β-alanine is a breakdown product of carnosine and anserine, which are dipeptides from meat consumption. Although β-alanine’s properties are limited, its relationship to carnosine makes it important. Both have antioxidant properties. Carnosine is critical for pH buffering in skeletal muscle during exercise, but its formation can be limited by enzymatic factors.
For this reason, supplementation with β-alanine is sometimes used to enhance carnitine and therefore improve athletic performance. In addition to diet and supplementation, β-alanine can also be endogenously produced. This occurs via degradation of uracil in the liver but it can also bea made by intestinal bacteria such as E. coli.
Since β-alanine comes from meat consumption, endogenous production is the only source in vegetarian and vegan populations. Given their limited diets, vegetarians and vegans have lower levels of β-alanine and muscle carnosine compared to omnivores. There is also an interesting interplay between taurine and β-alanine. Taurine and β-alanine share the same skeletal muscle transporter, whereby β-alanine can inhibit taurine’s uptake into muscle. Elevated beta-alanine can sometimes deplete taurine leading to oxidative stress, causing tissue damage. Additionally, these two amino acids compete for the same reabsorption transporters in the kidney. Elevated β-alanine can contribute to renal wasting of taurine.
References:
- Trexler ET, Smith-Ryan AE, Stout JR, et al. International society of sports nutrition position stand: Beta-Alanine. J Int Soc Sports Nutr. 2015;12:30.
- Eaton K, Howard M, Mphil AH. Urinary beta-alanine excretion is a marker of abnormal as well as normal gut fermentation. J Nutr Med. 1994;4(2):157-163.
- Trexler ET, Smith-Ryan AE, Stout JR, et al. International society of sports nutrition position stand: Beta-Alanine. J Int Soc Sports Nutr. 2015;12:30-30.
- Shetewy A, Shimada-Takaura K, Warner D, et al. Mitochondrial defects associated with beta-alanine toxicity: relevance to hyper-beta-alaninemia. Molec Cell Biochem. 2016;416(1-2):11-22.
- Jong CJ, Azuma J, Schaffer S. Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids. 2012;42(6):2223-2232.
- Chesney RW, Han X, Patters AB. Taurine and the renal system. J Sci. 2010;17 Suppl 1(Suppl 1):S4-S4.
- Suidasari S, Stautemas J, Uragami S, Yanaka N, Derave W, Kato N. Carnosine Content in Skeletal Muscle Is Dependent on Vitamin B6 Status in Rats. Front Nutr. 2015;2:39.
- Hahn CD, Shemie SD, Donner EJ. Status Epilepticus. In: Ped Critic Care. Elsevier; 2011:837-848.
- Parviz M, Vogel K, Gibson KM, Pearl PL. Disorders of GABA metabolism: SSADH and GABA-transaminase deficiencies. J Ped Epilepsy. 2014;3(4):217-227.
- Blancquaert L, Baba SP, Kwiatkowski S, et al. Carnosine and anserine homeostasis in skeletal muscle and heart is controlled by beta-alanine transamination. J Physiol. 2016;594(17):4849-4863.
- Perim P, Marticorena FM, Ribeiro F, et al. Can the Skeletal Muscle Carnosine Response to Beta-Alanine Supplementation Be Optimized? Front Nutr. 2019;6:135.
- Peters V, Klessens CQ, Baelde HJ, et al. Intrinsic carnosine metabolism in the human kidney. Amino Acids. 2015;47(12):2541-2550.
- Eaton K, Howard M, Mphil AH. Urinary beta-alanine excretion is a marker of abnormal as well as normal gut fermentation. J Nutr Med. 1994;4(2):157-163.
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Levels may be elevated in meat consumption when dipeptides anserine and carnosine are elevated since they both contain β-alanine. Supplementation with β-alanine also results in elevated levels.
Urinary beta-alanine excretion is associated with gut bacterial fermentation and elevated levels may indicate dysbiosis. Elevated β-alanine can contribute to renal wasting of taurine given their unique relationship.
The breakdown and metabolism of β-alanine requires vitamin B6-dependent enzymes. With that, a functional need for vitamin B6 can contribute to elevations.
Lastly, there are very rare inborn errors of metabolism that can cause elevations of β-alanine:
There are several rare inborn errors of metabolism that can cause elevations of β-alanine, a non-essential amino acid. These metabolic disorders are typically caused by genetic mutations that result in the impairment or deficiency of enzymes involved in the metabolism of β-alanine or related pathways. Some examples of such rare inborn errors of metabolism that can cause elevated β-alanine levels include:
Hyper-beta-alaninemia: This is a rare autosomal recessive disorder caused by mutations in the BCKDHA gene, which encodes the alpha subunit of the branched-chain alpha-ketoacid dehydrogenase complex. This complex is involved in the breakdown of the branched-chain amino acids, including β-alanine. Mutations in BCKDHA can result in the accumulation of β-alanine in the blood and urine.
Dihydropyrimidinase deficiency: This is a rare autosomal recessive disorder caused by mutations in the DPYS gene, which encodes the enzyme dihydropyrimidinase. This enzyme is involved in the degradation of uracil and thymine, which are pyrimidine bases that are part of nucleic acids. Accumulation of dihydropyrimidinase substrates, including β-alanine, can occur in individuals with dihydropyrimidinase deficiency.
Pyrimidine degradation disorders: Disorders that involve defects in enzymes involved in the degradation of pyrimidine nucleotides, such as dihydropyrimidinase, can lead to elevated levels of β-alanine as a result of the accumulation of pyrimidine intermediates.
It's important to note that these inborn errors of metabolism are rare and typically diagnosed through specialized testing by metabolic specialists. Treatment for these disorders depends on the specific metabolic defect and may involve dietary modifications, enzyme replacement therapy, or other interventions tailored to the individual's needs. If you suspect that you or your child may have a rare inborn error of metabolism, it's important to consult a qualified healthcare professional for proper evaluation, diagnosis, and management.
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Further questions:
Can catabolism of diseased tissue lead to elevated levels of beta alanine (urine)?
Yes, the catabolism of diseased tissue, such as in certain metabolic disorders or diseases affecting muscle tissue, can potentially lead to elevated levels of beta alanine in urine. Beta alanine is a naturally occurring amino acid that is a component of proteins and is involved in various physiological processes in the body. However, under certain conditions, such as tissue breakdown or altered metabolism, beta alanine can be released into the bloodstream and eventually excreted in urine.
For example, in conditions where there is increased breakdown of muscle tissue, such as in rhabdomyolysis, a condition where muscle tissue breaks down and releases its contents into the bloodstream, including beta alanine, the levels of beta alanine in urine may be elevated. Similarly, in metabolic disorders such as urea cycle disorders or disorders of amino acid metabolism, where there are abnormalities in the breakdown of proteins or amino acids, beta alanine may be increased in urine as a result of altered metabolism.
It's important to note that elevated levels of beta alanine in urine alone may not be diagnostic of a specific disease or condition, and further evaluation and testing by a qualified healthcare professional would be necessary to determine the underlying cause of the elevated levels. Other factors, such as diet, medications, and kidney function, can also affect beta alanine levels in urine.
Can this be treated with Vitamin B6 to transfer amines?
Vitamin B6, also known as pyridoxine, is involved in various metabolic pathways in the body, including the metabolism of amino acids. It acts as a coenzyme, facilitating the transfer of amino groups (amines) during certain biochemical reactions. However, the use of vitamin B6 to specifically treat elevated levels of beta alanine in urine would depend on the underlying cause of the condition.
In some cases, if the elevated levels of beta alanine in urine are due to a metabolic disorder or a genetic condition affecting amino acid metabolism, supplementation with vitamin B6 or other vitamins and cofactors may be part of the treatment approach. For example, in certain types of urea cycle disorders, where there are deficiencies in enzymes involved in the breakdown of ammonia, vitamin B6 supplementation may be beneficial in reducing ammonia levels, which could indirectly affect beta alanine metabolism.
However, it's important to note that the use of vitamin B6 or any other treatment for a medical condition should be determined and monitored by a qualified healthcare professional. The treatment approach would depend on the specific underlying cause of the elevated beta alanine levels in urine, and a comprehensive evaluation, including a thorough medical history, physical examination, and appropriate diagnostic testing, would be needed to determine the most appropriate treatment plan. Self-treatment or supplementation without proper medical supervision can be potentially harmful and is not recommended.
Possible cause for food sensitivity reactions when beta alanine is combined with low taurine and high 3-methylhistidine, carnosine and/or anserine, due to impaired renal tubular resorption.
While there is limited evidence to suggest a direct link between food sensitivity reactions and the combination of beta alanine with low taurine and high 3-methylhistidine, carnosine, and/or anserine levels due to impaired renal tubular resorption, it is important to consider the broader context of individual health and other factors that may contribute to food sensitivities.
Food sensitivities, also known as food intolerances or adverse food reactions, refer to adverse reactions to certain foods that may involve the immune system or other mechanisms. They can manifest with a variety of symptoms, such as digestive issues, skin rash, respiratory symptoms, and more.
Beta alanine is an amino acid that is involved in the synthesis of carnosine, and it is found in high concentrations in skeletal muscles. Taurine is another amino acid that plays various roles in the body, including bile acid conjugation, osmoregulation, and antioxidant activity. 3-methylhistidine is a metabolite of histidine, an essential amino acid, and is commonly used as a marker for skeletal muscle breakdown. Carnosine and anserine are dipeptides composed of beta alanine and histidine, and they are also found in high concentrations in skeletal muscles.
Impaired renal tubular resorption refers to a condition where the kidneys are unable to effectively reabsorb certain substances from the urine back into the bloodstream, which can result in increased excretion of these substances in the urine.
While there is evidence that these amino acids and dipeptides may be affected by impaired renal tubular resorption in certain metabolic disorders or renal diseases, their direct relationship with food sensitivities is not well-established. Food sensitivities are complex and multifactorial, involving immune responses to specific food components, and the exact mechanisms underlying food sensitivities are not fully understood.
It's important to note that multiple factors, such as genetics, immune system responses, gut health, and overall diet, can contribute to food sensitivities. If you suspect you have food sensitivities or other health concerns, it's best to consult a qualified healthcare professional for proper evaluation, diagnosis, and management. They can provide personalized medical advice based on your individual health history and circumstances.
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1-Methylhistidine (Plasma), 3-Methylhistidine (Plasma), Alanine (Plasma), Alpha-Amino-n-butyric acid (Plasma), Alpha-Aminoadipic Acid (Plasma), Alpha-ANB/Leucine, Anserine (Plasma), Arginine (Plasma), Asparagine (Plasma), Aspartic Acid (Plasma), Beta-Alanine, Beta-Aminoisobutyric Acid (Plasma), Carnosine (Plasma), Citrulline, Cystathionine (Plasma), Cystine, Ethanolamine (Plasma), g-Aminobutyric Acid (Plasma), Glutamic Acid (Plasma), Glutamic Acid/Glutamine, Glutamine (Plasma), Glycine (Plasma), Histidine (Plasma), Homocysteine (Genova), Homocystine (Genova), Hydroxylysine (Genova), Hydroxyproline (Genova), Hydroxyproline/Proline (Genova), Isoleucine (Plasma), Leucine (Plasma), Lysine (Plasma), Methionine (Plasma), Ornithine (Genova), Phenylalanine (Plasma), Phenylalanine/Tyrosine (Genova), Phosphoethanolamine (Plasma), Phosphoserine (Plasma), Proline (Plasma), Sarcosine (Plasma), Serine (Plasma), Taurine (Plasma), Threonine (Plasma), Tryptophan (Plasma), Tryptophan/LNAA (Genova), Tyrosine (Plasma), Valine (Plasma)