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Condition and Nutrition Assessment Table
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Amino Acids 40 - Plasma
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Overview
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Clinician Info
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CPT Codes
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Kit Instructions
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Sample Reports
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Interpretive Guide
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References
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Amino Acid testing—Assessing the Body's Fundamental Building Blocks
 
Additional Resources:
The Amino Acids 40 Plasma Profile
In addition to pinpointing problems in amino acid absorption and determining essential amino acid imbalances, the plasma amino acid 40 test includes evaluation of limiting, branched chain, and essential and non-essential amino acids. It also identifies several functional categories, such as neuroendocrine, vascular, collagen status and detoxification, along with five calculated ratios, and identifies vitamin and mineral insufficiencies.
Plasma Amino Acids
Fasting plasma levels represent a homeostatic balance between supply and utilization of amino acids making this specimen option ideal for repeated assessments to monitor progress of treatment. Collecting a fasting plasma specimen from a patient removes recent dietary intake effects. The following factors can effect changes over time in plasma:
- Chronic dietary intake
- Digestive efficiency
- Hepatic uptake
- Skeletal muscle's ability to maintain transamination
Why is amino acid testing important?
Amino acids, known as the "building blocks" of proteins are found in every tissue of the body. They play a major role in nearly every chemical process that affects both physical and mental function including the formation of ligaments, tendons, bones, and antibodies, as well as regulation of enzymes and blood transport proteins. Twenty different amino acids are used to synthesize proteins.
The human body can synthesize all of the amino acids necessary to build proteins except for ten called the "essential amino acids". These ten must be included in the diet or supplemented to be in adequate supplies. Failure to obtain enough of even 1 of the 10 essential amino acids has serious health implications and can result in degradation of the body's proteins. Muscle and other protein structures may be dismantled to obtain the one amino acid that is needed.
Amino acids have more diverse functions than any other nutrient group, including:
- Gastrointestinal function
- Cellular energy production
- Detoxification
- Neurotransmitter metabolism
Muscle catabolism
Collagen
Nutritional markers
Vascular function
Conditions Associated with Amino Acid Changes in Plasma:
- Cardiovascular disease
- Depression
- Anxiety
- Insomnia
- Chronic Fatigue Syndrome
- Multiple sclerosis
- Rheumatoid arthritis
- Epilepsy
- Congestive heart failure
- Impotence/Erectile pain syndromes
Multiple chemical sensitivities
Detoxification disorders
Autism Spectrum Disorders
Alzhiemer’s Disease
Hypothyroidism
Arrhythmias
Hypertension
ADD/ADHD
Infertility
Customized Amino Acid Formula
A formula for a customized amino acid blend, based on your patient's specific test results, is provided with every plasma amino acid test result. These customized amino acid formulations provide appropriate amounts of essential and conditionally essential amino acids, delivered in a balanced ratio to offset the risk of imbalance sometimes seen with the use of single amino acid supplements. This blend can be made by many compounding pharmacies.
| Test name: |
0010 - Amino Acids - 40 analytes
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| Description: |
Fasting plasma levels of amino acids represent homeostatic balance between supply and utilization of these critical building blocks. Problems in amino acid metabolism are revealed by the amino acids and metabolites that are reported in categories according to function. Amino acid analysis helps with determination of amino acid imbalances, evaluation of functional vitamin and mineral deficiencies, and diagnosis of metabolic disorders. A formula for a custom amino acid blend is provided with every plasma amino acid test result. This blend can be made by any compounding pharmacy. |
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| Method: |
Reversed Phase UHPLC Method |
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| Turnaround time: |
7-14 days, 10 days average |
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Analytes:
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1-Methylhistidine 3-Methylhistidine Alanine Alpha-Aminoadipic Acid Alpha-Amino-N-Butyric Acid Anserine Arginine Asparagine Aspartic Acid Beta-Alanine Beta-Aminoisobutyric Acid Carnosine Citrulline Cystahionine Cystine Ethanolamine Gamma-Aminobutyric Acid Glutamic Acid Glutamine Glycine Histidine Homocystine Hydroxylysine Isoleucine Leucine Lysine Methionine Ornithine Phenylalanine Phosphoethanolamine Phosphoserine Proline Sarcosine Serine Taurine Threonine Tryptophan Tyrosine Valine
Ratios
Phenylalanine/Tyrosine Glutamic Acid/Glutamine Hydroxyproline/Proline Alpha-ANB/Leucine Tryptophan/LNAA (Large Neutral Amino Acids)
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| 82139 |
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Amino acids, 6 or more, quantitative |
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ReferencesAmino Acids - Plasma
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Role of meal carbohydrate content for the imbalance of plasma amino acids in patients with liver cirrhosis.
Schulte-Frohlinde E, Wagenpfeil S, Willis J, Lersch C, Eckel F, Schmid R, Schusdziarra V. J Gastroenterol Hepatol. 2007 Aug;22(8):1241-8.
L-arginine and cardiovascular system. Cylwik D, Mogielnicki A, Buczko W. Pharmacol Rep. Jan-Feb 2005;57(1):14-22.
Plasma concentrations of excitatory amino acids serine, glycine, taurine and histidine in major depression.
Altamura C, Maes M, Dai J, Meltzer HY. Eur Neuropsychopharmacol. 1995;5 Suppl:71-75.
Tryptophan depletion, serotonin, and depression: where do we stand?
Neumeister A. Psychopharmacol Bull. 2003;37(4):99-115.
Pharmacogenetics and individual variation in the range of amino acid adequacy: the biological aspects.
Caldwell J. J Nutr. Jun 2004;134(6 Suppl):1600S-1604S; discussion 1630S-1632S, 1667S-1672S.
Metabolomics and its potential for assessment of adequacy and safety of amino acid intake.
Noguchi Y, Sakai R, Kimura T. J Nutr. Jun 2003;133(6 Suppl 1):2097S-2100S.
Effect of cortisol on energy expenditure and amino acid metabolism in humans.
Brillon DJ, Zheng B, Campbell RG, Matthews DE. Am J Physiol. 1995;268(3 Pt 1):E501-513.
Protein requirements and supplementation in strength sports.
Phillips SM. Nutrition. Jul-Aug 2004;20(7-8):689-695.
Serum levels of excitatory amino acids, serine, glycine, histidine, threonine, taurine, alanine and
arginine in treatment-resistant depression: modulation by treatment with antidepressants and prediction of clinical responsivity.
Maes M, Verkerk R, Vandoolaeghe E, Lin A, Scharpe S. Acta Psychiatr Scand. Apr 1998;97(4):302-308.
Plasma amino acid concentrations in patients with amnestic mild cognitive impairment or Alzheimer disease.
Ravaglia G, Forti P, Maioli F, et al. Am J Clin Nutr. Aug 2004;80(2):483-488.
Contribution of dietary protein and inorganic sulfur to urinary sulfate: toward a biomarker of inorganic sulfur intake.
Magee EA, Curno R, Edmond LM, Cummings JH. Am J Clin Nutr. Jul 2004;80(1):137-142.
Macronutrient intakes as determinants of dietary protein and amino acid adequacy.
Millward DJ. J Nutr. Jun 2004;134(6 Suppl):1588S-1596S.
Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: the effect of N- acetyl-cysteine.
Kinscherf R, Hack V, Fischbach T, et al. J Mol Med. 1996;74(7):393-400.
Co-existence of GABA and Glu in the hippocampal granule cells: implications for epilepsy.
Gutierrez R, Heinemann U. Curr Top Med Chem. 2006;6(10):975-978.
Response of alanine metabolism in humans to manipulation of dietary protein and energy intakes.
Yang RD, Matthews DE, Bier DM, Wen ZM, Young VR. Am J Physiol. Jan 1986;250(1 Pt 1):E39-46.
Ethanolamine and phosphoethanolamine inhibit mitochondrial function in vitro: implications for mitochondrial dysfunction hypothesis in depression and bipolar disorder.
Modica-Napolitano JS, Renshaw PF. Biol Psychiatry. Feb 1 2004;55(3):273-277.
Plasma proline and leucine kinetics: response to 4 wk with proline-free diets in young adults.
Hiramatsu T, Cortiella J, Marchini JS, Chapman TE, Young VR. Am J Clin Nutr. 1994;60(2):207-215.
Gender-related differences in carnosine, anserine and lysine content of murine skeletal muscle.
Penafiel R, Ruzafa C, Monserrat F, Cremades A. Amino Acids. Feb 2004;26(1):53-58.
Clinical usefulness of urinary 3-methylhistidine excretion in indicating muscle protein breakdown.
Elia M, Carter A, Bacon S, Winearls CG, Smith R. Br Med J (Clin Res Ed). 1981;282(6261):351-354.
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