
    Uh, no.
    I edited the post! above dude
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    Oh....
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    Quote Originally Posted by Bobo
    Oh....
    LOL ya right after I posted i re-read it and went back and changed them but you alraedy caught me lol
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    Quote Originally Posted by Bobo
    I know you would! I still won't do it! lol

    This is what Nandi had to say when asked this:

    "So lots of peopel our builiding up ICE and rightfully so, it is a very good product. The thing is though...it seems that loading up on BCAA's would be awesome for dieting, their anti-catabloic /anabolic actions would make it great to take in between meals and keep muscle wasting at an absolute minimum. However with BCAA's increasing Insulin release, wouldn't they be counter productive to fat loss goals...just looking for others thoughts.."

    Quite possibly. Amino acid infusions produce insulin resistance:

    " A approximately 2.1-fold elevation of plasma anabolic steroids [amino acids] reduced whole-body glucose disposal by 25% (P < 0.01). Rates of muscle glycogen synthesis decreased by 64% (180--315 min, 24 plus minus 3; control, 67 plus minus 10 micromol center dot l(-1) center dot min(-1); P < 0.01), which was accompanied by a reduction in G6P starting at 130 min (DeltaG6P(260--300 min), 18 plus minus 19; control, 103 plus minus 33 micromol/l; P < 0.05). In conclusion, plasma amino acid elevation induces skeletal muscle insulin resistance in humans by inhibition of glucose transport/phosphorylation, resulting in marked reduction of glycogen synthesis. (1)

    The resulting insulin resistance would be expected to lead to hyperinsulinemia and impaired lipolysis.

    An even more interesting question ( in my mind ) is to what extent the resulting insulin resistance affects protein metabolism. If a person is insulin resistant with respect to glucose, are they also insulin resistant with respect to the anabolic effects of insulin? The answer may be yes, at least somewhat.

    Resistance to glucose uptake evidently does not affect amino acid uptake; the transport systems are different (2). So amino acid transport seems to be the same in normal and insulin resistant people, and the stimulatory effect of hyperaminoacidemia on protein synthesis is the same as well. However, what appears to be different is that in insulin resistance, the antiproteolytic effect of insulin is lost, at least in the research presented here:

    "In conclusion, insulin resistance is a common feature of both glucose and protein metabolism in obesity. The defect in protein metabolism is characterized by an impairment of the ability of insulin to inhibit proteolysis; the stimulatory effect of hyperaminoacidemia on protein synthesis is intact in obesity." (3)

    So it seems, ironically, that a high protein diet could actually lead to a catabolic state. This is especially true in light of the fact that a high protein diet induces subclinical metabolic acidosis, which raises cortisol levels."

    (1) Diabetes 2002 Mar;51(3):599-605

    Mechanism of amino acid-induced skeletal muscle insulin resistance in humans.

    Krebs M, Krssak M, Bernroider E, Anderwald C, Brehm A, Meyerspeer M, Nowotny P, Roth E, Waldhausl W, Roden


    (2) Diabetes 1993 Dec;42(12):1868-77

    Different sensitivity of glucose and amino acid metabolism to insulin in NIDDM.

    Luzi L, Petrides AS, De Fronzo RA


    (3) Am J Physiol 1996 Feb;270(2 Pt 1):E273-81

    Insulin and hyperaminoacidemia regulate by a different mechanism leucine turnover and oxidation in obesity.

    Luzi L, Castellino P, DeFronzo RA




    "Most athletes take in more protein than they need. Especially without a buffering protocol, the resulting acidosis is quite catabolic. The insulin resistance only adds insult to injury. This is especially true in anabolic steroids using athletes who are already experiencing some degree of anabolic steroids induced insulin resistance. Moreover, there is evidence that AAS users require LESS protein than non users becuase the cells become much more efficient at recycling amino acids.

    BCAA supplementation is a waste of money, IMHO, and probably detrimental as well."


    Consdering you asked this, I remember this from years ago.

    this is a prime example of researchers misinterpreting their own research (not nandi, i'm talking about the conclusions in the research cited). My advisor & I actually discussed this yesterday. Many of these researchers are convinced that leucine induces insulin resistance because it reduces the length of the insulin signal by reducing the phosphorylation of IRS-1. BUT IT IS THE VERY FACT that it cuts this short that in the long term it increases insulin sensitivity! If you don't cut the signal off & allow it to persist in the long term that will decrease sensitivity. By reducing the length of the signal it keeps your body more sensitive to insulin. Essentially they are trying to use a short term signal to look at a long term condition... which is ridiculous. When we run a high protein diet rich in bcaa vs a high carb diet in our lab, every time we see an increase in insulin area under the curve in response to a meal in the high carb group & every time we have seen a reduction in the protein group.

    -Layne
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    Quote Originally Posted by str8flexed
    this is a prime example of researchers misinterpreting their own research. My advisor & I actually discussed this yesterday. Many of these researchers are convinced that leucine induces insulin resistance because it reduces the length of the insulin signal by reducing the phosphorylation of IRS-1. BUT IT IS THE VERY FACT that it cuts this short that in the long term it increases insulin sensitivity! If you don't cut the signal off & allow it to persist in the long term that will decrease sensitivity. By reducing the length of the signal it keeps your body more sensitive to insulin. Essentially they are trying to use a short term signal to look at a long term condition... which is ridiculous. When we run a high protein diet rich in bcaa vs a high carb diet in our lab, every time we see an increase in insulin area under the curve in response to a meal in the high carb group & every time we have seen a reduction in the protein group.

    -Layne
    Yeah I know.

    I was giving him Nandi's point of view since he was very close friends with him and actually help develop his first product.
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    Aaaand then!
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    Quote Originally Posted by Bobo
    Take them with a small form of carbohydrate during workout. YOu can take the pre workout just take half pre and half during. IF you have adequate carbs before workout then you can just take them with water.
    What amount of BCAA do you suggest then (pre and during workout)? and combined with how much carb?
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    8-10g total with 15-20g carbs is fine.

    If you have a large pre workout meal then you don't even need the carbs.

    Keep it simple. No need to split hairs or megadose on this stuff IMO.
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    Quote Originally Posted by str8flexed
    this is a prime example of researchers misinterpreting their own research (not nandi, i'm talking about the conclusions in the research cited). My advisor & I actually discussed this yesterday. Many of these researchers are convinced that leucine induces insulin resistance because it reduces the length of the insulin signal by reducing the phosphorylation of IRS-1. BUT IT IS THE VERY FACT that it cuts this short that in the long term it increases insulin sensitivity! If you don't cut the signal off & allow it to persist in the long term that will decrease sensitivity. By reducing the length of the signal it keeps your body more sensitive to insulin. Essentially they are trying to use a short term signal to look at a long term condition... which is ridiculous. When we run a high protein diet rich in bcaa vs a high carb diet in our lab, every time we see an increase in insulin area under the curve in response to a meal in the high carb group & every time we have seen a reduction in the protein group.

    -Layne
    Interesting but how about using the lab to conduct an experiment with BCAA's vs. whey pre workout and protein synthesis.
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    Quote Originally Posted by Rostam
    What amount of BCAA do you suggest then (pre and during workout)? and combined with how much carb?
    ya genreally as long as your getting a 2:1 carb/protein ratio that is the key. I will do 15/15/30 pre mid post as far as grams of protein mixed with BCAA approximately.
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    Quote Originally Posted by USPLabs
    Interesting but how about using the lab to conduct an experiment with BCAA's vs. whey pre workout and protein synthesis.
    you want to get me the grant money chief?
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    Admin is living over his means so ask him. He's rich
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    lol... people don't realize even for a small scale animal study for something like this you are looking at 30K easy
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    Quote Originally Posted by str8flexed
    lol... people don't realize even for a small scale animal study for something like this you are looking at 30K easy
    depends on how you want to measuer it etc. but yes it is expensive. After working with IGF and other peptides in the lab its easy to see the bill stack up, and it really sux when you have all these great ideas and they tell you they just gave 8K to another group so ur screwed for a while !!!!
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    Quote Originally Posted by Bobo

    Keep it simple. No need to split hairs or megadose on this stuff IMO.
    hey bodybuilders are never guilty of splitting hairs
  

  
 

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