Leucine. Medical search

DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). The DNA-binding residues are located in the bifurcated region of the Y.

A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.

An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.

Amino acids which have a branched carbon chain.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.

A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.

A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain AMINO ACIDS to 2-oxoglutarate.

An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE, forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. This enzyme was formerly listed as EC 4.1.3.12.

An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.

Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The rate dynamics in chemical or physical systems.

The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis.

An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.

A family of transcription factors found primarily in PLANTS that bind to the G-box DNA sequence CACGTG or to a consensus sequence CANNTG.

Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure.

The process by which two molecules of the same chemical composition form a condensation product or polymer.

A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.

An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

The amounts of various substances in food needed by an organism to sustain healthy life.

A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.

Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

A disease due to deficiency of NIACIN, a B-complex vitamin, or its precursor TRYPTOPHAN. It is characterized by scaly DERMATITIS which is often associated with DIARRHEA and DEMENTIA (the three D's).

Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.

The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.

Established cell cultures that have the potential to propagate indefinitely.

An essential amino acid. It is often added to animal feed.

A LEUCINE and DNA-binding protein that is found primarily in BACTERIA and ARCHAEA. It regulates GENETIC TRANSCRIPTION involved in METABOLISM of AMINO ACIDS in response to the increased concentration of LEUCINE.

A sulfur-containing essential L-amino acid that is important in many body functions.

A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.

An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

A zinc-containing sialoglycoprotein that is used to study aminopeptidase activity in the pathogenesis of hypertension. EC 3.4.11.3.

A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).

Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.

A family of transcription factors that contain regions rich in basic residues, LEUCINE ZIPPER domains, and HELIX-LOOP-HELIX MOTIFS.

Proteins prepared by recombinant DNA technology.

A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

Proteins found in any species of bacterium.

A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.

Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.

The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.

A serine threonine kinase that controls a wide range of growth-related cellular processes. The protein is referred to as the target of RAPAMYCIN due to the discovery that SIROLIMUS (commonly known as rapamycin) forms an inhibitory complex with TACROLIMUS BINDING PROTEIN 1A that blocks the action of its enzymatic activity.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.

Transport proteins that carry specific substances in the blood or across cell membranes.

A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

A flavoprotein enzyme that catalyzes the formation of acetolactate from 2 moles of PYRUVATE in the biosynthesis of VALINE and the formation of acetohydroxybutyrate from pyruvate and alpha-ketobutyrate in the biosynthesis of ISOLEUCINE. This enzyme was formerly listed as EC 4.1.3.18.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Cellular DNA-binding proteins encoded by the c-jun genes (GENES, JUN). They are involved in growth-related transcriptional control. There appear to be three distinct functions: dimerization (with c-fos), DNA-binding, and transcriptional activation. Oncogenic transformation can take place by constitutive expression of c-jun.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.

Cellular proteins and protein complexes that transport amino acids across biological membranes.

A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

A family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.

Elements of limited time intervals, contributing to particular results or situations.

Transforming protein coded by jun oncogenes (GENES, JUN). This is a gag-onc fusion protein of about 65 kDa derived from avian sarcoma virus. v-jun lacks a negative regulatory domain that regulates transcription in c-jun.

A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

A class of amino acids characterized by a closed ring structure.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.

Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.

The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.

Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.

An essential amino acid that is physiologically active in the L-form.

The sum of the weight of all the atoms in a molecule.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

Oxidoreductases that are specific for KETONES.

A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.

Proteins found in any species of fungus.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

Products in capsule, tablet or liquid form that provide dietary ingredients, and that are intended to be taken by mouth to increase the intake of nutrients. Dietary supplements can include macronutrients, such as proteins, carbohydrates, and fats; and/or MICRONUTRIENTS, such as VITAMINS; MINERALS; and PHYTOCHEMICALS.

The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

Agents that improve the ability to carry out activities such as athletics, mental endurance, work, and resistance to stress. The substances can include PRESCRIPTION DRUGS; DIETARY SUPPLEMENTS; phytochemicals; and ILLICIT DRUGS.

Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.

Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.

Regular course of eating and drinking adopted by a person or animal.

A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.

A triglyceride that is used as an antifungal agent.

A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis.

Glucose in blood.

A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis.

Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.

Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Recurring supersecondary structures characterized by 20 amino acids folding into two alpha helices connected by a non-helical "loop" segment. They are found in many sequence-specific DNA-BINDING PROTEINS and in CALCIUM-BINDING PROTEINS.

A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.

Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.

Abstaining from all food.

CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.

A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.

Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

Calculation of the energy expenditure in the form of heat production of the whole body or individual organs based on respiratory gas exchange.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).

Contractile tissue that produces movement in animals.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

The relationship between the dose of an administered drug and the response of the organism to the drug.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.

A family of ribosomal protein S6 kinases that are considered the major physiological kinases for RIBOSOMAL PROTEIN S6. Unlike RIBOSOMAL PROTEIN S6 KINASES, 90KDa the proteins in this family are sensitive to the inhibitory effects of RAPAMYCIN and contain a single kinase domain. They are referred to as 70kDa proteins, however ALTERNATIVE SPLICING of mRNAs for proteins in this class also results in 85kDa variants being formed.

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.

Amino acids containing an aromatic side chain.

A family of neurotransmitter transporter proteins that facilitate NEUROTRANSMITTER reuptake into PRESYNAPTIC TERMINALS. They may play a role in regulating the intensity and duration of neurotransmission.

DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.

The creation of an amine. It can be produced by the addition of an amino group to an organic compound or reduction of a nitro group.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.

Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).

A pyridoxal-phosphate protein that catalyzes the deamination of THREONINE to 2-ketobutyrate and AMMONIA. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for ISOLEUCINE biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. This enzyme was formerly listed as EC 4.2.1.16.

A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.

Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).

A genus of ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES.

A microanalytical technique combining mass spectrometry and gas chromatography for the qualitative as well as quantitative determinations of compounds.

The long-term (minutes to hours) administration of a fluid into the vein through venipuncture, either by letting the fluid flow by gravity or by pumping it.

A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.

Biochemical identification of mutational changes in a nucleotide sequence.

An essential amino acid that is required for the production of HISTAMINE.

Peptides composed of two amino acid units.

The thermodynamic interaction between a substance and WATER.

The administering of nutrients for assimilation and utilization by a patient who cannot maintain adequate nutrition by enteral feeding alone. Nutrients are administered by a route other than the alimentary canal (e.g., intravenously, subcutaneously).

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.

The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.

A transplantable carcinoma of the rat that originally appeared spontaneously in the mammary gland of a pregnant albino rat, and which now resembles a carcinoma in young transplants and a sarcoma in older transplants. (Stedman, 25th ed)

A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.

Radioactive substances added in minute amounts to the reacting elements or compounds in a chemical process and traced through the process by appropriate detection methods, e.g., Geiger counter. Compounds containing tracers are often said to be tagged or labeled. (Hawley's Condensed Chemical Dictionary, 12th ed)

Cellular DNA-binding proteins encoded by the c-fos genes (GENES, FOS). They are involved in growth-related transcriptional control. c-fos combines with c-jun (PROTO-ONCOGENE PROTEINS C-JUN) to form a c-fos/c-jun heterodimer (TRANSCRIPTION FACTOR AP-1) that binds to the TRE (TPA-responsive element) in promoters of certain genes.

The chemical reactions involved in the production and utilization of various forms of energy in cells.

Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.

A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.

Mitogen-activated protein kinase kinase kinases (MAPKKKs) are serine-threonine protein kinases that initiate protein kinase signaling cascades. They phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES; (MAPKKs) which in turn phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs).

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511)

EXOPEPTIDASES that specifically act on dipeptides. EC 3.4.13.

Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.

A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.

An enzyme that catalyzes the transfer of methyl groups from S-adenosylmethionine to free carboxyl groups of a protein molecule forming methyl esters. EC 2.1.1.-.

The process of cleaving a chemical compound by the addition of a molecule of water.

Techniques for labeling a substance with a stable or radioactive isotope. It is not used for articles involving labeled substances unless the methods of labeling are substantively discussed. Tracers that may be labeled include chemical substances, cells, or microorganisms.

Lengthy and continuous deprivation of food. (Stedman, 25th ed)

Control of ketogenesis from amino acids. IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine. (1/5969)

In vitro and in vivo studies were made on the tissue specificity of oxidation of the ketogenic amino acids, leucine, tyrosine, and lysine. In in vitro studies the abilities of slices of various tissues of rats to form 14CO2 from 14C-amino acids were examined. With liver, but not kidney slices, addition of alpha-ketoglutarate was required for the maximum activities with these amino acids. Among the various tissues tested, kidney had the highest activity for lysine oxidation, followed by liver; other tissues showed very low activity. Kidney also had the highest activity for leucine oxidation, followed by diaphragm; liver and adipose tissue had lower activities. Liver had the highest activity for tyrosine oxidation, but kidney also showed considerable activity; other tissues had negligible activity. In in vivo studies the blood flow through the liver or kidney was stopped by ligation of the blood vessels. Then labeled amino acids were injected and recovery of radioactivity in respiratory 14CO2 was measured. In contrast to results with slices, no difference was found in the respiratory 14CO2 when the renal blood vessels were or were not ligated. On the contrary ligation of the hepatic vessels suppressed the oxidations of lysine and tyrosine completely and that of leucine partially. Thus in vivo, lysine and tyrosine seem to be metabolized mainly in the liver, whereas leucine is metabolized mostly in extrahepatic tissues and partly in liver. Use of tissue slices seems to be of only limited value in elucidating the metabolisms of these amino acids. (+info)

A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (2/5969)

The enzyme acetolactate decarboxylase (Ald) plays a key role in the regulation of the alpha-acetolactate pool in both pyruvate catabolism and the biosynthesis of the branched-chain amino acids, isoleucine, leucine, and valine (ILV). This dual role of Ald, due to allosteric activation by leucine, was used as a strategy for the isolation of Ald-deficient mutants of Lactococcus lactis subsp. lactis biovar diacetylactis. Such mutants can be selected as leucine-resistant mutants in ILV- or IV-prototrophic strains. Most dairy lactococcus strains are auxotrophic for the three amino acids. Therefore, the plasmid pMC004 containing the ilv genes (encoding the enzymes involved in the biosynthesis of IV) of L. lactis NCDO2118 was constructed. Introduction of pMC004 into ILV-auxotrophic dairy strains resulted in an isoleucine-prototrophic phenotype. By plating the strains on a chemically defined medium supplemented with leucine but not valine and isoleucine, spontaneous leucine-resistant mutants were obtained. These mutants were screened by Western blotting with Ald-specific antibodies for the presence of Ald. Selected mutants lacking Ald were subsequently cured of pMC004. Except for a defect in the expression of Ald, the resulting strain, MC010, was identical to the wild-type strain, as shown by Southern blotting and DNA fingerprinting. The mutation resulting in the lack of Ald in MC010 occurred spontaneously, and the strain does not contain foreign DNA; thus, it can be regarded as food grade. Nevertheless, its application in dairy products depends on the regulation of genetically modified organisms. These results establish a strategy to select spontaneous Ald-deficient mutants from transformable L. lactis strains. (+info)

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase. (3/5969)

The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Deltahmo1 and Deltafpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions. (+info)

Nuclear export of LIM-kinase 1, mediated by two leucine-rich nuclear-export signals within the PDZ domain. (4/5969)

LIM-kinase 1 (LIMK1) is a serine/threonine kinase that phosphorylates cofilin and regulates actin-filament dynamics. LIMK1, which contains two LIM domains and a single PDZ domain, localizes predominantly in the cytoplasm, but its mutant, deleted with the PDZ domain, localizes mainly in the nucleus, thereby indicating that the PDZ domain plays a role in the cytoplasmic localization of LIMK1. Here we provide evidence that the PDZ domain of LIMK1 contains two functional leucine-rich nuclear-export signals (NESs). The PDZ domain of LIMK1 fused with glutathione S-transferase (GST-PDZ), when injected into the nucleus, was rapidly excluded from the nucleus, but its mutant with replacements of conserved hydrophobic residues in two putative NESs by alanines remained in the nucleus. The nuclear export of GST-PDZ was sensitive to leptomycin B (LMB), a specific inhibitor of nuclear export mediated by leucine-rich NESs. Malfunctional mutation of two NESs or LMB treatment prevented the nuclear export of full-length LIMK1 and induced its nuclear accumulation. These results suggest that the predominant localization of LIMK1 in the cytoplasm is supported by two NESs within the PDZ domain and that LIMK1 normally shuttles between the cytoplasm and the nucleus. We also provide evidence that a short basic cluster sequence within the protein-kinase domain is involved in the nuclear import of LIMK1. (+info)

Ion binding and permeation through the lepidopteran amino acid transporter KAAT1 expressed in Xenopus oocytes. (5/5969)

1. The transient and steady-state currents induced by voltage jumps in Xenopus oocytes expressing the lepidopteran amino acid co-transporter KAAT1 have been investigated by two-electrode voltage clamp. 2. KAAT1-expressing oocytes exhibited membrane currents larger than controls even in the absence of amino acid substrate (uncoupled current). The selectivity order of this uncoupled current was Li+ > Na+ approximately Rb+ approximately K+ > Cs+; in contrast, the permeability order in non-injected oocytes was Rb+ > K+ > Cs+ > Na+ > Li+. 3. KAAT1-expressing oocytes gave rise to 'pre-steady-state currents' in the absence of amino acid. The characteristics of the charge movement differed according to the bathing ion: the curves in K+ were strongly shifted (> 100 mV) towards more negative potentials compared with those in Na+, while in tetramethylammonium (TMA+) no charge movement was detected. 4. The charge-voltage (Q-V) relationship in Na+ could be fitted by a Boltzmann equation having V of -69 +/- 1 mV and slope factor of 26 +/- 1 mV; lowering the Na+ concentrations shifted the Q-V relationship to more negative potentials; the curves could be described by a generalized Hill equation with a coefficient of 1.6, suggesting two binding sites. The maximal movable charge (Qmax) in Na+, 3 days after injection, was in the range 2.5-10 nC. 5. Addition of the transported substrate leucine increased the steady-state carrier current, the increase being larger in high K+ compared with high Na+ solution; in these conditions the charge movement disappeared. 6. Applying Eyring rate theory, the energy profile of the transporter in the absence of organic substrate included a very high external energy barrier (25.8 RT units) followed by a rather deep well (1.8 RT units). (+info)

A surrogate measure of whole body leucine transport across the cell membrane. (6/5969)

Based on a mass-balance model, a surrogate measure of the whole body leucine transport into and out of cells under steady-state conditions was calculated as u/DeltaTTR, where u is the infusion rate of (stable label) leucine tracer and DeltaTTR is the difference between the tracer-to-tracee ratio of extracellular and intracellular leucine. The approach was evaluated in ten healthy subjects [8 males and 2 females; age, 31 +/- 9 (SD) yr; body mass index, 24.0 +/- 1.6 kg/m2] who received a primed (7.58 micromol/kg) constant intravenous infusion (7.58 micromol. kg-1. h-1) of L-[1-13C]leucine over 180 min (7 subjects) or 240 min (3 subjects). Five subjects were studied on two occasions >/=1 wk apart to assess reproducibility. Blood samples taken during the last 30 min of the leucine infusion were used to determine plasma leucine concentration (129 +/- 35 micromol/l), TTR of leucine (9.0 +/- 1.5%), and TTR of alpha-ketoisocaproic acid (6.7 +/- 0.8%). The latter TTR was taken as the measure of the free intracellular leucine TTR. The whole body inward and outward transport was 6.66 +/- 3.82 micromol. kg-1. min-1; the rate of leucine appearance due to proteolysis was 1.93 +/- 0.24 micromol. kg-1. min-1. A positive linear relationship between the inward transport and plasma leucine was observed (P < 0.01), indicating the presence of the mass effect of leucine on its own transport. The transport was highly variable between subjects (between-subject coefficient of variation 57%) but reproducible (within-subject coefficient of variation 17%). We conclude that reproducible estimates of whole body transport of leucine across the cell membrane can be obtained under steady-state conditions with existing experimental and analytical procedures. (+info)

Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis. (7/5969)

We report a middle-aged woman with a novel transthyretin (TTR) variant, Leu12Pro. She had extensive amyloid deposition in the leptomeninges and liver as well as the involvement of the heart and peripheral nervous system which characterizes familial amyloid polyneuropathy caused by variant TTR. Clinical features attributed to her leptomeningeal amyloid included radiculopathy, central hypoventilation, recurrent subarachnoid haemorrhage, depression, seizures and periods of decreased consciousness. MRI showed a marked enhancement throughout her meninges and ependyma, and TTR amyloid deposition was confirmed by meningeal biopsy. The simultaneous presence of extensive visceral amyloid and clinically significant deposits affecting both the peripheral and central nervous system extends the spectrum of amyloid-related disease associated with TTR mutations. The unusual association of severe peripheral neuropathy with symptoms of leptomeningeal amyloid indicates that leptomeningeal amyloidosis should be considered part of the syndrome of TTR-related familial amyloid polyneuropathy. (+info)

Leucine metabolism in preterm infants receiving parenteral nutrition with medium-chain compared with long-chain triacylglycerol emulsions. (8/5969)

BACKGROUND: Although medium-chain triacylglycerols (MCTs) may be utilized more efficiently than long-chain triacylglycerols (LCTs), their effect on protein metabolism remains controversial. OBJECTIVE: The aim of the study was to compare the effects of mixed MCT-LCT and pure LCT emulsions on leucine metabolism in preterm infants. DESIGN: Fourteen preterm [gestational age: 30+/-1 wk; birth weight: 1409+/-78 g (x +/- SE)] neonates were randomly assigned to receive, from the first day of life, either a 50:50 MCT-LCT (mixed MCT group; n = 7) or an LCT (LCT group; n = 7) lipid emulsion as part of an isonitrogenous, isoenergetic total parenteral nutrition program. On the fourth day, infants received intravenous feeding providing 3 g lipid, 15 g glucose, and 3 g amino acids kg(-1) x d(-1) and underwent 1) indirect calorimetry and 2) a primed, 2-h infusion of H13CO3Na to assess the recovery of 13C in breath, immediately followed by 3) a 3-h infusion of L-[1-13C]leucine. RESULTS: The respiratory quotient tended to be slightly but not significantly higher in the mixed MCT than in the LCT group (0.96+/-0.06 compared with 0.93+/-0.03). We did not detect a significant difference between the mixed MCT and LCT groups with regard to release of leucine from protein breakdown (B; 309+/-40 compared with 257+/-46 micromol x kg(-1) x h(-1)) and nonoxidative leucine disposal (NOLD; 296+/-36 compared with 285+/-49 micromol x kg(-1) x h(-1)). In contrast, leucine oxidation was greater in the mixed MCT than in the LCT group (113+/-10 compared with 67+/-10 micromol x kg(-1) x h(-1); P = 0.007). Net leucine balance (NOLD - B) was less positive in the mixed MCT than in the LCT group (-14+/-9 compared with 28+/-10 micromol x kg(-1) x h(-1); P = 0.011). CONCLUSION: Mixed MCTs may not be as effective as LCT-containing emulsions in promoting protein accretion in parenterally fed preterm neonates. (+info)

Pellagra is characterized by three main symptoms: diarrhea, dermatitis (skin rashes), and dementia or confusion. The disease can be acute or chronic, depending on the severity of the nutritional deficiency.

The disease was first identified in the early 1900s, and it is named after the Italian physician who first described it, Cesare Pellagri. Pellagra was initially thought to be caused by a bacterial or fungal infection, but it was later discovered that the cause was actually a lack of niacin in the diet.

Treatment of pellagra typically involves supplementation with niacin, and the disease is now relatively rare in developed countries where access to a balanced diet is widespread. However, it can still be found in some developing countries where malnutrition is common.

Causes of Hyperammonemia:

1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.

Symptoms of Hyperammonemia:

1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting

Diagnosis of Hyperammonemia:

1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.

Treatment of Hyperammonemia:

1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.

Complications of Hyperammonemia:

1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.

In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.

Without more information about the context in which this term is being used, it is difficult to provide a clear definition or interpretation of its meaning. However, based on the name "Walker" and the fact that it is followed by a number (256), it is possible that this term may refer to a specific type of cancer or tumor that has been identified in a patient with the last name Walker.

It's important to note that the diagnosis and treatment of cancer can be complex and highly individualized, and any medical information or terminology should only be interpreted and applied by qualified healthcare professionals who have access to the relevant clinical context and patient information.

Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.

Types of Starvation:

There are several types of starvation, each with different causes and effects. These include:

1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.

Effects of Starvation on the Body:

Starvation can have severe effects on the body, including:

1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.

It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.

Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.

There are several ways to measure body weight, including:

1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.

It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.

The infection occurs when these larvae enter the host's body through contaminated food or water, or through contact with infected feces. Once inside the host's body, the larvae migrate to the small intestine, where they attach to the mucosal surface and begin to feed on the host's blood and tissues.

The symptoms of trichostrongylosis can vary depending on the severity of the infection and the species of Trichostrongylus involved. Some common symptoms include:

* Diarrhea
* Vomiting
* Abdominal pain
* Weight loss
* Anemia
* Fever

If left untreated, trichostrongylosis can lead to serious complications such as intestinal obstruction, hemorrhage, and damage to the host's immune system. Treatment typically involves the use of anthelmintic drugs to eliminate the parasites from the host's body.

Prevention is key in avoiding trichostrongylosis, and this can be achieved through:

* Proper sanitation and hygiene practices
* Avoiding contact with infected animals or their feces
* Using clean water and feed
* Implementing parasite control measures such as deworming programs

It is important for veterinarians to be aware of the risk of trichostrongylosis in the animals they treat, and to take appropriate steps to prevent and diagnose this condition.

Causes and risk factors:

1. Poverty and lack of access to nutritious food
2. Poor sanitation and hygiene
3. Inadequate healthcare and nutritional education
4. Conflict and displacement
5. Chronic illnesses such as HIV/AIDS and tuberculosis

Symptoms:

1. Wasting and stunting of children
2. Poor appetite and weight loss
3. Fatigue, weakness, and lethargy
4. Increased susceptibility to infections
5. Poor wound healing and skin problems

Complications:

1. Stunted growth and development
2. Weakened immune system
3. Increased risk of infections and diseases such as diarrhea, pneumonia, and malaria
4. Poor cognitive development and reduced educational attainment
5. Increased risk of mortality

Diagnosis:

1. Clinical evaluation of symptoms and physical examination
2. Anthropometric measurements such as height and weight
3. Laboratory tests to assess nutrient deficiencies and infections
4. Dietary assessment to determine food intake and nutrient adequacy

Treatment and prevention:

1. Providing access to nutrient-dense foods, particularly protein-rich foods such as meat, poultry, fish, beans, and dairy products
2. Addressing underlying causes such as poverty and poor sanitation
3. Implementing nutritional education programs to promote healthy eating habits
4. Providing micronutrient supplements and fortified foods
5. Addressing infectious diseases and providing appropriate medical care

In conclusion, protein-energy malnutrition is a serious condition that affects millions of people worldwide, particularly in developing countries. It can have severe consequences on physical growth, cognitive development, and overall health. Early diagnosis and treatment are crucial to prevent long-term health problems and improve quality of life. Addressing underlying causes such as poverty and poor sanitation is also essential to prevent the condition from occurring in the first place.

There are several factors that can contribute to protein deficiency, including:

1. Poor diet: A diet that is lacking in protein-rich foods, such as meat, poultry, fish, eggs, dairy products, legumes, and nuts, can lead to protein deficiency.
2. Vegetarian or vegan diet: People who follow a vegetarian or vegan diet may be at risk of protein deficiency if they do not consume enough protein-rich plant-based foods.
3. Malabsorption: Certain medical conditions, such as celiac disease, can lead to malabsorption of proteins and other nutrients.
4. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher protein requirement to support the growth and development of their baby.
5. Chronic diseases: Certain chronic diseases, such as kidney disease, can lead to protein deficiency.

Protein deficiency can cause a range of symptoms, including:

1. Fatigue and weakness
2. Muscle wasting and loss of muscle mass
3. Poor wound healing
4. Hair loss
5. Difficulty concentrating and making decisions
6. Mood changes, such as irritability and depression
7. Increased risk of infections

If protein deficiency is not treated, it can lead to a range of complications, including:

1. Stunted growth in children
2. Weakened immune system
3. Poor wound healing
4. Increased risk of infections
5. Nutrient deficiencies
6. Reproductive problems
7. Cardiovascular disease

Treatment for protein deficiency typically involves increasing the intake of protein-rich foods or supplements. The goal is to provide enough protein to support growth and development, as well as overall health and well-being. In some cases, medication may be prescribed to help manage symptoms or address underlying conditions.

In addition to dietary changes, other treatments for protein deficiency may include:

1. Nutritional supplements: Protein supplements can be taken to increase protein intake.
2. Vitamin and mineral supplements: If the protein deficiency is due to a lack of certain vitamins or minerals, supplements may be prescribed.
3. Hormone replacement therapy: In cases where protein deficiency is caused by hormonal imbalances, hormone replacement therapy may be recommended.
4. Medications: Certain medications, such as antidepressants or anti-anxiety drugs, may be prescribed to help manage symptoms of protein deficiency.
5. Addressing underlying conditions: If the protein deficiency is due to an underlying condition, such as kidney disease, treatment will focus on managing that condition.

Preventing protein deficiency is important for maintaining overall health and well-being. Here are some tips for preventing protein deficiency:

1. Eat a balanced diet: Include a variety of protein-rich foods in your diet, such as lean meats, fish, eggs, dairy products, legumes, and nuts.
2. Consult with a healthcare professional: If you are vegetarian or vegan, or if you have certain medical conditions, consult with a healthcare professional to ensure you are getting enough protein.
3. Consider supplements: If you are unable to get enough protein through your diet alone, consider taking protein supplements.
4. Monitor your symptoms: Pay attention to any symptoms of protein deficiency and seek medical attention if they persist or worsen over time.

Overall, preventing protein deficiency is important for maintaining overall health and well-being. If you suspect you or someone you know may have a protein deficiency, it is important to seek medical attention as soon as possible. With proper diagnosis and treatment, protein deficiency can be effectively managed and symptoms can improve.

There are several types of inborn errors of amino acid metabolism, including:

1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.

It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.

There are several types of hypertrophy, including:

1. Muscle hypertrophy: The enlargement of muscle fibers due to increased protein synthesis and cell growth, often seen in individuals who engage in resistance training exercises.
2. Cardiac hypertrophy: The enlargement of the heart due to an increase in cardiac workload, often seen in individuals with high blood pressure or other cardiovascular conditions.
3. Adipose tissue hypertrophy: The excessive growth of fat cells, often seen in individuals who are obese or have insulin resistance.
4. Neurological hypertrophy: The enlargement of neural structures such as brain or spinal cord due to an increase in the number of neurons or glial cells, often seen in individuals with neurodegenerative diseases such as Alzheimer's or Parkinson's.
5. Hepatic hypertrophy: The enlargement of the liver due to an increase in the number of liver cells, often seen in individuals with liver disease or cirrhosis.
6. Renal hypertrophy: The enlargement of the kidneys due to an increase in blood flow and filtration, often seen in individuals with kidney disease or hypertension.
7. Ovarian hypertrophy: The enlargement of the ovaries due to an increase in the number of follicles or hormonal imbalances, often seen in individuals with polycystic ovary syndrome (PCOS).

Hypertrophy can be diagnosed through various medical tests such as imaging studies (e.g., CT scans, MRI), biopsies, and blood tests. Treatment options for hypertrophy depend on the underlying cause and may include medications, lifestyle changes, and surgery.

In conclusion, hypertrophy is a growth or enlargement of cells, tissues, or organs in response to an excessive stimulus. It can occur in various parts of the body, including the brain, liver, kidneys, heart, muscles, and ovaries. Understanding the underlying causes and diagnosis of hypertrophy is crucial for effective treatment and management of related health conditions.

Both L-leucine and D-leucine protect mice against epileptic seizures. D-leucine also terminates seizures in mice after the ... Leucines, the isomers and derivatives of leucine Leucine zipper, a common motif in transcription factor proteins This reaction ... The activation of mTOR by leucine is mediated through Rag GTPases, leucine binding to leucyl-tRNA synthetase, leucine binding ... and urinary leucine excretion were observed with leucine intakes >500 mg · kg−1 · d−1. The oxidation of l-[1-13C]-leucine ...

https://en.wikipedia.org/wiki/Leucine

... (beta-leucine) is a beta amino acid and positional isomer of L-leucine which is naturally produced in humans via the ... Metabolism of L-leucine Archived 22 March 2018 at the Wayback Machine "Leucine metabolism". BRENDA. Technische Universität ... is initially catalyzed by leucine aminomutase, producing β-leucine, which is subsequently metabolized into β-ketoisocaproate (β ... A small fraction of L-leucine metabolism - less than 5% in all tissues except the testes where it accounts for about 33% - ...

https://en.wikipedia.org/wiki/Β-Leucine

... is created by the dimerization of two specific alpha helix monomers bound to DNA. The leucine zipper is formed ... A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. They were first described by ... Leucine zippers are a dimerization motif of the bZIP (Basic-region leucine zipper) class of eukaryotic transcription factors. ... The ZIP domain is found in the alpha-helix of each monomer, and contains leucines, or leucine-like amino acids. These amino ...

https://en.wikipedia.org/wiki/Leucine_zipper

Other names in common use include L-leucine aminotransferase, leucine 2-oxoglutarate transaminase, leucine aminotransferase, ... In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction L-leucine + 2-oxoglutarate ... This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine ... Leucine (methionine) transaminase of rat liver mitochondria". Biochim. Biophys. Acta. 445 (3): 622-31. doi:10.1016/0005-2744(76 ...

https://en.wikipedia.org/wiki/Leucine_transaminase

In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction L-leucine + H2O + NAD+ ... This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. As of ... Other names in common use include L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, and LeuDH. ... Sanwal BD, Zink MW (1961). "L-Leucine dehydrogenase of Bacillus cereus". Arch. Biochem. Biophys. 94 (3): 430-435. doi:10.1016/ ...

https://en.wikipedia.org/wiki/Leucine_dehydrogenase

... s are frequently involved in the formation of protein-protein interactions. Leucine-rich repeat motifs have ... Leucine zipper Kobe B, Deisenhofer J (October 1994). "The leucine-rich repeat: a versatile binding motif". Trends Biochem. Sci ... with the absence of the beta-sheets present in other leucine-rich repeats. Leucine-rich repeats are often flanked by N-terminal ... A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20-30 ...

https://en.wikipedia.org/wiki/Leucine-rich_repeat

As mentioned in the introduction, l-photo-leucine is a synthetic derivative of the l-Leucine amino acid. l-photo-leucine is ... l-Photo-leucine is a synthetic derivative of the l-leucine amino acid that is used as its natural analog and is characterized ... l-Photo-leucine acquires its function after being exposed to UV light. This causes diazirine ring of l-photo-leucine to lose ... In the absence of the original amino acid (l-leucine) in an environment, l-photo-leucine is used just as its naturally ...

https://en.wikipedia.org/wiki/L-Photo-leucine

This box: view edit Except where noted otherwise, data relate to Standard temperature and pressure. Reliability of data general note. ^a ^b ^c ^d ^e CID 6106 from PubChem (PubChem ID (CID) not in Wikidata, Chemical data pages, Chemical data pages cleanup ...

https://en.wikipedia.org/wiki/Leucine_(data_page)

The Leucine operon leader is an RNA element found upstream of the first gene in the Leucine biosynthetic operon. The leader ... Page for Leucine operon leader at Rfam v t e (Articles needing additional references from April 2020, All articles needing ... This structure forms when the cell has an excess of leucine and ribosome movement over the leader transcript is not impeded. ... The leader also codes for very short peptide sequence that is rich in leucine amino acid. The terminator structure is ...

https://en.wikipedia.org/wiki/Leucine_operon_leader

... in this case leucine). The transport is not dependent on any other source of energy (for example, ATP). Leucine transporter, ... Bacterial Leucine Transporter imports leucine from the outside of the cell to the inside with the aid of two sodium ions. It is ... Leucine and alanine are the main amino acids that this protein brings across the membrane since it has a high affinity for ... Bacterial Leucine Transporter (LeuT) is a bundled twelve alpha helix protein which belongs to the family of transporters that ...

https://en.wikipedia.org/wiki/Bacterial_Leucine_Transporter

The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine ... N-acetyl-L-leucine Thus, the two substrates of this enzyme are acetyl-CoA and L-leucine, whereas its two products are CoA and N ... In enzymology, a leucine N-acetyltransferase (EC 2.3.1.66) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... Isolation and properties of an enzyme synthesizing acetyl-L-leucine". J. Antibiot. 33 (8): 857-862. doi:10.7164/antibiotics. ...

https://en.wikipedia.org/wiki/Leucine_N-acetyltransferase

... leucine-tRNA synthetase, and leucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and ... In enzymology, a leucine-tRNA ligase (EC 6.1.1.4) is an enzyme that catalyzes the chemical reaction ATP + L-leucine + tRNALeu ... The systematic name of this enzyme class is L-leucine:tRNALeu ligase (AMP-forming). Other names in common use include leucyl- ... L-leucine, and tRNA(Leu), whereas its 3 products are AMP, diphosphate, and L-leucyl-tRNA(Leu). This enzyme belongs to the ...

https://en.wikipedia.org/wiki/Leucine—tRNA_ligase

... is an enzyme that in humans is encoded by the LCMT1 gene. LCMT1 has been shown to interact ... "Entrez Gene: LCMT1 leucine carboxyl methyltransferase 1". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, ... Lee JA, Pallas DC (Oct 2007). "Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in ... "Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue". ...

https://en.wikipedia.org/wiki/Leucine_carboxyl_methyltransferase_1

... beta-leucine Hence, this enzyme is responsible for the conversion of L-leucine to β-leucine. This enzyme belongs to the family ... In enzymology, a leucine 2,3-aminomutase (EC 5.4.3.7) is an enzyme that catalyzes the chemical reaction (2S)-alpha-leucine ⇌ {\ ... Poston JM (1976). "Leucine 2,3-aminomutase, an enzyme of leucine catabolism". J. Biol. Chem. 251 (7): 1859-63. PMID 1270414. ... The systematic name of this enzyme class is (2S)-alpha-leucine 2,3-aminomutase. This enzyme participates in valine, leucine and ...

https://en.wikipedia.org/wiki/Leucine_2,3-aminomutase

Leucine responsive protein, or Lrp, is a global regulator protein, meaning that it regulates the biosynthesis of leucine, as ... Leucine-Responsive+Regulatory+Protein at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles ... de los Rios S, Perona JJ (March 2007). "Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a ... Baek, Chang-Ho; Wang, Shifeng; Roland, Kenneth L.; Curtiss, Roy (2009). "Leucine-Responsive Regulatory Protein (Lrp) Acts as a ...

https://en.wikipedia.org/wiki/Leucine-responsive_regulatory_protein

The leucines are primarily the four isomeric amino acids: leucine, isoleucine, tert-leucine (terleucine, pseudoleucine) and ... Leucine and isoleucine belong to the proteinogenic amino acids; the others are non-natural. Including the stereoisomers, six ... L-Photo-Leucine Jeremy M. Berg, John L. Tymoczko, Lubert Stryer: Biochemie. 6 Auflage, Spektrum Akademischer Verlag, Heidelberg ... further isomers could be added: D-leucine, D-isoleucine, L-alloisoleucine, D-alloisoleucine, D-tert-leucine and D-norleucine. ...

https://en.wikipedia.org/wiki/Leucines

... is a cell membrane expressed protein that in humans is encoded by the LRRC15 gene. located on ... "Entrez Gene: Leucine rich repeat containing 15". Gisby JS, Buang NB, Papadaki A, Clarke CL, Malik TH, Medjeral-Thomas N, ... Satoh K, Hata M, Yokota H (January 2002). "A novel member of the leucine-rich repeat superfamily induced in rat astrocytes by ... Cui J, Dean D, Wei R, Hornicek FJ, Ulmert D, Duan Z (September 2020). "Expression and Clinical Implications of Leucine-Rich ...

https://en.wikipedia.org/wiki/Leucine_rich_repeat_containing_15

... hypoglycemia leucine induced; and familial infantile hypoglycemia precipitated by leucine. "Leucine-sensitive hypoglycemia of ... "OMIM Entry - # 240800 - HYPOGLYCEMIA, LEUCINE-INDUCED; LIH". www.omim.org. Retrieved 27 October 2019. "Hypoglycemia, Leucine- ... Leucine-sensitive hypoglycemia of infancy is a type of metabolic disorder. It is inherited in an autosomal dominant fashion. It ...

https://en.wikipedia.org/wiki/Leucine-sensitive_hypoglycemia_of_infancy

... is a protein that in humans is encoded by the LRRC3 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Leucine rich repeat containing 3". Retrieved 2016-05-12. v t e (Articles with short description, Short description ...

https://en.wikipedia.org/wiki/Leucine_rich_repeat_containing_3

... is a protein that in humans is encoded by the LRRC61 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Leucine rich repeat containing 61". Retrieved 2017-01-16. v t e (Genes on human chromosome 7, All stub articles, ...

https://en.wikipedia.org/wiki/Leucine_rich_repeat_containing_61

... (EC 2.1.1.233, leucine carboxy methyltransferase-1, LCMT1) is an ... leucine methyl ester Methylates the C-terminal leucine of phosphatase 2A. De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens ... phosphatase+2A+protein)-leucine-carboxy+methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH ... Tsai ML, Cronin N, Djordjevic S (January 2011). "The structure of human leucine carboxyl methyltransferase 1 that regulates ...

https://en.wikipedia.org/wiki/(Phosphatase_2A_protein)-leucine-carboxy_methyltransferase

... (PEPR1 and PEPR2 in Arabidopsis thaliana and Xa21 in rice) are plant cell ... PEPR 1 is a receptor kinase with extra cellular leucine rich repeat motif and functions as a receptor for AtPEPs. In addition, ... Yamaguchi Y, Pearce G, Ryan CA (June 2006). "The cell surface leucine-rich repeat receptor for AtPep1, an endogenous peptide ... membrane localized Leucine-rich repeat (LRR) receptor kinase that play critical roles in plant innate immunity. Plants have ...

https://en.wikipedia.org/wiki/Leucine-rich_repeat_receptor_like_protein_kinase

... are, as their name indicates, transcription factors containing both ... leucine+zipper+transcription+factors at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles ... Basic helix-loop-helix and leucine zipper motifs. Examples include Microphthalmia-associated transcription factor and Sterol ...

https://en.wikipedia.org/wiki/Basic_helix-loop-helix_leucine_zipper_transcription_factors

... is a protein that in humans is encoded by the FBXL15 gene. GRCh38: Ensembl release 89 ... "Entrez Gene: F-box and leucine rich repeat protein 15". Retrieved 2018-03-21. v t e (Articles with short description, Short ...

https://en.wikipedia.org/wiki/F-box_and_leucine_rich_repeat_protein_15

The Leucine-Rich Repeat domain is found in three isoforms of LRRIQ1. LRRIQ1 contains 4 Leucine Rich Repeats (LRR). The LRR ... Leucine-rich repeats and IQ motif containing 1 is a protein that in humans is encoded by the LRRIQ1 gene. The protein is likely ... "LRRIQ1 leucine-rich repeats and IQ motif containing 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved ... "Entrez Gene: Leucine-rich repeats and IQ motif containing 1". Retrieved 2016-03-29. Hart, Gerald W.; Akimoto, Yoshihiro (2009- ...

https://en.wikipedia.org/wiki/Leucine-rich_repeats_and_iq_motif_containing_1

... is a protein that in humans is encoded by the LRRD1 gene. GRCh38: Ensembl ... "Entrez Gene: Leucine-rich repeats and death domain containing 1". Retrieved 2016-02-22. v t e (Genes on human chromosome 7, ...

https://en.wikipedia.org/wiki/Leucine-rich_repeats_and_death_domain_containing_1

"Entrez Gene: BZW2 basic leucine zipper and W2 domains 2". "BZW2 basic leucine zipper and W2 domains 2 [Homo sapiens (human)] - ... Basic Leucine Zipper and W2 Domain-Containing Protein 2 is a protein that is encoded by the BZW2 gene. It is a eukaryotic ... It has been found to interact with SARS-CoV-2. BZW2 is known as Basic Leucine Zipper W2 Domain-Containing Protein 2, MST017, ... As described in the name, the protein contains a leucine-zipper motif. Four "L……" repeats are present in the beginning, giving ...

https://en.wikipedia.org/wiki/Basic_leucine_zipper_and_W2_domain-containing_protein_2

... is a protein that in humans is encoded by the ANP32A gene. It is ... Acidic leucine-rich nuclear phosphoprotein 32 family member A has been shown to interact with MAP1B, TAF1A and Protein SET. ... 1997). "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1". Nature. 389 (6654): 974-8. Bibcode: ... "Entrez Gene: ANP32A Acidic (leucine-rich) nuclear phosphoprotein 32 family, member A". Opal, Puneet; Garcia Jesus J; Propst ...

https://en.wikipedia.org/wiki/Acidic_leucine-rich_nuclear_phosphoprotein_32_family_member_A

... is a protein that in humans is encoded by the LRFN4 gene. ... "Entrez Gene: Leucine rich repeat and fibronectin type III domain containing 4". Retrieved 2016-10-17. Konakahara S, Saitou M, ... Fibronectin type III domain Leucine rich repeat GRCh38: Ensembl release 89: ENSG00000173621 - Ensembl, May 2017 GRCm38: Ensembl ...

https://en.wikipedia.org/wiki/Leucine_rich_repeat_and_fibronectin_type_iii_domain_containing_4

Treatment includes lowering leucine intake and a specialized diet to make up for the lack of leucine ingestion. CID 70 from ... are metabolic intermediates in the metabolic pathway for L-leucine. Leucine is an essential amino acid, and its degradation is ... "Leucine". Wilson, Jacob M.; Fitschen, Peter J.; Campbell, Bill; Wilson, Gabriel J.; Zanchi, Nelo; Taylor, Lem; Wilborn, Colin; ... HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB ...

https://en.wikipedia.org/wiki/Alpha-Ketoisocaproic_acid

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science. 2016;351(6268):53-8. doi:10.1126/science.aad2087. ... Sestrin2 is a leucine sensor for the mTORC1 pathway. Science. 2016;351(6268):43-8. doi:10.1126/science.aab2674. ...

https://www.broadinstitute.org/bibcite/keyword/3864

Leucine aminopeptidase is a type of protein called an enzyme. It is normally found in liver cells and cells of the small ... Leucine aminopeptidase is a type of protein called an enzyme. It is normally found in liver cells and cells of the small ...

https://medlineplus.gov/ency/article/003617.htm

Glucocorticoid-induced leucine zipper "quantifies" stressors and increases male susceptibility to PTSD Transl Psychiatry. 2019 ... This study focuses on PTSD markers in the glucocorticoid pathway, spotlighting glucocorticoid-induced leucine zipper (GILZ), a ...

https://pubmed.ncbi.nlm.nih.gov/31346158/

... *Formula: C15H29NO4 ...

https://webbook.nist.gov/cgi/inchi/InChI%3D1S/C15H29NO4/c1-6-8-9-10-20-14

leucine-rich repeat and calponin homology domain-containing protein 4. Names. leucine rich repeat neuronal 4. leucine-rich ... LRR_4; Leucine Rich repeats (2 copies). pfam13855. Location:138 → 194. LRR_8; Leucine rich repeat. ... LRR_4; Leucine Rich repeats (2 copies). pfam13855. Location:138 → 194. LRR_8; Leucine rich repeat. ... LRCH4 leucine rich repeats and calponin homology domain containing 4 [Homo sapie... LRCH4 leucine rich repeats and calponin ...

https://www.ncbi.nlm.nih.gov/gene/4034

L-leucine is one of the nine essential amino acids. Its called essential because our bodies need it to live and thrive, but ... What is L-Leucine?. L-leucine is one of the nine essential amino acids. Its called essential because our bodies need it to ... the L refers to naturally produced leucine, but if you find D-leucine, it means that it was produced in laboratory settings, ... What is L-Leucine. by John Staughton (BASc, BFA) last updated - March 19, 2020. ✐ Evidence Based. ...

https://www.organicfacts.net/l-leucine.html

View mouse Lrig3 Chr10:125802088-125851228 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression

https://www.informatics.jax.org/marker/MGI:2443955

Measures involving L-Leucine About. Data sets: Data set. Procedure. Whats in this data set. Panel. Sex. Age (weeks). Year. ...

https://phenome.jax.org/interventions/L-Leucine

Valine, leucine and isoleucine degradation (WP1451). Caenorhabditis elegans. Open in new tab ...

https://www.wikipathways.org/pathways/WP1451.html

Effects of N-Acetyl-L-Leucine on Niemann-Pick Disease Type C (NPC): A Phase III, Randomized, Placebo-controlled, Double-blind, ... N-Acetyl-L-Leucine (prohibited if not provided as IMP in the IB1001-301 trial) Yes for N-Acetyl-L-Leucine (prohibited if not ... Acetyl-Leucine (DL-, L-, D-) or derivatives Yes for Acetyl-Leucine (DL-, L-, D-) or derivatives exclusion criteria 2 ... N-Acetyl-DL-Leucine (e.g. Tanganil®) Yes for N-Acetyl-DL-Leucine (e.g. Tanganil®) exclusion criteria 17 ...

https://www.centerwatch.com/clinical-trials/listings/305055/effects-of-n-acetyl-l-leucine-on-niemann-pick-disease-type-c-npc-a-phase-iii-randomized-placebo-controlled-double-blind-crossover-study/?q=nasopharyngeal+carcinoma&query=nasopharyngeal%20carcinoma&rnk=2

L-Leucine Market Business Opportunities Current Trends Industry Forecast & Global Industry Analysis By 2031 ... L-Leucine is also available as a dietary supplement. The market for L-Leucine is growing due to the health benefits it provides ... What are the prospects for the L-Leucine Market?. What is the difference between performance characteristics of L-Leucine and ... This report focuses on the L-Leucine market during the 2031 evaluation period. This report also includes an L-Leucine market ...

https://www.einpresswire.com/article/600525282/l-leucine-market-size-share-analysis-will-experience-an-increase-in-growth-by-2031

... encoding a small protein with short leucine-rich-repeats by cDNA microarray analyses in the lamina joint and panicles of wild- ... encoding a small protein with short leucine-rich-repeats by cDNA microarray analyses in the lamina joint and panicles of wild- ... It encodes a small leucine rich repeat (LRR) protein possessing cell elongation activity. Sequentially, OsAP2 and OsWRKY24 are ... Oryza sativa BRASSINOSTEROID UPREGULATED1 LIKE1 Induces the Expression of a Gene Encoding a Small Leucine-Rich-Repeat Protein ...

https://www.frontiersin.org/articles/10.3389/fpls.2017.01253/full

Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat E L Delwart 1 , G Mosialos, T Gilmore ... Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat E L Delwart et al. AIDS Res Hum Retroviruses. 1990 Jun ... The BZLF1 protein of EBV has a coiled coil dimerisation domain without a heptad leucine repeat but with homology to the C/EBP ... Dimer-to-tetramer assembly of Lac repressor involves a leucine heptad repeat. Alberti S, Oehler S, von Wilcken-Bergmann B, ...

https://pubmed.ncbi.nlm.nih.gov/2364015

... neural retina leucine zipper (human). Find diseases associated with this biological target and compounds tested against it in ... neural retina-specific leucine zipper protein. Names. Maf-family bZIP transcription factor NRL. neural retinal-specific leucine ... NRL neural retina leucine zipper [Homo sapiens] NRL neural retina leucine zipper [Homo sapiens]. Gene ID:4901 ... neural retina leucine zipperprovided by HGNC. Primary source. HGNC:HGNC:8002 See related. Ensembl:ENSG00000129535 MIM:162080; ...

https://www.ncbi.nlm.nih.gov/gene/?term=4901

LEUCINE (UNII: GMW67QNF9C) (LEUCINE - UNII:GMW67QNF9C) LEUCINE. 8 [hp_X] in 1 mL. ... Label: VITAL SKIN HAIR NAILS- l-alanine, l-arginine, l-carnitine, cysteinum, l-glutamine, l-histidine, l-isoleucine, l-leucine ... l-alanine, l-arginine, l-carnitine, cysteinum, l-glutamine, l-histidine, l-isoleucine, l-leucine, l-lysine, l-methionine, l- ... VITAL SKIN HAIR NAILS- l-alanine, l-arginine, l-carnitine, cysteinum, l-glutamine, l-histidine, l-isoleucine, l-leucine, l- ...

https://dailymed.nlm.nih.gov/dailymed/drugInfo.cfm?setid=2fd28d08-ee4e-498d-907a-de311874c66b

Leucine is commonly known as the Anabolic Trigger. With Leucine flavorless powder you have the freedom to easily customize your ...

https://mansports.com/products/leucine-100-servings-40-off

Follow the link to learn about leucine, an essential branched-chain amino acid crucial to muscle development and protein ... What exactly is leucine?. Leucine (l-leucine) is a proteinogenic (protein-building) branched-chain amino acid (BCAA) that ... Foods rich in leucine. Most healthy adults will get all the leucine they need from a varied and balanced diet that includes the ... The effects of leucine. The role of leucine is widespread, so its best if we break down the amino acids abilities into ...

https://www.cibdol.com/uk/encyclopedia/what-is-leucine

Results 1 - 10 of 20 for ALANINE OR ARGININE OR CHLORIDE ION OR DEXTROSE OR GLYCINE OR HISTIDINE OR ISOLEUCINE OR LEUCINE OR ... subset of amino acids (including methionine, glutamic acid, alanine, serine, glycine, leucine, valine, threonine, and ... Jewish descent; this mutation replaces the amino acid arginine with the ... leucine, isoleucine, and valine. As a result, these ...

http://vsearch.nlm.nih.gov/vivisimo/cgi-bin/query-meta?v:project=medlineplus&query=ALANINE+OR+ARGININE+OR+CHLORIDE+ION+OR+DEXTROSE+OR+GLYCINE+OR+HISTIDINE+OR+ISOLEUCINE+OR+LEUCINE+OR+LYSINE+OR+METHIONINE+OR+PHENYLALANINE+OR+POTASSIUM+CATION+OR+PROLINE+OR+SERINE+OR+SODIUM+CATION+OR+THREONINE+OR+TRYPTOPHAN+OR+TYROSINE+OR+VALINE

L-Leucine has many beneficial effects on sports performance. It helps preserve lean muscle tissue, it supplies the body with ... L-Leucine has many beneficial effects on sports performance. It helps preserve lean muscle tissue, it supplies the body with ... Directions For Supplement Direct L-Leucine: 3 grams 2-4 times a day in divided doses for a total of 6-12 grams per day. Likely ...

https://www.supplementdirect.com/l-leucine500grams.aspx

... The following example shows how to set up a Leu amino acid: TOPOlogy MASS H 1.008 ...

https://nmr.cit.nih.gov/xplor-nih/xplorMan/node48.html

Low valine as well as low leucine predicted mortality independently from the presence of T2DM in the total cohort and, in ... We conclude that low valine and leucine serum levels predict mortality in patients with established CVD independently from the ... 418-P: The Branched-Chain Amino Acids Valine and Leucine Predict All-Cause Mortality in Cardiovascular Disease Patients ... At baseline, serum valine, leucine and isoleucine were significantly associated with T2DM (all p-values ,0.001). Prospectively ...

https://diabetesjournals.org/diabetes/article/68/Supplement_1/418-P/60383/418-P-The-Branched-Chain-Amino-Acids-Valine-and

You searched for: Subject basic-leucine zipper transcription factors Remove constraint Subject: basic-leucine zipper ... The basic leucine zipper (bZIP) family is one of the largest transcription factor (TF) families in plants, which play crucial ... Malus domestica; apples; basic-leucine zipper transcription factors; drought; fruiting; gene expression regulation; genes; ... growth and development; leaves; leucine zipper; models; plant growth; quantitative polymerase chain reaction; reverse ...

https://pubag.nal.usda.gov/?f%5Bsubject_facet%5D%5B%5D=basic-leucine+zipper+transcription+factors&f%5Bsubject_facet%5D%5B%5D=Malus+domestica&per_page=100&sort=date-asc

Learn what leucine does in the body, its roles in human health, and what foods are the best sources. ... How Much Leucine Do We Need?. The World Health Organization recommends that healthy adults should consume 39 mg if leucine per ... Health Effects of Leucine Deficiency. Chronically low intake of leucine can lead to reduced appetite, weight loss, hair loss, ... Leucine and Muscle Growth. In general, human trials show that leucine supplements can stimulate muscle protein synthesis in the ...

https://nutrivore.com/nutrients/leucine/

3H]Leucine incorporation. Cardiomyocytes cultures were treated with PE (20 μM) or angiotensin-II (Ang, 0.1 μM) in the presence ... b) Cultures of cardiomyocytes were labelled with [3H]-leucine and then treated with PE (20 μM) in the presence or absence of 5 ... Immediately after treatment with agonists, cells were incubated with [3H]-leucine (1.0 mCi ml−1, 163 Ci mmol−1 specific ... 2a). Hypertrophy of cardiomyocytes was evaluated by measuring incorporation of [3H]-leucine into total cellular proteins, a ...

https://www.nature.com/articles/ncomms7656?error=cookies_not_supported&code=b6995c7d-2fae-48ac-8006-0a7fed748af9

Dive into the research topics of Cancer outcomes among Parkinsons disease patients with leucine rich repeat kinase 2 ... Cancer outcomes among Parkinsons disease patients with leucine rich repeat kinase 2 mutations, idiopathic Parkinsons disease ...

https://einstein.pure.elsevier.com/en/publications/cancer-outcomes-among-parkinsons-disease-patients-with-leucine-ri/fingerprints/

The gastrocnemius muscle of WL rats showed increased incorporation of leucine in protein compared to W rats; the leucine-rich ... three other groups of pregnant rats were fed a leucine-rich diet: L - pregnant leucine, WL - tumour-bearing, and PL - pair-fed ... The results suggest that a leucine-rich diet increased the protein synthesis in skeletal muscle in tumour-bearing rats possibly ... Controversly, insulin, other hormones, and branched-chain amino acids, especially leucine, stimulate protein synthesis and ...

https://bmccancer.biomedcentral.com/articles/10.1186/1471-2407-7-42

Disclaimer: Results may vary from person to person. Always consult with a qualified healthcare professional prior to beginning any diet or exercise program or taking any dietary supplement. The content on our website is for informational and educational purposes only and is not intended as medical advice or to replace a relationship with, or the advice of, a qualified healthcare professional ...

https://5percentnutrition.com/blogs/articles/tagged/leucine

... This SWELL Protein Keeps Cells in Shape Posted on April 15th, 2014. by Dr. Francis ... Tags: cell volume regulation, cells, leucine-rich repeat-containing gene 8, LLRC8, SWELL1 ...

https://directorsblog.nih.gov/tag/leucine-rich-repeat-containing-gene-8/

Leucine-rich repeat-containing protein 74A OS=Homo... [more]. sp,A0JPI9,LR74A_RAT. 4.185e-12. 25.25. Leucine-rich repeat- ... Leucine-rich repeat-containing protein 74B OS=Homo... [more]. sp,Q14BP6,LR74B_MOUSE. 2.577e-7. 32.17. Leucine-rich repeat- ... leucine rich repeat containing 74A [Source:HGNC Sy... [more]. LRRC74B. 9.863e-9. 31.30. leucine rich repeat containing 74B [ ... leucine rich repeat containing 74A [Source:ZFIN;Ac... [more]. lrrc74b. 1.039e-12. 40.43. leucine rich repeat containing 74B [ ...

https://planosphere.stowers.org/feature/Schmitea/mediterranea-sexual/transcript/SMED30011349

Leucín (L-leucín, L-Leucine). V kategórii leucín (L-leucín, L-Leucine) máme práve teraz na ScitecPro.sk celkom 2 produktov. ... Leucín (L-leucín, L-leucine, chemická značka Leu alebo L) je najdôležitejšia aminokyselina, ktorá urýchľuje regeneráciu a bráni ... Leucín (L-leucín, L-Leucine) Scitec Nutrition. Pozrite sa na produkty zoradené podľa ceny od najlacnejšieho v kategórii lacné ... Scitec Nutrition Leucine, 100 kapsúl Leucín - najdôležitejšia aminokyselina! Leucín urýchľuje regeneráciu a zabráni úbytku ...

https://scitecpro.sk/leucin

Leucine aminopeptidase is a type of protein called an enzyme. (medlineplus.gov)
The leucine aminopeptidase (LAP) test measures how much of this enzyme is in your blood. (nih.gov)
Leucine aminopeptidase 3:a promising serum biomarker candidate for nonalcoholic steatohepatitis diagnosis. (bvsalud.org)
Increasing evidence demonstrated that aberrant expression of leucine aminopeptidase 3 (LAP3) is involved in NASH. (bvsalud.org)

Low valine as well as low leucine predicted mortality independently from the presence of T2DM in the total cohort and, in subgroup analysis, specifically in patients with T2DM. (diabetesjournals.org)
We conclude that low valine and leucine serum levels predict mortality in patients with established CVD independently from the presence of T2DM. (diabetesjournals.org)

This gene encodes a protein that contains leucine-rich repeats (LRR) at its amino terminus and that is known to be involved in ligand binding. (nih.gov)
Leucine-rich repeats and calponin homology containing 4 (Lrch4) regulates the innate immune response. (nih.gov)
Here, we identified a putative downstream gene of OsBUL1, OsBUL1 DOWNSTREAM GENE1 ( OsBDG1 ) encoding a small protein with short leucine-rich-repeats by cDNA microarray analyses in the lamina joint and panicles of wild-type and osbul1 plants. (frontiersin.org)
LRRK1 is structurally distinct compared to LRRK2, particularly in the position of the leucine-rich repeats relative to the kinase domain. (nih.gov)
Leucine rich repeats and calponin homology containing protein 4 (Lrch4) is a gene that encodes a protein predicted to have a C-terminal transmembrane domain, a calponin homology domain, and 5-8 leucine rich repeats (LRRs). (nih.gov)

Leucine possesses a unique molecular structure with a branched side-chain, making it one of only three branched-chain amino acids (or BCAAs) and giving it a major role in muscle growth and maintenance. (nutrivore.com)
Along with serving as a building block for protein, leucine is one of only two exclusively ketogenic amino acids (meaning it eventually gets metabolized into ketone bodies), and one of only three branched-chain amino acids (referring to the "branched" structure of their molecular side chains). (nutrivore.com)
Controversly, insulin, other hormones, and branched-chain amino acids, especially leucine, stimulate protein synthesis and modulate the activity of translation initiation factors involved in protein synthesis. (biomedcentral.com)

Very few studies investigated the effect of long-term supplementation with leucine on body composition. (ast-ss.com)
Recent research tested the hypothesis that leucine supplementation during most of the adult life of rats might alter body composition by decreasing body fat and attenuating the loss of lean mass, in addition to promoting metabolic risk indicators of acquired chronic diseases [4]. (ast-ss.com)
Supplementation with leucine attenuated weight gain, body fat accumulation, and hyperleptinemia associated with aging. (ast-ss.com)
Long-term supplementation with leucine significantly attenuated fat gain as shown by the mass of visceral fat depots and the percentage of total body fat. (ast-ss.com)
Lipid and glycemic profiles were not affected by leucine supplementation. (ast-ss.com)
Supplementation with leucine did not prevent loss of body protein and muscle protein during aging. (ast-ss.com)
Results from this study confirm previous findings showing that leucine supplementation promotes a decrease in body fat [6]. (ast-ss.com)
Leucine supplementation did not affect the metabolic indicators of acquired chronic diseases (i.e. total cholesterol, triacylglycerol, glycemia). (ast-ss.com)
In addition, long-term supplementation with leucine was ineffective in attenuating the negative effects of aging on indicators of protein nutritional status such as muscle RNA, protein concentration, total body protein, and lean mass. (ast-ss.com)
Long-term leucine supplementation reduces fat mass gain without changing body protein status of aging rats. (ast-ss.com)
Effects of leucine supplementation on the body composition and protein status of rats submitted to food restriction. (ast-ss.com)
Keep reading to discover more about the purpose of amino acids, foods rich in leucine, and the potential benefits of supplementation. (cibdol.com)

A higher dose (2.8 g) of leucine compared to a smaller dose (1.7 g) was effective in stimulating protein synthesis is elderly people whereas both these doses stimulated protein synthesis in younger people. (ast-ss.com)
Postprandial stimulation of muscle protein synthesis in old rats can be restored by a leucine-supplemented meal. (ast-ss.com)
L-Leucine is a nonessential amino acid that plays an important role in protein synthesis. (einpresswire.com)
One of several essential amino acids, leucine plays a crucial role in activating muscle protein synthesis. (cibdol.com)
Leucine-enriched essential amino acids (LEAAs) enhance muscle protein synthesis (MPS) at rest and after exercise. (springeropen.com)
Although a recent review suggested that CHO should be consumed with protein to maximize muscle hypertrophy by inducing an additive effect of insulin and leucine on protein synthesis (Stark et al. (springeropen.com)
Leucine is regarded as the most important BCAA, due to being the greatest activator of protein synthesis. (nutrivore.com)
Through its ability to both increase muscle synthesis and decrease its breakdown, leucine can be beneficial for protecting against sarcopenia (age-related loss of muscle mass). (nutrivore.com)
Since the tumour effects are more pronounced when associated with pregnancy, ehancing muscle-wasting proteolysis, in this study, the influence of a leucine-rich diet on the protein synthesis caused by cancer were investigated. (biomedcentral.com)
The results suggest that a leucine-rich diet increased the protein synthesis in skeletal muscle in tumour-bearing rats possibly through the activation of eIF factors and/or the S6kinase pathway. (biomedcentral.com)
Knowing this, the aim of this study was to examine the effects of a leucine-rich diet on the increased protein degradation and reduced protein synthesis seen in the skeletal muscle of tumour-bearing pregnant rats. (biomedcentral.com)

L-leucine is one of the nine essential amino acids. (organicfacts.net)
Amino acids such as L-leucine are the compounds that make protein and protein are what build up our bones and muscles and skin , essentially our bodies! (organicfacts.net)
It is well known that resistance exercise alone or that followed by the ingestion of essential amino acids (EAA), leucine-enriched essential amino acids (LEAAs), or protein with or without carbohydrate (CHO) increases MPS in humans (Biolo et al. (springeropen.com)
Leucine is one of the nine essential amino acids that we must consume from our diets, and one of the 20 proteinogenic amino acids (used to create proteins). (nutrivore.com)
Leucine is one of only two exclusively ketogenic amino acids-meaning it gets metabolized into ketone bodies rather than glucose. (nutrivore.com)
Leucine (symbol Leu) is one of the nine essential amino acids that we must consume from our diets, and was one of the very first amino acids to be discovered! (nutrivore.com)

There may be an additive effect of enhancing leucine concentration in the diet coupled with resistance exercise on the same age group as used in this study. (ast-ss.com)

If you're looking to build muscle, however, you might consider adding leucine supplements to your daily diet. (organicfacts.net)
NEW YORK CITY, NEW YORK, UNITED STATES, November 10, 2022 / EINPresswire.com / -- L-Leucine is an amino acid that is used in dietary supplements and foods. (einpresswire.com)
L-Leucine supplements are safe for most people, but there are some side effects that can occur. (einpresswire.com)
Instead, we must consume external sources, such as leucine-rich foods and supplements, to get the necessary levels. (cibdol.com)
Due to its effects on insulin, high-dose leucine supplements can cause issues with low blood sugar. (nutrivore.com)

Leucine stimulates insulin secretion, giving it a role in modulating blood glucose levels. (nutrivore.com)
Animal studies and in vitro experiments show that leucine could help improve insulin sensitivity and decrease fat mass, although human trials have been less consistent. (nutrivore.com)

This study focuses on PTSD markers in the glucocorticoid pathway, spotlighting glucocorticoid-induced leucine zipper (GILZ), a transcription factor encoded by the gene Tsc22d3 on the X chromosome. (nih.gov)
If a mutation in the HMGCL gene reduces or eliminates the activity of HMG-CoA lyase, the body is unable to process leucine or make ketones properly. (nih.gov)

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. (broadinstitute.org)
Sestrin2 is a leucine sensor for the mTORC1 pathway. (broadinstitute.org)

The basic leucine zipper (bZIP) family is one of the largest transcription factor (TF) families in plants, which play crucial roles in plant growth and development. (usda.gov)

Leucine (l-leucine) is a proteinogenic (protein-building) branched-chain amino acid (BCAA) that contributes to various bodily functions. (cibdol.com)

Leucine is an essential amino acid (meaning we must get it from our diet) that can be used to synthesize protein. (nutrivore.com)

Leucine biosynthesis in fungi: entering metabolism through the back door. (wikipathways.org)

Specifically, it is responsible for processing leucine, an amino acid that is part of many proteins. (nih.gov)

Elderly rats (6 months old) were divided into two groups, one group received 4% leucine for 40 weeks, and the other group received a control diet for 40 weeks. (ast-ss.com)
three other groups of pregnant rats were fed a leucine-rich diet: L - pregnant leucine, WL - tumour-bearing, and PL - pair-fed, which received the same amount of food as ingested by the WL group. (biomedcentral.com)

The 2022 market could see another significant year for L-Leucine. (einpresswire.com)

L-Leucine has many beneficial effects on sports performance. (supplementdirect.com)
Like other BCCAs, leucine may play a beneficial role in immune function. (nutrivore.com)

When leucine is not processed normally, a buildup of chemical byproducts called organic acids can result in metabolic acidosis. (nih.gov)

The two human leucine-rich repeat kinases (LRRKs), LRRK1 and LRRK2 are large and unusually complex multi-domain kinases which serve to regulate fundamental cellular processes. (nih.gov)

L-leucine has a bitter taste, so there may be added sugars in certain products that could counteract the effects you're seeking. (organicfacts.net)
Also, the effects of leucine combined with resistance exercise may be different in this age group on protein mass. (ast-ss.com)

Studies show that l-leucine can increase rates of muscle repair after the strain and a reduction in loss of muscle mass due to illness. (organicfacts.net)
L-Leucine has been shown to help improve muscle mass and strength. (einpresswire.com)

However, what makes leucine unique is its "essential" status. (cibdol.com)

The market for L-Leucine is growing due to the health benefits it provides. (einpresswire.com)

This graph shows the total number of publications written about "Leucine Transaminase" by people in this website by year, and whether "Leucine Transaminase" was a major or minor topic of these publications. (ouhsc.edu)
Below are the most recent publications written about "Leucine Transaminase" by people in Profiles. (ouhsc.edu)

When exercise is combined with taking additional leucine, it is known to improve weight loss over exercise alone. (organicfacts.net)

This report also includes an L-Leucine market growth analysis that incorporates Porter's five-factor analysis as well as supply chain analysis. (einpresswire.com)
This report provides critical market information, including L-Leucine market size, growth rates and forecasts in key regions and countries, as well as growth opportunities in niche markets. (einpresswire.com)

Anatomy13

Organisms9

Diseases7

Chemicals and Drugs136

Analytical, Diagnostic and Therapeutic Techniques and Equipment28

Psychiatry and Psychology1

Phenomena and Processes62

Technology, Industry, Agriculture3

Information Science3

Health Care1

Control of ketogenesis from amino acids. IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine. (1/5969)

A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (2/5969)

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase. (3/5969)

Nuclear export of LIM-kinase 1, mediated by two leucine-rich nuclear-export signals within the PDZ domain. (4/5969)

Ion binding and permeation through the lepidopteran amino acid transporter KAAT1 expressed in Xenopus oocytes. (5/5969)

A surrogate measure of whole body leucine transport across the cell membrane. (6/5969)

Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis. (7/5969)

Leucine metabolism in preterm infants receiving parenteral nutrition with medium-chain compared with long-chain triacylglycerol emulsions. (8/5969)

Leucine Zippers

Leucyl Aminopeptidase

Keto Acids

Isoleucine

Amino Acids

Leucine Dehydrogenase

Amino Acids, Branched-Chain

Molecular Sequence Data

Amino Acid Sequence

Valine

Basic-Leucine Zipper Transcription Factors

Leucine Transaminase

2-Isopropylmalate Synthase

Phenylalanine

Carbon Isotopes

Base Sequence

Kinetics

Protein Biosynthesis

Mutation

RNA, Transfer, Leu

Norleucine

Proteins

Amino Acids, Essential

Mutagenesis, Site-Directed

Glutamine

Alanine

DNA-Binding Proteins

Transcription Factors

Sequence Homology, Amino Acid

Escherichia coli

Nitrogen

G-Box Binding Factors

Caproates

Dimerization

Pentanoic Acids

Insulin

Binding Sites

Muscle Proteins

Leucine-tRNA Ligase

Oxidation-Reduction

Transaminases

Protein Binding

Nutritional Requirements

Proline

Carbon Radioisotopes

Structure-Activity Relationship

Tritium

Pellagra

Dietary Proteins

Amino Acid Substitution

Cell Line

Lysine

Leucine-Responsive Regulatory Protein

Methionine

Glucose

Protein Structure, Tertiary

Liver

Oxo-Acid-Lyases

Recombinant Fusion Proteins

Threonine

3-Isopropylmalate Dehydrogenase

Protein Conformation

Biological Transport

Models, Molecular

DNA

Cystinyl Aminopeptidase

Isovaleryl-CoA Dehydrogenase

Deuterium

Basic Helix-Loop-Helix Leucine Zipper Transcription Factors

Recombinant Proteins

Glycine

Peptides

Bacterial Proteins

Muscle, Skeletal

Nitrogen Isotopes

Transcription, Genetic

Aminopeptidases

Dicarboxylic Acids

Decarboxylation

TOR Serine-Threonine Kinases