Leucic Acid - NutraPedia
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Leucic Acid - Overview
Leucic acid, also known as alpha-hydroxy-isocaproic acid (HICA), is a metabolite of the branched-chain amino acid leucine. It has been studied for various potential health benefits, primarily in the context of exercise physiology and muscle metabolism.
1) Studied Conditions
Leucic acid has been studied in the context of:
- Enhancing muscle recovery
- Increasing muscle mass and strength
- Reducing muscle soreness after exercise
- Improving overall exercise performance
2) Effectiveness in Treating Conditions
The effectiveness of leucic acid in treating the above conditions remains somewhat unclear. Some studies suggest that it may help in reducing muscle breakdown and improving recovery times, but the evidence is not definitive. More research is needed to establish its efficacy conclusively.
3) Health Benefits
Potential health benefits of leucic acid include:
- Supporting muscle recovery
- Possibly reducing the extent of muscle damage
- May enhance muscle protein synthesis
- Could contribute to better body composition when combined with resistance training
4) Downsides
While leucic acid is considered safe for most people, potential downsides may include:
- Unpredictable effects on blood sugar levels
- Interactions with certain medications
- Gastrointestinal discomfort in some individuals
- Lack of extensive research on long-term safety and side effects
5) Impact on Genetic Variations
There is limited research on whether leucic acid is particularly beneficial or harmful for specific genetic variations. Metabolic responses to supplements like leucic acid can vary between individuals, possibly due to genetic factors, but targeted studies are required to draw any meaningful conclusions.
Leucic Acid Metabolism Study Summary
A study focusing on the metabolism of the amino acids valine and leucine was conducted on four healthy young men. These subjects maintained a protein-rich diet before receiving an infusion of isotopically labeled valine or leucine. Stable plasma levels of these amino acids were achieved within two hours.
The metabolism rates for valine and leucine were found to be proportional to their content in body protein. Notably, leucine was metabolized at a higher rate than valine. The study also established significant rates of transamination and deamination for both amino acids, with leucine transamination being favored.
Additionally, the leucine analog L-alpha-hydroxyisocaproate was identified to have similar effects on protein degradation as leucine itself, suggesting a complex regulation of hepatic protein degradation by amino acids, influenced by hormones such as insulin and glucagon.
The study concluded that the metabolism of branched-chain amino acids and their derivatives in humans changes significantly post-meal and during prolonged fasting. Moreover, despite a thermodynamic balance favoring the formation of alpha-hydroxy analogues of these acids, their conversion from keto acids is slow and does not reach equilibrium in the body.
This summary highlights the metabolism of leucine and its impact on protein degradation, providing insights into the regulation of amino acid metabolism under different nutritional states.
References:
- Regulation of valine metabolism in man: a stable isotope study
- l-Hydroxy acid oxidase
- Overexpression of Lactobacillus casei D-hydroxyisocaproic acid dehydrogenase in cheddar cheese
- 2-Hydroxyisocaproic acid (HICA): a new potential topical antibacterial agent
- Multiphasic control of hepatic protein degradation by regulatory amino acids. General features and hormonal modulation
- Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle?
- Alpha-keto and alpha-hydroxy branched-chain acid interrelationships in normal humans
- Branched-chain alpha-keto acids isolated as oxime derivatives: relationship to the corresponding hydroxy acids and amino acids in maple syrup urine disease
- Hydroxy acid metabolites of branched-chain amino acids in amniotic fluid
- Stable isotope dilution assay for branched chain alpha-hydroxy-and alpha-ketoacids: serum concentrations for normal children
- Cloning, sequencing and expression in Escherichia coli of the D-2-hydroxyisocaproate dehydrogenase gene of Lactobacillus casei
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