Leucine 2.5g oral powder sachets
An essential branched-chain amino acid important for hemoglobin formation.
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Therapeutically similar medicines
Similarity is based on WHO Anatomical Therapeutic Chemical (ATC) classification and on a factual NHS dm+d therapeutic-grouping code prefix. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
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Codes for healthcare professionals and prescribing systems
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NHS UK identifiers
SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF code shown is the factual mapping value distributed by NHS Business Services Authority (NHSBSA) in the dm+d supplementary file under OGL v3.0; it is not affiliated with, nor licensed from, the publishers of the British National Formulary.
Active and completed clinical studies from ClinicalTrials.gov
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Academic studies and reviews for this medicine's active substance
Showing all 30 studies.
Reviews & meta-analyses: 8 · Randomised trials: 2 · 1982–2024
Showing all 30 studies, sorted by most relevant.
F. Martínez-Arnau, Rosa Fonfría-Vivas, O. Cauli
Nutrients, 2019
- Dietary Supplements
- Leucine
- Sarcopenia
OBJECTIVE: Treating sarcopenia remains a challenge, and nutritional interventions present promising approaches. We summarize the effects of leucine supplementation in treating older individuals with sarcopenia associated with aging or to specific disorders, and we focus on the effect of leucine supplementation on various sarcopenia criteria, e.g., muscular strength, lean mass, and physical performance. METHODS: A literature search for articles related to this topic was performed on the relevant databases, e.g., the PubMed/Medline, Embase, EBSCO, Cochrane, Lilacs, and Dialnet. The identified articles were reviewed according to Preferred Reporting Items for Systematic reviews and meta-analyses (PRISMA) guidelines. RESULTS: Of the 163 articles we consulted, 23 met our inclusion criteria, analysing the effect of leucine or leucine-enriched protein in the treatment of sarcopenia, and 13 of these studies were based on randomized and placebo-controlled trials (RCTs). In overall terms, the published results show that administration of leucine or leucine-enriched proteins (range 1.2-6 g leucine/day) is well-tolerated and significantly improves sarcopenia in elderly individuals, mainly by improving lean muscle-mass content and in this case most protocols also include vitamin D co-administration. The effect of muscular strength showed mix results, and the effect on physical performance has seldom been studied. For sarcopenia-associated with specific disorders, the most promising effects of leucine supplementation are reported for the rehabilitation of post-stroke patients and in those with liver cirrhosis. Further placebo-controlled trials will be necessary to determine the effects of leucine and to evaluate sarcopenia with the criteria recommended by official Working Groups, thereby limiting the variability of methodological issues for sarcopenia measurement across studies.
Abstract licence: CC BY
Gabriele Zaromskyte, Konstantinos Prokopidis, T. Ioannidis, et al.
Frontiers in Nutrition, 2021
Background: The “leucine trigger” hypothesis was originally conceived to explain the post-prandial regulation of muscle protein synthesis (MPS). This hypothesis implicates the magnitude (amplitude and rate) of post-prandial increase in blood leucine concentrations for regulation of the magnitude of MPS response to an ingested protein source. Recent evidence from experimental studies has challenged this theory, with reports of a disconnect between blood leucine concentration profiles and post-prandial rates of MPS in response to protein ingestion. Aim: The primary aim of this systematic review was to qualitatively evaluate the leucine trigger hypothesis to explain the post-prandial regulation of MPS in response to ingested protein at rest and post-exercise in young and older adults. We hypothesized that experimental support for the leucine trigger hypothesis will depend on age, exercise status (rest vs. post-exercise), and type of ingested protein (i.e., isolated proteins vs. protein-rich whole food sources). Methods: This qualitative systematic review extracted data from studies that combined measurements of post-prandial blood leucine concentrations and rates of MPS following ingested protein at rest and following exercise in young and older adults. Data relating to blood leucine concentration profiles and post-prandial MPS rates were extracted from all studies, and reported as providing sufficient or insufficient evidence for the leucine trigger hypothesis. Results: Overall, 16 of the 29 eligible studies provided sufficient evidence to support the leucine trigger hypothesis for explaining divergent post-prandial rates of MPS in response to different ingested protein sources. Of these 16 studies, 13 were conducted in older adults (eight of which conducted measurements post-exercise) and 14 studies included the administration of isolated proteins. Conclusion: This systematic review underscores the merits of the leucine trigger hypothesis for the explanation of the regulation of MPS. However, our data indicate that the leucine trigger hypothesis confers most application in regulating the post-prandial response of MPS to ingested proteins in older adults. Consistent with our hypothesis, we provide data to support the idea that the leucine trigger hypothesis is more relevant within the context of ingesting isolated protein sources rather than protein-rich whole foods. Future mechanistic studies are warranted to understand the complex series of modulatory factors beyond blood leucine concentration profiles within a food matrix that regulate post-prandial rates of MPS.
Abstract licence: CC BY
F. Martínez-Arnau, Rosa Fonfría-Vivas, C. Buigues, et al.
Nutrients, 2020
- Leucine
- Respiratory Muscles
- Muscle Strength
Treating sarcopenia in older individuals remains a challenge, and nutritional interventions present promising approaches in individuals that perform limited physical exercise. We assessed the efficacy of leucine administration to evaluate whether the regular intake of this essential amino acid can improve muscle mass, muscle strength and functional performance and respiratory muscle function in institutionalized older individuals. The study was a placebo-controlled, randomized, double-blind design in fifty participants aged 65 and over (ClinicalTrials.gov identifier NCT03831399). The participants were randomized to a parallel group intervention of 13 weeks’ duration with a daily intake of leucine (6 g/day) or placebo (lactose, 6 g/day). The primary outcome was to study the effect on sarcopenia and respiratory muscle function. The secondary outcomes were changes in the geriatric evaluation scales, such as cognitive function, functional impairment and nutritional assessments. We also evaluated whether leucine administration alters blood analytical parameters and inflammatory markers. Administration of leucine was well-tolerated and significantly improves some criteria of sarcopenia in elderly individuals such as functional performance measured by walking time (p = 0.011), and improved lean mass index. For respiratory muscle function, the leucine-treated group improved significantly (p = 0.026) in maximum static expiratory force compared to the placebo. No significant effects on functional impairment, cognitive function or nutritional assessment, inflammatory cytokines IL-6, TNF-alpha were observed after leucine administration compared to the placebo. The use of l-leucine supplementation can have some beneficial effects on sarcopenia and could be considered for the treatment of sarcopenia in older individuals.
Abstract licence: CC BY
M. Devries, C. McGlory, D. Bolster, et al.
The American journal of clinical nutrition, 2018
- Amino Acids
- Blood Glucose
- Body Weight
E. Ananieva, J. Powell, S. Hutson
Advances in nutrition, 2016
- Mechanistic Target of Rapamycin Complex 1
- Transaminases
- Immunity
B. Kobe, A. Kajava
Current opinion in structural biology, 2001
- Leucine
- Models, Molecular
- Protein Binding
B. Kobe, J. Deisenhofer
Trends in biochemical sciences, 1994
- Leucine
- Repetitive Sequences, Nucleic Acid
- Binding Sites
Chunzhao Zhao, Chunzhao Zhao, Omar Zayed, et al.
Proceedings of the National Academy of Sciences, 2018
- Stress, Physiological
- Plant Development
- Leucine-Rich Repeat Proteins
K. Anderson, Frank K. Huynh, Kelsey H. Fisher-Wellman, et al.
Cell metabolism, 2017
- Insulin Secretion
- Amidohydrolases
- Amino Acid Sequence
Shahab Ur Rehman, Rahmat Ali, Hao Zhang, et al.
Frontiers in Physiology, 2023
Leucine, a branched-chain amino acid, is essential in regulating animal growth and development. Recent research has uncovered the mechanisms underlying Leucine's anabolic effects on muscle and other tissues, including its ability to stimulate protein synthesis by activating the mTORC1 signaling pathway. The co-ingestion of carbohydrates and essential amino acids enhances Leucine's anabolic effects. Moreover, Leucine has been shown to benefit lipid metabolism, and insulin sensitivity, making it a promising strategy for preventing and treating metabolic diseases, including type 2 diabetes and obesity. While emerging evidence indicates that epigenetic mechanisms may mediate Leucine's effects on growth and development, more research is needed to elucidate its mechanisms of action fully. Specific studies have demonstrated that Leucine promotes muscle growth and metabolic health in animals and humans, making it a promising therapeutic agent. However, it is essential to note that Leucine supplementation may cause digestive issues or interact with certain medications, and More study is required to determine definitively optimal dosages. Therefore, it is important to understand how Leucine interacts with other nutrients, dietary factors, and lifestyle habits to maximize its benefits. Overall, Leucine's importance in human nutrition is far-reaching, and its potential to prevent muscle loss and enhance athletic performance warrants further investigation.
Abstract licence: CC BY
Sources: aggregated from Europe PMC (EMBL-EBI), OpenAlex, Crossref, PubMed and other open scholarly databases. Retracted articles are excluded. Study information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
Not available
Mechanism
This group of essential amino acids are identified as the branched-chain amino acids, BCAAs.
Food interactions
None known
Human targets
6 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Proteins and enzymes this drug interacts with in the body
PMID:25051973 PMID:32232361
It performs tRNA aminoacylation in a two-step reaction: Leu is initially activated by ATP to form a leucyl-adenylate (Leu-AMP) intermediate; then the leucyl moiety is transferred to the acceptor 3' end of the tRNA to yield leucyl-tRNA .
PMID:25051973
To improve the fidelity of catalytic reactions, it is also able to hydrolyze misactivated aminoacyl-adenylate intermediates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) PMID:25051973
PMID:17050531 PMID:25653144 PMID:8702755
May also function as a transporter of branched chain alpha-keto acids (By similarity)
Proteins that transport this drug across cell membranes
PMID:11827462 PMID:18337592 PMID:28754537
Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels .
PMID:18337592
Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa) .
PMID:11827462 PMID:28754537
Plays an important role in homeostasis of aromatic amino acids (By similarity)
PMID:16887882 PMID:18337592 PMID:20628049 PMID:23550058 PMID:26426690 PMID:27805744 PMID:31436139
Acts as an important mediator of thyroid hormone transport, especially T3, through the blood-brain barrier (Probable) PMID:28526555
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
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Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Leucine
Additional database identifiers
Drugs Product Database (DPD)
943
Drugs Product Database (DPD)
10239
Drugs Product Database (DPD)
751
ChemSpider
5880
BindingDB
50219348
PDB
LEU
ZINC
ZINC000003645145
HUGO Gene Nomenclature Committee (HGNC)
HGNC:17095
GenAtlas
LARS2
GeneCards
LARS2
GenBank Gene Database
D21851
GenBank Protein Database
40788954
UniProt Accession
SYLM_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:17558
GenAtlas
LCMT2
GeneCards
LCMT2
GenBank Gene Database
AB011119
GenBank Protein Database
40788285
UniProt Accession
TYW4_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:17557
GenAtlas
LCMT1
GeneCards
LCMT1
GenBank Gene Database
AF037601
GenBank Protein Database
6580758
UniProt Accession
LCMT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:6512
GenAtlas
LARS
GeneCards
LARS1
GenBank Gene Database
D84223
GenBank Protein Database
7804450
UniProt Accession
SYLC_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:977
GenAtlas
BCAT2
GeneCards
BCAT2
GenBank Gene Database
U68418
GenBank Protein Database
2342862
Guide to Pharmacology
2893
UniProt Accession
BCAT2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:976
GenAtlas
BCAT1
GeneCards
BCAT1
GenBank Gene Database
U21551
GenBank Protein Database
1036780
Guide to Pharmacology
3210
UniProt Accession
BCAT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:17027
GeneCards
SLC16A10
GenBank Gene Database
AB057445
GenBank Protein Database
18640047
UniProt Accession
MOT10_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:10923
GenAtlas
SLC16A2
GeneCards
SLC16A2
GenBank Gene Database
U05321
GenBank Protein Database
458255
UniProt Accession
MOT8_HUMAN
DrugBank citations
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Structured knowledge from the free knowledge base
Linked open data from Wikidata (Q106345666), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication.