Announcement

Collapse
No announcement yet.

Amino Acids

Collapse
X
 
  • Filter
  • Time
  • Show
Clear All
new posts

  • Amino Acids

    Who here takes Amino acids as a supplement pill? Are they worth the money?

  • #2
    I use them with great success. I began using amino in pill form and in powder pre and post workout 1 week short of being 3 months ago. In that time I have dropped 20 pounds and increased every lift ,every week, in the gym since. I must add that 2 weeks ago I began an M1T and 4AD cycle as well. Since the addition of that things have increased more rapidly as they should. I tried to eliminate everything that would have an affect while I trialed the amino's. I have also began amino loading first thing when I get up and right before I go to bed... this has helped me continue to drop bf when I had hit a sticking point. Some say they dont work ( amino's), others have told me they only work if you have a piss poor diet, well at least for myself I disproved that theory. Is disproved a word?? Here is some other info posted on QM by Superior1:



    Branched-Chain Amino
    Acids (L-Leucine, L-
    Isoleucine, L-Valine)


    DESCRIPTION
    The branched-chain amino acids (BCAAs) comprise the three essential amino acids L-leucine, L-isoleucine and L-valine. These amino acids are found in proteins of all life forms. Dietary sources of the branched-chain amino acids are principally derived from animal and vegetable proteins. Vegetables and juices contain small amounts of the free amino acids, which are also found in fermented foods like yogurt and miso.


    Branched-chain amino acids are sometimes used in enteral and parenteral feedings in the management of hepatic encephalopathy. They are also occasionally used enterally and parenterally in the management of extensive burns and other severe trauma conditions because of their possible anticatabolic action in these conditions.

    L-leucine is also known as 2-amino-4-methylvaleric acid, alpha-aminoisocaproic acid and (S)-2-amino-4-methylpentanoic acid. It is abbreviated as Leu or by its one letter abbreviation L. Its molecular formula is C6H13NO2, and its molecular weight is 131.17 daltons. The structural formula is:


    L-isoleucine is also known as 2-amino-3-methylvaleric acid, alpha-amino-beta-methylvaleric acid and (2S, 3S)-2-amino-3-methylpentanoic acid. It is abbreviated as Ile or by its one letter abbreviation I. Its molecular formula is C 6H13NO2, and its molecular weight is 131.17 daltons. The structural formula is:

    L-valine is also known as 2-aminoisovaleric acid, 2-amino-3-methylbutyric acid, alpha-aminoisovaleric acid and (S)-2-amino-3-methylbutanoic acid. It is abbreviated as Val, and its one letter abbreviation is V. Its molecular formula is C5H11NO2, and its molecular weight is 117.15 daltons. The structural formula is:

    The branched-chain amino acids are sometimes classified as large neutral amino acids or LNAAs.

    ACTIONS AND PHARMACOLOGY
    ACTIONS
    The branched-chain amino acids may have antihepatic encephalopathy activity in some. They may also have anticatabolic and antitardive dyskinesia activity in some.

    MECHANISM OF ACTION
    Although amino acids are not considered important energy sources, BCAAs serve as important fuel sources for skeletal muscle during periods of metabolic stress. (i.e. training) Under such conditions, BCAAs may promote protein synthesis, suppress protein catabolism and serve as substrates for gluconeogenesis. BCAAs are mainly catabolized in skeletal muscle, stimulating the production of, among other substances, L-alanine and L-glutamine.


    PHARMACOKINETICS
    Following ingestion, the BCAAs are absorbed from the small intestine by a sodium-dependent active-transport process and transported to the liver via the portal circulation. In the liver, the BCAAs can serve as substrates for protein synthesis. Some catabolism of the BCAAs occurs in the liver. The catabolism of L-leucine, L-isoleucine and L-valine initially involves the same three reactions: the conversion of the amino acids to their corresponding alpha-keto acids; the conversion of the alpha-keto acids to their corresponding acyl-CoA thioesters and carbon dioxide; and the conversion of the acyl-CoA thioesters to their corresponding alpha, beta-unsaturated acyl-CoA thioesters. The enzyme deficiency in the inborn error of metabolism maple syrup urine disease is in the conversion of the acyl-CoA thioesters to the alpha, beta-unsaturated acyl-CoA thioesters, via the enzyme branched-chain alpha-keto acid decarboxylase.

    L-leucine, L-isoleucine and L-valine are catabolized differently starting from their corresponding acyl-CoA thioesters. L-leucine, which is a ketogenic amino acid, is converted via a number of metabolic steps to beta-hydroxy-beta-methyl-glutaryl-CoA, which in turn is converted to acetoacetic acid and acetyl-CoA. The B vitamin biotin participates in this pathway. L-isoleucine, which is both glycogenic and ketogenic, is converted via a number of metabolic steps to alpha-methyl-acetoacetyl-CoA, which in turn is converted to acetyl-CoA (ketogenic) and propionyl-CoA (glycogenic). Finally, the glycogenic L-valine is converted via a number of steps to methylmalonyl-CoA and then, with the assistance of vitamin B12, to succinyl-CoA.

    The BCAAs are distributed to the various tissues of the body via the systemic circulation. The BCAAs appear to be preferentially taken up by skeletal muscle, where they undergo similar catabolic reactions to those described above. Skeletal muscle appears to be the major site of both BCAA transamination and oxidation in humans. BCAAs are also taken up by other organs, particularly the brain and kidney, where they also undergo oxidation.

    INDICATIONS AND USAGE
    There is preliminary evidence that BCAAs may prevent muscle catabolism and promote protein synthesis in some trauma subjects and, possibly, in some exercises. There is no evidence that they are effective for enhancement of athletic performance. Neither have they proved useful in treating amotrophic lateral sclerosis (ALS). In one trial, BCAAs reduced symptoms of tardive dyskinesia. They have also been used with some benefit in some with phenylketonuria.

    RESEARCH SUMMARY
    Meta-analyses have produced conflicting and largely ambiguous results with respect to the role, if any, that BCAAs may play in the prevention or treatment of hepatic encephalopathy. One group of researchers concluded several years ago that BCAAs might be helpful in treating some with advanced cirrhosis who are intolerant to alimentary proteins. More recently, a consensus review written under the auspices of the European society for parenteral and enteral nutrition, similarly concluded that BCAAs might be indicated in that small number of patients intolerant to the supplementary dietary proteins needed to achieve nitrogen balance in this condition.

    There is some preliminary evidence that BCAAs might help prevent muscle catabolism and promote protein synthesis in those with various forms of trauma. In one very small study, BCAAs were reported to inhibit protein breakdown in five men exercising the knee extensor muscles. Another very small study suggested that BCAAs might have inhibited muscle glycogen degradation during exercise.

    On the other hand, there is no credible evidence that BCAAs have any significant effect on exercise performance. In a study of well-trained cyclists, BCAAs had no effect on performance in a 100-kilometer trial.

    There were some early reports suggesting that BCAAs might help ameliorate some of the symptoms of amyotrophic lateral sclerosis (ALS). In one of these studies, ALS patients receiving 12 grams of L-leucine, 8 grams of L-isoleucine and 6.4 grams of L-valine daily for one year showed significant benefit, as measured by maintenance of muscle strength in extremities and walking ability. Those receiving placebo in this small study showed a linear decline in these parameters consistent with the normal course of this disease.

    CONTRAINDICATIONS, PRECAUTIONS, ADVERSE REACTIONS
    CONTRAINDICATIONS
    Branched-chain amino acids are contraindicated in those with the rare inborn errors of metabolism maple syrup urine disease and isovaleric acidemia. BCAAs are also contraindicated in those with hypersensitivity to any component of a BCAA-containing supplement.

    PRECAUTIONS
    Pregnant women and nursing mothers should avoid BCAA supplementation.

    OVERDOSAGE
    No reports of overdosage.

    DOSAGE AND ADMINISTRATION
    Branched-chain amino acids are available for enteral and parenteral nutrition in the management of hepatic encephalopathy and metabolic stress conditions.

    Nutritional supplements of BCAAs are available. Dosage is variable. Some combination BCAA products include other nutrients such as biotin and vitamin B12, which are involved in the metabolism of the BCAAs.

    HOW SUPPLIED
    Capsules

    Powder

    Tablets

    LITERATURE
    Abeta S, Inoue N, Matsui H, Yoshino Y. [Effect of branched-chain amino acids on glutamate neurotoxicity in primary cultured rat cerebral neurons.] [Article in Japanese.] Rinsho Shinkeigaku. 1995; 35:420-423.

    Austic RE, Su C-L, Strupp BJ, Levitsky DA. Effects of dietary mixtures of amino acids on fetal growth and maternal and fetal amino acid pools in experimental maternal phenylketonuria. Am J Clin Nutr. 1999; 69:687-696.

    Bastone A, Michel. A, Beghi E, Salmona M. The imbalance of brain large-chain amino acid availability in amyotrophic lateral sclerosis patients treated with high doses of branched-chain amino acids. Neurochem Int. 1995; 27:467-472.

    Berry HK, Brunner RL, Hunt MM, White PP. Valine, isoleucine and leucine. A new treatment for phenylketonuria. Am J Dis Child. 1990; 144:539-543.

    Fabbri A, Magrini N, Bianchi G, et al. Overview of randomized clinical trials of oral branched-chain amino acid treatment in chronic hepatic encephalopathy. J Parenter Enteral Nutr. 1996; 20:159-164.

    MacLean DA, Graham TE, Saltin B. Stimulation of muscle ammonia production during exercise following branched-chain amino acid supplementation in humans. J Physiol (Lond). 1996; 493(Pt3):909-922.

    Maddrey WC. Branched chain amino acid therapy in liver disease. J Am Coll Nutr. 1985; 4:639-650.

    Madsen K, Maclean DA, Kiens B, Christensen D. Effects of glucose, glucose plus branched-chain amino acids, or placebo on bike performance over 100km. J Appl Physiol. 1996; 81:2644-2650.

    Marchesini G, Bianchi G, Rossi B, et al. Nutritional treatment with branched-chain amino acids in advanced liver cirrhosis. J Gastroenterol. 2000; 35 Suppl 12:7-12.

    Marchesini G, Zoli M, Dondi C, et al. Anticatabolic effect of branched-chain amino acid-enriched solutions with liver cirrhosis. Hepatology. 1982; 2:420-425.

    Pelosi G, Proietti R, Magalini SI, et al. Anticatabolic properties of branched chain amino acids in trauma. Resuscitation. 1983; 10:153-158.

    Plaitakis A, Smith J, Mandeli J, Yahr MD. Pilot trial of branched-chain amino acids in amyotrophic lateral sclerosis. Lancet. 1988; 1(8593):1015-1018.

    Richardson MA, Bevans ML, Weber JB, et al. Branched chain amino acids decrease tardive dyskinesia symptoms. Psychopharmacol. 1999; 143:358-364.

    Suryawan A, Hawes JW, Harris RA, et al. A molecular model of human branched-chain amino acid metabolism. Am J Clin Nutr. 1998; 68:72-81.

    Tandan R, Bromberg MB, Forshew D, et al. A controlled trial of amino acid therapy in amyotropic lateral sclerosis: I. Clinical, functional, and maximum isometric torque data. Neurology. 1996; 47 -1226.

    Testa D, Caraceni T, Fetoni V. Branched-chain amino acids in the treatment of amyotrophic lateral sclerosis. J Neurol. 1989; 236:445-447.

    The Italian ALS Study Group. Branched-chain amino acids and amyotrophic sclerosis: a treatment failure? Neurology. 1993; 43:2466-2470.


    I have more info if you want it, I thought this may be enough for 1 post

    PD
    Last edited by Pumpdogg; 12-30-04, 01:44 PM.

    Comment


    • #3
      Protein pills cost too much, at least the ones I've seen.

      Not sure why you are saying that BCAA's are ketogenic, Pumpdogg. Most aminos can stimulate the release of Glucogon if the blood sugar levels are low (and therefor insulin), but if blood amino levels are too high they will be used preferentially before ketone stores. Ketogenesis requires moderately low blood amino and glucose levels which are normally achieved through lowered food intake or elevated activity levels.

      Here is a less technical rundown on proteins in general
      http://www.onr.com/user/lylemcd/Prot...teinpart1.html

      Comment


      • #4
        Hey Gort that was part of the piece I pulled from QM site posted by Superior1. I should have proof read the piece again, it had been a while since I looked at that post. I will pull out the comments of the author and leave the rest of the study.

        PD

        Comment

        Working...
        X