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  1. #1
    Actual Pharmacist Bane's Avatar
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    Actual Pharmacist Bane's Avatar
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    Actual Pharmacist Bane's Avatar
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    More...
    Unfortunately the study Big'r asked me for isn't yet available full text
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    Registered User Big_r's Avatar
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    I'm getting in to them Bane.

    Bit busy searching pubmed for additional info about the super-supplement glutamine.

    One thing s*cks: i can only open the pdf's.
    Thanx so far.
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  5. #5
    C6H13NO2 pu12en12g's Avatar
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    "Exercise Promotes BCAA Catabolism: Effects of BCAA Supplementation on Skeletal Muscle during Exercise"

    http://www.nutrition.org/cgi/reprint/134/6/1583S




    "High levels of dietary amino and branched-chain alpha-keto acids alter plasma and brain amino acid concentrations in rats."

    http://forum.bodybuilding.com/showpo...&postcount=171




    "Leucine Supplementation and Intensive Training"

    http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract


    "Essential amino acids and muscle protein recovery from resistance exercise"

    http://ajpendo.physiology.org/cgi/co...ull/283/4/E648


    A interesting perspective:

    "Ingesting free, crystalline L-amino acids is thought by many athletes to be superior to ingesting natural foods containing protein for muscle protein synthesis. However, amino acids using the same carrier system compete with each other for absorption. Thus, ingesting one amino acid or a particular group of amino acids that use the same carrier system may create, depending on the amount ingested, a competition between the amino acids for absorption. The result may be that the amino acid present in the highest concentration is absorbed but also may impair the absorption of the other, less concentrated amino acids carried by that same system. Thus, amino acid supplements may result in impaired or imbalanced amino acid absorption. Furthermore, absorption of peptides (which are obtained from digestion of natural protein-containing foods) is more rapid than absorption of an equivalent mixture of free amino acids. Also, nitrogen assimilation following ingestion of protein-containing foods is superior to that following ingestion of free amino acids. In other words, free amino acids have no absorptive advantage."

    "Advanced Nutrition and Human Metabolism", 4th Edition, pg 184

    "Amino Acids Stimulate Translation Initiation and Protein Synthesis through an Akt-Independent Pathway in Human Skeletal Muscle"

    http://jcem.endojournals.org/cgi/con...ull/87/12/5553


    "Amino acids regulate skeletal muscle PHAS-I and p70 S6-kinase phosphorylation independently of insulin"

    http://ajpendo.physiology.org/cgi/reprint/279/2/E301
    Last edited by pu12en12g; 10-15-2005 at 02:41 PM.
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  6. #6
    C6H13NO2 pu12en12g's Avatar
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  7. #7
    Registered User Big_r's Avatar
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    Keep em coming, keep em coming
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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  8. #8
    Registered User siegler's Avatar
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    Glutamine is only interesting when used for the immunesystem - supplementation for bodybuilding purposes DOES NOT increase protein synthesis nor does it add pounds of muscle to your frame.

    Can't believe that everyone is still buying into this crap.

    Ask Pat Arnold what he thinks..

    Glutamine is not worthless but it is for bodybuilding purposes. L-leucine might be an interesting amino acid just as propiony L-carntine for mainting muscle mass. Glutamine is usefull if you have the flu or have suffer from Crohn or some other intestinal disease.

    I rate glutamine as a bodybuilding supplement zero

    Better spend some money on a marine oil supplement if you cannot stand eating coldwater fish. Unfortunately there are not many nutritional ingredients that will be reviewed as worthwhile in the longrun. Most will be forgotten as time goes by.
    Last edited by siegler; 10-16-2005 at 01:11 PM.
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  9. #9
    bada bing! tonutzda2@veriz's Avatar
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    so what's the scoop with the amino acids are the good or bad?
    Hard work pays off.Lift big or go home :)
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  10. #10
    Actual Pharmacist Bane's Avatar
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    Originally Posted by Big'r
    Keep em coming, keep em coming
    I will, we will. Didn't occur to me to post the abstracts too

    P.S. pu12en12g nice image
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  11. #11
    Actual Pharmacist Bane's Avatar
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    Amino acids (AAs), especially BCAAs, play pivotal roles in hormonal secretion and action as well as in intracellular signaling. There is emerging data showing that BCAAs regulate gene transcription and translation. Signaling proteins such as the mammalian target of rapamycin act as sensors of BCAAs, especially leucine, to modulate anabolic action. AAs stimulate protein synthesis and inhibit protein breakdown in skeletal muscle and liver. The specific role of BCAAs in regulating synthesis and breakdown of individual protein or proteins with common function or functions remains to be defined. Future studies should also focus on potential adverse effects of BCAAs on insulin sensitivity, renal function, and tumor growth. It also remains to be determined whether potential adverse effects of BCAA supplementation is similar in people of different age groups.
    BCAAs seem to be very safe:
    Since the in vitro study of Buse and Reid in 1975 showing a stimulatory effect of leucine upon rat muscle protein synthesis and reduction in proteolysis, a similar effect has been sought in humans. In 1978, Sherwin demonstrated in humans an improvement in N balance with infusion of leucine in obese subjects fasting to lose weight. A variety of subsequent studies have been performed in humans where leucine alone or the BCAAs have been administered in varying amounts and durations, and the effect upon protein metabolism has been measured. Measurements of changes in muscle amino acid metabolism were made by arteriovenous difference measurements and by biopsies. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. Later studies using stable isotope tracers to define both whole-body protein turnover and leg or arm protein metabolism have similarly concluded that leucine administration specifically induces a reduction in protein breakdown without increasing protein synthesis. This anabolic effect, produced through a reduction of protein breakdown in vivo in humans by leucine is contrary to in vitro studies of rat muscle where stimulation of protein synthesis, has been demonstrated by leucine. Likewise an increase in protein synthesis has also been demonstrated by insulin in rat muscle that is not seen in humans. Of the various studies administering BCAAs or leucine to humans for varying periods of time and amount, the results have been consistent. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day.
    BCAAs are also good for the traumatized liver. Also pdf#1
    Because of their peculiar role in whole-body nitrogen metabolism and the competitive action on amino acid transport across the blood-brain barrier, branched-chain amino acids (BCAAs) have been extensively used in subjects with liver disease to preserve or to restore muscle mass and to improve hepatic encephalopathy. There are no data regarding safe limits of BCAA administration; the results appear to be better when BCAA-enriched formulas or BCAA-supplemented diets are preferred to pure BCAA formulas. Improved nitrogen retention might ameliorate the nutritional status, a prognostic index of long-term survival in cirrhosis and of short-term survival in patients undergoing surgical procedures. The effects on nutrition and ultimately on prognosis of patients with advanced cirrhosis were confirmed in a large multicenter, long-term trial where oral BCAA supplements were compared with equicaloric or equinitrogenous-equicaloric supplements (maltodextrin or lactoalbumin). Similarly, BCAA treatment improved the prognosis of patients with hepatocellular carcinoma, treated by surgical resection or chemoembolization, and of liver transplant patients. The mechanism(s) for the beneficial effects of BCAAs might be mediated by their stimulating activity on hepatocyte growth factor, favoring liver regeneration. The debate regarding the potential effectiveness of BCAAs dates back to the early 1980s. The number of patients who cannot tolerate dietary proteins in amounts sufficient to meet the higher catabolism of advanced liver disease is probably low, but BCAAs remain the sole treatment of proved efficacy in this specific setting.
    pdf#3 is a must of must, almst worthy to post entirely on a new post(maybe I'll do so another time). Pasted text from it:
    Evidence supporting a beneficial role for BCAAs in
    treating a variety of diseases has accumulated over the
    past 30 years, and continues to grow each year. New
    areas for their use, both as regulators of protein
    metabolism and as regulators of neurotransmitter synthesis,
    are emerging. We need long-term, randomized
    clinical studies, both in the prevention and in the
    treatment of various pathological conditions. These
    studies, as the recent BCAA trial in cirrhosis showed
    [11..], are extremely difficult to perform, but they are
    the only way to improve our standard of care.
    Last edited by Bane; 10-20-2005 at 08:55 AM.
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  12. #12
    Registered User Big_r's Avatar
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    BCAAs prevent protein breakdown, but do not increase protein synthesis.
    -Since 1978 a variety of studies have been performed in humans where BCAAs or leucine alone was administrated in varying amounts and durations. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day (B1).
    -BCAA infusion in 10 postabsorptive normal subjects causes a 4-fold rise in arterial BCAA levels. Plasma insulin levels were unchanged from basal levels. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by BCAA infusion. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids (B2).
    -Short-term (3 to 4 hours) infusion of branched-chain amino acids (BCAA) has been shown to suppress muscle protein breakdown.
    An overnight (16-hour) systemic BCAA infusion in 8 subjects increases plasma BCAA concentrations by fivefold to eightfold, and this was associated with a 20% to 60% decline in arterial concentrations of other amino acids.
    In the forearm, overnight BCAA infusion resulted in a diminished net release of Phe (-3 +/- 2 v -18 +/- 4 [saline] nmol/min/100 mL, P < .02), and BCAA balance became markedly positive (751 +/- 93 v -75 +/- 30, P < .001) (B4).
    -BCAA infusion in 10 postabsorptive normal subjects does not change plasma insulin levels. Skeletal muscle proteolysis was suppressed in the absense of any apparent increase in muscle protein synthesis (B5).
    -In humans, infusion of BCAA alone slows skeletal muscle protein degradation, but does not increase protein synthesis. This is perhaps not surprising, as the BCAA also inhibit whole body protein degradation and thereby decrease the arterial concentrations of other essential and nonessential amino acids. This decline may blunt any effect of infused BCAA on protein synthesis by limiting substrate availability and/or interfering with nutrient signaling by other amino acids.
    BCAA stimulate the phosphorylation of eIF4E-BP1 and p70S6K involved in activating the mRNA translation apparatus. These results demonstrate that the cellular pathways that regulate translation initiation are, in fact, stimulated by BCAA in humans and suggest a potentially significant anabolic signaling role for BCAA in increasing mRNA translation and protein synthesis. This occurs with increments of circulating BCAA like those seen postprandially, suggesting that this is a normal physiological response.
    After a 12 h overnight fast 7 healthy volunteers were adminitered a BCAA infusion for 6 h. Insulin concentrations did not significantly change. BCAA infusion significantly improved forearm phenylalanine balance in control subjects at 6 h (Fig. 4A), although, as we previously reported, it did not increase phenylalanine Rd (B6).
    -BCAAs during 1h cycle exercise and a 2h recovery period does not influence the rate of exchange of the aromatic AAs during exercise. In the recovery period, a faster decrease in the muscle concentration of aromatic AAs was found (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise (E5)
    -7.5-12 g BCAAs during intense exercise (a 30 km cross-country race and a full marathon) increases BCAA plasma and muscle concentration. In the placebo group plasma BCAA decreased and left muscle levels unchanged. The placebo group showed a 20-40% increase in the muscle concentration of aromatic AAs. BCAA supplementation prevented this increase in aromatic AAs in both muscle and plasma. These results suggest that an intake of BCAAs during exercise can prevent or decrease the net rate of protein degradation caused by heavy exercise (E8).
    -Consumption of BCAA (30 to 35% leucine) before or during endurance exercise may prevent or decrease the net rate of protein degradation, may improve both mental and physical performance and may have a sparing effect on muscle glycogen degradation and depletion of muscle glycogen stores (E14).
    -77 mg BCAAs/kg supplementation before exercise resulted in a doubling (P < 0.05) of the arterial BCAA levels before exercise (339 +/- 15 vs. 822 +/- 86 microM). During the 60 min of exercise, the total release of BCAA was 68 +/- 93 vs. 816 +/- 198 mumol/kg (P < 0.05) for the BCAA and control trials, respectively. Furthermore, the increased intramuscular and arterial BCAA levels before and during exercise result in a suppression of endogenous muscle protein breakdown during exercise.(E105).
    -BCAA activate mRNA translation initiation, but without the anticipated increase in protein synthesis. One possible explanation for this apparent discrepancy is that BCAA inhibit proteolysis and thereby decrease the arterial concentrations of other AA (P4).
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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  13. #13
    Registered User Big_r's Avatar
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    Helps in fat loss while cutting
    -BCAA supplementation (76% leucine) in combination with moderate energy restriction has been shown to induce significant and preferential losses of visceral adipose tissue and to allow maintenance of a high level of performance (E14).
    -In adipocytes from fed rats, the rate of fatty acid synthesis in the presence of glucose and insulin was inhibited 40% by valine (5 mm) (E4).
    -Twenty-five competitive wrestlers restricted their caloric intake (28 kcal.kg-1.day-1) for 19 days. A high-BCAA diet provided 4 kg of weight loss, and 17,3% decrease in fat loss. There was no change in aerobic (VO2max) (p > 0.75) and anaerobic capacities (Wingate test) (p > 0.81), and in muscular strength (p > 0.82). (E7).

    Prevents a decrease in glutamine
    -Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation (G12).
    -BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine (G13).

    Prevents muscle damage
    -We hypothesized that BCAA supplementation would reduce the serum activities of intramuscular enzymes associated with muscle damage. 120 minutes exercise on a cycle ergometer significantly increases serum creatine kinase (CK) and lactate dehydrogenase (LDH) up to 5d postexercise.
    12 g BCAAs for 14d in 16 men (the exercise on day 7) significantly reduces this change in LDH and CK (B3).



    REFERENCES

    (B1)http://www.ncbi.nlm.nih.gov/entrez/q...473&query_hl=1
    (B2)http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
    (B3)http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
    (B4)http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
    (B5)http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
    (B6)http://jcem.endojournals.org/cgi/content/full/86/5/2136
    (E4) http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract
    (E5) http://ajpendo.physiology.org/cgi/co...ull/281/2/E365
    (E7) http://www.ncbi.nlm.nih.gov/entrez/q...t=ExternalLink
    (E8) http://www.ncbi.nlm.nih.gov/entrez/q...t=ExternalLink
    (E14) http://www.ncbi.nlm.nih.gov/entrez/q...t=ExternalLink
    (E105) http://www.ncbi.nlm.nih.gov/entrez/q...t=ExternalLink
    (G12) http://www.ncbi.nlm.nih.gov/entrez/q...939&query_hl=1
    (G13) http://www.ncbi.nlm.nih.gov/entrez/q...884&query_hl=1
    (P4)http://jcem.endojournals.org/cgi/con...ull/87/12/5553
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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  14. #14
    C6H13NO2 pu12en12g's Avatar
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    Originally Posted by BiggJohn
    This one is my favorite on leucine, and it is actually done on humans.


    The combined ingestion of protein and free leucine with carbohydrate increases post-exercise muscle protein synthesis in vivo in male subjects.

    Am J Physiol Endocrinol Metab. 2004 Nov 23;

    Koopman R, Wagenmakers AJ, Manders RJ, Zorenc AH, Senden JM, Gorselink M, Keizer HA, van Loon LJ.

    Department of Human Biology, Nutrition Research Institute Maastricht (NUTRIM Maastricht University, Maastricht, The Netherlands.

    The present study was designed to determine post-exercise muscle protein synthesis and whole-body protein balance following the combined ingestion of carbohydrate with or without protein and/or free leucine. Eight male subjects were randomly assigned to 3 trials in which they consumed drinks containing either carbohydrate (CHO), carbohydrate and protein (CHO+PRO), or carbohydrate, protein and free leucine (CHO+PRO+leu) following 45 min of resistance exercise. A primed, continuous infusion of L-[ring-(13)C6]phenylalanine was applied, with blood samples and muscle biopsies collected to assess fractional synthetic rate (FSR) in the m. vastus lateralis as well as whole-body protein turnover during 6 h of post-exercise recovery. Plasma insulin response was higher in the CHO+PRO+leu compared to the CHO and CHO+PRO trials (+240+/-19% and +77+/-11%, respectively, P<0.05). Whole-body protein breakdown rates were lower, and whole-body protein synthesis rates were higher in the CHO+PRO and CHO+PRO+leu trials compared to the CHO trial (P<0.05). Addition of leucine in the CHO+PRO+leu trial resulted in a lower protein oxidation rate compared to the CHO+PRO trial. Protein balance was negative during recovery in the CHO trial, but positive in the CHO+PRO and CHO+PRO+leu trials. In the CHO+PRO+leu trial, whole-body net protein balance was significantly greater compared to values observed in the CHO+PRO and CHO trials (P<0.05). Mixed muscle FSR, measured over a 6h period of post-exercise recovery, was significantly greater in the CHO+PRO+leu trial compared to the CHO trial (0.095+/-0.006 %(.)h(-1) vs. 0.061+/-0.008 %(.)h(-1), respectively; P<0.05), with intermediate values observed in the CHO+PRO trial (0.0820 +/- 0.0104 %(.)h(-1)). We conclude that the co-ingestion of protein and leucine stimulates muscle protein synthesis and optimizes whole-body protein balance when compared to the intake of carbohydrate only.
    .....
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    Actual Pharmacist Bane's Avatar
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    Originally Posted by pu12en12g
    .....
    Cool. Tomorrow I'll bring the full pdf i hope
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    Good thread man! You're taking over my job...
    Matt Weik, BS, CSCS, CPT, CSN
    www.MattWeik.com
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    Actual Pharmacist Bane's Avatar
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    Originally Posted by MCWTRAINER
    Good thread man! You're taking over my job...
    What job? I never wanted to be a personal trainer :P
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    The Physique Architect str8flexed's Avatar
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    here's the new study i was talking about plus a few others

    http://www.ncbi.nlm.nih.gov/entrez/q...230&query_hl=3
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    great thread!
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    Lightbulb Interesting reading

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    C6H13NO2 pu12en12g's Avatar
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    Observations of Branched-Chain Amino Acid Administration in Humans

    .PDF format
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    Registered User Big_r's Avatar
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    Originally Posted by pu12en12g
    Observations of Branched-Chain Amino Acid Administration in Humans

    .PDF format
    Thanx man!

    Can anyone get their hands on this complete study:

    Flooding with L-[1-13C]leucine stimulates human muscle protein incorporation of continuously infused L-[1-13C]valine.

    BTW How do you guys get your hands on these complete studies?
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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    The Physique Architect str8flexed's Avatar
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    Originally Posted by Big'r
    Thanx man!

    Can anyone get their hands on this complete study:

    Flooding with L-[1-13C]leucine stimulates human muscle protein incorporation of continuously infused L-[1-13C]valine.

    BTW How do you guys get your hands on these complete studies?
    I have access to the university of IL library, the third biggest library in the US. I would post the study on here but it's too large. If you PM me your email i'll send you the study.

    -Layne
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    Erotic Politician BiggJohn's Avatar
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    Originally Posted by pu12en12g
    .....

    That was orginally posted by Nandi on CEM.
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    Actual Pharmacist Bane's Avatar
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    Originally Posted by Big'r
    Thanx man!

    Can anyone get their hands on this complete study:

    Flooding with L-[1-13C]leucine stimulates human muscle protein incorporation of continuously infused L-[1-13C]valine.

    BTW How do you guys get your hands on these complete studies?
    Tried to find it, but unfortunately for now only the abstract is availabel for me I can request an interlibrary loan, but that is a process I do only for studies that interest me(not an easy or fast process).
    I have access to the computers of Aristotele University of Thessaloniki, which has subscription to most of the worlds journals, databases e.t.c. If you search for a particular study PM me or mail me and I'll see what I can do.
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    Registered User Big_r's Avatar
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    Originally Posted by str8flexed
    I have access to the university of IL library, the third biggest library in the US. I would post the study on here but it's too large. If you PM me your email i'll send you the study.

    -Layne

    I only have access to a rather "bad" dictionary!

    Did the pm thing.

    Suddenly remembered the name of a good uploadsite for sharing somewhat larger files.
    Just upload and copy/past the given URL. Siample:

    http://rapidshare.de/
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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  27. #27
    Registered User Big_r's Avatar
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    Originally Posted by Bane
    Tried to find it, but unfortunately for now only the abstract is availabel for me I can request an interlibrary loan, but that is a process I do only for studies that interest me(not an easy or fast process).
    I have access to the computers of Aristotele University of Thessaloniki, which has subscription to most of the worlds journals, databases e.t.c. If you search for a particular study PM me or mail me and I'll see what I can do.
    Thanx guys "thumbs up smilie"
    Which SUPPLEMENTS do i use PRE/POSTWORKOUT:
    [url]http://forum.bodybuilding.com/showthread.php?t=584191[/url]
    The effects of ANTI-E'S and AI'S on the axis and gyno:
    [url]http://forum.bodybuilding.com/showthread.php?t=587578&highlight=raloxifene[/url]
    MILK THISTLE info:
    http://forum.bodybuilding.com/showthread.php?t=629438
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  28. #28
    Actual Pharmacist Bane's Avatar
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    Originally Posted by Big'r
    Thanx guys "thumbs up smilie"
    No we thank you! I admire your patience to read all this stuff and write articles based on them(and to your non-native language to boot!). Personally my patience wanes the moment I read & post them. I hope you enjoy the 10s of studies I have posted these days.
    Keep up the good work!
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  29. #29
    Actual Pharmacist Bane's Avatar
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    Originally Posted by jonny21
    Some pretty good articles/studies, thanks.
    I don't think I saw this one:

    http://ajpendo.physiology.org/cgi/co...ull/281/2/E197

    Emmmm.....
    I thank you for trying to be helpful but the link you provided is about Aminos in general, not BCAAs. BCAAs are leucine, isoleucine and valine.
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  30. #30
    AEN Board Rep HalleluYAH's Avatar
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    Regulation of cardiac and skeletal muscle protein synthesis by individual branched-chain amino acids in neonatal pigs.

    Escobar J, Frank JW, Suryawan A, Nguyen HV, Kimball SR, Jefferson LS, Davis TA.

    USDA/ARS Children's Nutrition Research Center, Dept. of Pediatrics, Baylor College of Medicine, 1100 Bates St., Houston, TX 77030. tdavis@bcm.tmc.edu).

    Skeletal muscle grows at a very rapid rate in the neonatal pig, due in part to an enhanced sensitivity of protein synthesis to the postprandial rise in amino acids. An increase in leucine alone stimulates protein synthesis in skeletal muscle of the neonatal pig; however, the effect of isoleucine and valine has not been investigated in this experimental model. The left ventricular wall of the heart grows faster than the right ventricular wall during the first 10 days of postnatal life in the pig. Therefore, the effects of individual BCAA on protein synthesis in individual skeletal muscles and in the left and right ventricular walls were examined. Fasted pigs were infused with 0 or 400 mumol.kg(-1).h(-1) leucine, isoleucine, or valine to raise individual BCAA to fed levels. Fractional rates of protein synthesis and indexes of translation initiation were measured after 60 min. Infusion of leucine increased (P < 0.05) phosphorylation of eukaryotic initiation factor (eIF)4E-binding protein-1 and increased (P < 0.05) the amount and phosphorylation of eIF4G associated with eIF4E in longissimus dorsi and masseter muscles and in both ventricular walls. Leucine increased (P < 0.05) the phosphorylation of ribosomal protein (rp)S6 kinase and rpS6 in longissimus dorsi and masseter but not in either ventricular wall. Leucine stimulated (P < 0.05) protein synthesis in longissimus dorsi, masseter, and the left ventricular wall. Isoleucine and valine did not increase translation initiation factor activation or protein synthesis rates in skeletal or cardiac muscles. The results suggest that the postprandial rise in leucine, but not isoleucine or valine, acts as a nutrient signal to stimulate protein synthesis in cardiac and skeletal muscles of neonates by increasing eIF4E availability for eIF4F complex assembly.
    Contributing Author, Strength and Science Weekly
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