BCAAs and anti-aging -
It provides structural support, strength, and elasticity to these tissues, making it crucial for optimal health and function. BCAAs, consisting of leucine, isoleucine, and valine, are essential amino acids that cannot be produced by the body and must be obtained through diet or supplementation.
BCAAs play a vital role in muscle protein synthesis, muscle recovery, and energy production during exercise. Muscle Recovery and Repair: Collagen, rich in glycine and proline, provides the building blocks for the synthesis of new collagen fibers, supporting the repair and recovery of muscles and connective tissues.
BCAAs, particularly leucine, stimulate muscle protein synthesis, enhancing muscle recovery and growth. Together, collagen and BCAAs create an optimal environment for muscle repair and rejuvenation.
Joint Health and Function: Collagen is a fundamental component of joints, providing strength and elasticity to cartilage. BCAAs support the synthesis of collagen and other connective tissues, helping to maintain joint health and flexibility.
By combining collagen and BCAAs, individuals can nourish their joints and promote long-term joint function and mobility. Exercise Performance and Endurance: BCAAs are known for their ability to reduce exercise-induced fatigue and improve endurance.
By promoting energy production and reducing muscle breakdown during intense exercise, BCAAs can support enhanced exercise performance. Collagen, with its supportive role in muscle recovery, complements the effects of BCAAs, helping athletes push their limits and recover more efficiently.
Skin Health and Anti-Aging Benefits: Collagen is often associated with its benefits for skin health, promoting elasticity, hydration, and reducing the appearance of wrinkles. BCAAs, with their role in muscle preservation, can help maintain a toned and youthful physique.
The combination of collagen and BCAAs can provide comprehensive anti-aging benefits for both skin and body. Overall Well-being: Collagen and BCAAs both contribute to overall health and well-being.
Collagen supports gut health, immune function, and promotes healthy hair and nails. BCAAs, in addition to their muscle benefits, aid in reducing exercise-induced muscle soreness and support immune function.
Together, they offer a holistic approach to optimizing health and vitality. Collagen and BCAAs form a powerful duo that complements and enhances each other's effects. Collagen supports muscle recovery, joint health, and skin elasticity, while BCAAs promote muscle protein synthesis, exercise performance, and endurance.
Incorporating both collagen and BCAAs into your routine can provide a comprehensive approach to supporting your fitness goals, promoting overall well-being, and unlocking your full potential.
Remember, consult with a healthcare professional or registered dietitian to determine the optimal dosage and usage of collagen and BCAAs based on your individual needs and goals. Embrace the synergy of collagen and BCAAs, and experience the transformative effects they can have on your health and fitness journey.
Le Couteur, D. Branched chain amino acids, cardiometabolic risk factors and outcomes in older men: the Concord Health and Ageing in Men Project. The journals of gerontology. Hoogendijk, E. Frailty: implications for clinical practice and public health.
Article PubMed Google Scholar. De Lepeleire, J. Frailty: an emerging concept for general practice. Article Google Scholar. Rockwood, K. A comparison of two approaches to measuring frailty in elderly people.
Hubbard, R. Sex Differences in Frailty. Wolfson, R. Sestrin2 is a leucine sensor for the mTORC1 pathway. aab Article ADS CAS PubMed Google Scholar. Mansfeld, J. Branched-chain amino acid catabolism is a conserved regulator of physiological ageing.
Article ADS CAS PubMed PubMed Central Google Scholar. Budanov, A. p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. Shah, S. Association of a peripheral blood metabolic profile with coronary artery disease and risk of subsequent cardiovascular events.
Article CAS PubMed Google Scholar. Lotta, L. Genetic Predisposition to an Impaired Metabolism of the Branched-Chain Amino Acids and Risk of Type 2 Diabetes: A Mendelian Randomisation Analysis.
Bloomgarden, Z. Diabetes and branched-chain amino acids: What is the link? Katagiri, R. Association between plasma concentrations of branched-chain amino acids and adipokines in Japanese adults without diabetes. Alvers, A. Autophagy and amino acid homeostasis are required for chronological longevity in Saccharomyces cerevisiae.
x Article PubMed PubMed Central Google Scholar. Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice.
Juricic, P. Branched-Chain Amino Acids Have Equivalent Effects to Other Essential Amino Acids on Lifespan and Aging-Related Traits in Drosophila. Sahin, E. Telomere dysfunction induces metabolic and mitochondrial compromise.
Dent, E. Frailty index from routine laboratory measurements correlates with leukocyte telomere length. Araujo Carvalho, A.
Telomere length and frailty in older adults-A systematic review and meta-analysis. Sun, L. Trans-ethnical shift of the risk genotype in the CETP IV with longevity: a Chinese case-control study and meta-analysis.
Franzke, B. Super DNAging-New insights into DNA integrity, genome stability and telomeres in the oldest old. Mutation research. Ubaida-Mohien, C. Discovery proteomics in aging human skeletal muscle finds change in spliceosome, immunity, proteostasis and mitochondria.
Sakuma, K. Current understanding of sarcopenia: possible candidates modulating muscle mass. Kimball, S. Signaling pathways and molecular mechanisms through which branched-chain amino acids mediate translational control of protein synthesis.
Cawthon, R. Telomere measurement by quantitative PCR. e47 Lai, T. Comparison of telomere length measurement methods. Philosophical transactions of the Royal Society of London. Lapham, K.
Automated Assay of Telomere Length Measurement and Informatics for , Subjects in the Genetic Epidemiology Research on Adult Health and Aging GERA Cohort. Yang, R. Association of branched-chain amino acids with coronary artery disease: A matched-pair case-control study.
Rapid and precise measurement of serum branched-chain and aromatic amino acids by isotope dilution liquid chromatography tandem mass spectrometry. Mitnitski, A. Accumulation of deficits as a proxy measure of aging. Yashin, A. Cumulative index of elderly disorders and its dynamic contribution to mortality and longevity.
Download references. This work was supported by the National Scientific Foundation of P. Thanks to all the participants involved in the study. Peking University Fifth School of Clinical Medicine, Beijing, , China. The MOH Key Laboratory of Geriatrics, Beijing Hospital, National Center of Gerontology, Beijing, , China.
Department of Neurology, JiangBin Hospital, Nanning, Guangxi, , China. Department of Cardiothoracic Surgery, Guangxi Maternal and Child Health Hospital, Nanning, Guangxi, , China. You can also search for this author in PubMed Google Scholar. designed research; Y.
and Z. conducted research; Y. and Q. analyzed data; Y. wrote manuscript; L. had primary responsibility for final content. All authors read and approved the final manuscript. Correspondence to Liang Sun. Open Access This article is licensed under a Creative Commons Attribution 4. Reprints and permissions.
Zhang, Y. Serum branched-chain amino acids are associated with leukocyte telomere length and frailty based on residents from Guangxi longevity county. Sci Rep 10 , Again, the role of mTOR in CR is tissue specific.
CR reduces mTOR signaling in liver [ 71 ] but increases it in WAT and heart [ 72 ]. Further, the CR-mediated increase of mitochondrial function in different tissues [ 8 ] is not consistent with reduced mTOR signaling. In addition, recent evidence indicates that mTOR signaling is down- or up-regulated depending of age and the type of CR regimen [ 73 ].
All in all, the role of mTOR in CR mechanisms is complex and not yet conclusively clarified [ 74 ]. With this in mind, more work needs to be done to address the possible contribution of mTOR in BCAAem prolongevity effects. Why does the BCAAem promote mitochondrial biogenesis in metabolically active tissues and what is the relationship between this effect and the CR-induced changes in mitochondrial function?
Conclusive answers are not available yet, but a sound hypothesis can be put forward. First, amino acids are important precursors of TCA cycle components Fig. Secondly, amino acid catabolism leads to production of ammonia, which is metabolized via the urea cycle, whose first two steps occurr in the mitochondrial matrix Fig.
Thus, the amino acid supplementation could induce mitochondrial biogenesis to promote catabolism of amino acid themselves. Interestingly, Nakagawa et al. Accordingly, Hallows et al. These findings suggest that the amino acid-induced mitochondrial biogenesis might be functional to amino acid catabolism and that amino acids might be, either directly or indirectly, related to the effects of CR on survival of mammals.
Figure 1. Amino acids are degraded to compounds that can be metabolized to CO 2 and H 2 O, or used in gluconeogenesis. The standard amino acids are degraded to one among the seven metabolic intermediates pyruvate, α-ketoglutarate, succinyl-CoA, fumarate, oxaloacetate, acetyl-CoA or acetoacetate.
Thus, amino acids may be divided into two groups, on the basis of their catabolic pathways: 1 gluconeogenic amino acids, which are catabolized to pyruvate, α-ketoglutarate, succinyl-CoA, fumarate or oxaloacetate, and are glucose precursors; 2 ketogenic amino acids, which are catabolized to acetyl-CoA or acetoacetate, and, thus, may be transformed into fatty acids or ketone bodies.
Some amino acids are precursors both of carbohydrates and ketone bodies. Because mammals have no metabolic pathway which allows a net transformation of acetyl-CoA or acetoacetate to gluconeogenic precursors, no net synthesis of carbohydrates is possible from lysine and leucine, exclusively ketogenic amino acids.
BCAAs, branched-chain amino acids. Figure 2. Catabolism of branched-chain amino acids. Starvation and exercise stimulate protein breakdown, thereby increasing the concentrations of branched-chain amino acids BCAAs in adipose and muscle cells.
The BCAAs are transaminated in muscle mitochondria by branched-chain aminotransferase BCAT , and branched-chain α-keto acids BCKAs, especially α-keto acid from leucine inhibit branched-chain α-keto acid dehydrogenase kinase, resulting in elevation of the active state of the rate limiting enzyme branched-chain α-keto acid dehydrogenase complex BCKDH.
Recent results indicate a novel mechanism for regulation of BCAA oxidation in adipose tissue, i. changes in the expression of BCAA enzymes, in contrast to altered BCKDH phosphorylation, which is the major mechanism regulating BCAA oxidation in muscle and liver [ ]. Ala, alanine; α-KG, α-ketoglutarate; Glu, glutamate; Gln, glutamine; IB-CoA, isobutyryl-coenzyme A; IV-CoA, isovaleryl-coenzyme A; MB-CoA, α-methylbutyryl-coenzyme A; R-CoA, acyl-coenzyme A; TCA, tricarboxylic acid.
For decades, dietary supplementation with amino acids has been proposed in various physiological or pathological conditions.
Based on the recent progress in our understanding of the BCAA cell signaling and in vivo metabolism, and on accumulating experimental results, the concept that dietary BCAA supplementation might have health effects is now experiencing a major revival see [ 75 ] for review.
The effects of BCAA intake have been investigated in a number of disease models, including obesity and metabolic disorders, liver disease, impaired immunity, muscle atrophy, cancer, and a variety of injury postoperative, trauma, burn, and sepsis [ 75 ].
Here we will briefly revise the most recent developments of this topic. First of all, BCAAs appear to have unique obesity-related effects. BCAAs, and in particular leucine, increase fat leptin secretion [ 76 ], decrease food intake and body weight via mTOR signaling [ 77 ], and improve muscle glucose uptake and whole body glucose metabolism [ 78 ].
To explore loss of catabolic capacity as a potential contributor to the obesity-related rises in BCAAs, She et al. They found tissue-specific alterations in BCAA catabolic enzymes, involving a decline of BCKDH E1α in liver and adipose tissue, but not in muscle, possibly contributing to the rise in plasma BCAAs in obesity.
In a separate series of experiments, the same investigators generated mice in which the gene encoding the BCAT2 isozyme was disrupted [ 79 ]. They found that rises in plasma BCAAs were associated with improvements in glucose tolerance and resistance to diet-induced obesity in these animals.
The authors proposed that increased protein synthesis and degradation would contribute directly to increased energy expenditure in mice lacking peripheral BCAA metabolism. These findings suggest that the increased BCAA levels in obese animals might be compensatory to obesogenic stimuli.
Actually, controversy exists about the effects of increasing dietary leucine on insulin sensitivity. For example, Zhang and colleagues have demonstrated that an increased leucine dietary intake improves the whole-body glucose metabolism in mice maintained on a high-fat diet [ 80 ].
By contrast, in a recent study, leucine deprivation was observed to increase whole-body insulin sensitivity [ 81 ]. Again, leucine deprivation improved insulin sensitivity under insulin-resistant conditions [ 81 ].
Noteworthy, Noguchi et al. This dietary amino acid manipulation improved glucose tolerance, decreased lipogenesis and prevented hepatic steatosis in diet-induced obese mice, and was suggested as a novel preventive and therapeutic approach for non-alcoholic fatty liver disease.
Accordingly, in a recent study, rats orally administered an amino acid mixture containing cysteine, methionine, valine, isoleucine and different concentrations of leucine together with a high-glucose solution, have shown an improved glucose tolerance as compared to non-supplemented animals [ 83 ].
Overall, these results would suggest that specific mixtures of amino acids, rather than a single amino acid supplement, may be more efficacious in lowering the blood glucose response to a glucose challenge.
A promising area of preclinical research is regarding the effects of BCAAs on skeletal muscle atrophy. We observed that BCAAem intake preserves muscle fiber size and improved physical endurance and motor coordination in middle-aged mice [ 12 ].
Accordingly, an amino acid mixture with BCAAem composition has been found to improve sarcopenia, i. Correspondingly, other groups have recently reported that BCAAs decrease protein breakdown and protect against dexamethasone-induced soleus muscle atrophy in rats [ 86 ].
BCAAem-mediated improvement of muscle functional capacity was further enhanced by exercise training [ 12 ]. Exercise promotes longevity and is the best intervention to alleviate and reverse sarcopenia and frailty in the elderly [ 87 ].
Our results suggest that the BCAAem could meet the need for a safe PGC-1α inducer in sarcopenia treatment [ 87 ] and a valid substitute for dietary supplementation with antioxidants in active elderly people.
The BCAAs leucine and valine have been also reported to prevent muscle atrophy in mice bearing a cachexia-inducing tumor [ 89 ].
Given the possible benefits of BCAAs in cancer patients, it would be of relevance to determine their effects on neoplastic cell growth. Dietary amino acids, incluning BCAAs, have been used in cancer models with mixed results [ 90 - 92 ]. Anyway, convincing data demonstrate that BCAA treatment does not directly potentiate neoplastic cell growth and may actually diminish neoplastic cell proliferation at supraphysiological concentrations [ 93 ].
Further investigation is needed to examine the effects of amino acid mixtures with different BCAA composition on normal and tumor cell proliferation. Additional observations deal with the capability of the BCAAem formula to ameliorate myocardial dysfunction in diabetic rats [ 94 ] and to maintain the health of kidney in aged rats [ 95 ].
In particular, when administered orally at the beginning of rat senescence, BCAAem induces eNOS and vascular endothelial growth factor in the kidney, thus increasing vascularization and reducing kidney fibrosis.
Improved vascularization and increased collagen deposition and fibroblast proliferation seem also to be involved in the cutaneous wound healing obtained with topical application of BCAAs and other essential amino acids in aged rats [ 96 ]. Again, BCAAs compete for large, neutral amino acid transport at the blood-brain barrier and can influence brain neurotrasmitter synthesis [ 97 ].
Experimental studies show that BCAAs have favourable effects on cognitive functions. BCAA supplementation has been reported to improve cognitive performance in active dogs, with greater benefit to senior dogs [ 98 ].
BCAA transamination plays an essential role in the synthesis of glutamate and subsequently of GABA. Cole et al. Dietary delivery of BCAAs to brain-injured mice restored hippocampal BCAA levels, synaptic glutamate and GABA pools and net synaptic efficacy, and eradicated injury-induced cognitive impairment [ 99 ].
Emerging metabolomic technologies make it feasible to investigate the metabolic status of the whole human organism in high-throughput applications.
Newgard et al. By metabolic profiling, they identified a cluster of obesity-related changes in specific amino acids that was associated with insulin resistance. In particular, circulating levels of the BCAAs were higher in obese compared to lean subjects [ ].
Obesity was also associated with decreases in bioavailable IGF The authors suggested that, in the context of overnutrition and low IGF-1 levels, circulating BCAAs rise, leading to an overload of BCAA catabolism that contributes to insulin resistance in obese subjects. A more recent nested case-control study in the Framingham Offspring Study has investigated whether metabolite profiles could predict the development of type 2 diabetes [ ].
Fasting concentrations of BCAAs and of two aromatic amino acids, phenylalanine and tyrosine, were found elevated up to 12 years before the onset of diabetes in high risk subjects as compared to propensity-matched control subjects.
The strongest risk of future diabetes was associated to a combination of three amino acids, namely isoleucine, phenylalanine and tyrosine. In a more heterogeneous study sample, obtained by looking at a random set of controls from the Framingham cohort having lower baseline body mass index and fasting glucose values compared to the case-control sample , the relative risk associated with elevated amino acids, though still significant, was attenuated [ ].
The authors recognize that contrasting data exist on BCAA effects on glucose homeostasis and that further investigation is necessary to assess whether amino acids may be markers or effectors of insulin resistance. On the other hand, sparse studies in wrestlers and in obese subjects have shown that BCAA supplementation exerts beneficial effects on body weight and body fat [ ].
This high-quality study demonsrated that a higher BCAA intake is associated with a lower prevalence of being overweight or obese in middle-aged individuals from East Asian and Western countries [ ]. In this line, Solerte et al. studied the effects of a balanced amino acid formula corresponding to the BCAAem in a long-term randomized study of elderly subjects with type 2 diabetes and found improved metabolic control i.
BCAAs and anti-aging show that BCAAs may increase muscle growth, reduce soreness and anti-agkng, prevent muscle anti-aginy, and support liver health. Immune-boosting lifestyle are also BCAAs and anti-aging in xnd variety of food sources, Holistic slimming pills meat, eggs, and dairy products. There are 20 different amino acids that make up the thousands of different proteins in the human body. Nine of the 20 are considered essential amino acidsmeaning they cannot be made by your body and must be obtained through your diet. Of the nine essential amino acids, three are considered branched-chain amino acids BCAAs : leucineisoleucine, and valine. Thank you Holistic slimming pills Athletic performance strategies BCAAs and anti-aging. You are using a browser an with limited support for CSS. To BCAAAs the best experience, we recommend Holistic slimming pills use a more up to date browser or turn antj-aging compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. Branched-chain amino acids BCAAs and telomere length are biologically associated with healthy aging. However, the association between them and their interaction on frailty remain unclear in humans. Here, a cross-sectional study based on residents from Guangxi longevity county was conducted to investigate the association of serum BCAAs, peripheral leukocyte telomere length LTL and frailty.
0 thoughts on “BCAAs and anti-aging”