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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
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.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
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.
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 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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
The rate dynamics in chemical or physical systems.
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).
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Proteins prepared by recombinant DNA technology.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Amino acids containing an aromatic side chain.
Amino acids which have a branched carbon chain.
An essential branched-chain amino acid important for hemoglobin formation.
The sum of the weight of all the atoms in a molecule.
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 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 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).
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
Established cell cultures that have the potential to propagate indefinitely.
Proteins found in any species of bacterium.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
The relationships of groups of organisms as reflected by their genetic makeup.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
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.
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.
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.
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.
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.
The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.
The functional hereditary units of BACTERIA.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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 restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
An essential amino acid. It is often added to animal feed.
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.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
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.
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 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).
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.
Amino acids with side chains that are positively charged at physiological pH.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
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.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
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.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
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 mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
A sulfur-containing essential L-amino acid that is important in many body functions.
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.
An essential amino acid that is physiologically active in the L-form.
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 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.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
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.
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
Deletion of sequences of nucleic acids from the genetic material of an individual.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
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.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity.
Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
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.
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.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Sites on an antigen that interact with specific antibodies.
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.
Amino acids with uncharged R groups or side chains.
A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.
The process of cleaving a chemical compound by the addition of a molecule of water.
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 large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
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.
Proteins found in any species of virus.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins.
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).
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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).)
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
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.
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Biochemical identification of mutational changes in a nucleotide sequence.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
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.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
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)
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Proteins found in any species of fungus.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Antibodies produced by a single clone of cells.
A sequential pattern of amino acids occurring more than once in the same protein sequence.
A class of amino acids characterized by a closed ring structure.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.
Any method used for determining the location of and relative distances between genes on a chromosome.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
Peptides composed of between two and twelve amino acids.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Genotypic differences observed among individuals in a population.
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.
Proteins obtained from ESCHERICHIA COLI.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.
A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Elements of limited time intervals, contributing to particular results or situations.
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).
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
A method (first developed by E.M. Southern) for detection of DNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.
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 chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).
The functional hereditary units of FUNGI.
A CD98 antigen light chain that when heterodimerized with CD98 antigen heavy chain (ANTIGENS, CD98 HEAVY CHAIN) forms a protein that mediates sodium-independent L-type amino acid transport.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.
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.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)
Variant forms of the same gene, occupying the same locus on homologous CHROMOSOMES, and governing the variants in production of the same gene product.
Amino acids with side chains that are negatively charged at physiological pH.
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 ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.
An essential amino acid that is required for the production of HISTAMINE.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
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.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
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.
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.
A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.

A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (1/531)

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)

Criteria for choosing amino acid therapy in acute renal failure. (2/531)

Metabolic studies were performed on 19 patients with acute renal failure. Therapy included intravenous hyperalimentation using 15 to 20 g of essential amino acids or 20 to 40 g of essential plus nonessential amino acids and hypertonic glucose (37 to 50%). The effect of this parenteral feeding appears to be primarily pharmacological. Hypertonic glucose promotes the hyperinsulinemia important to be membrane function, the operation of the sodium pump, and cell metabolism. Administration of high biological value crystalline amino acdis potentiates the effect of insulin by inhibiting protein breakdown and promoting protein synthesis, particularly in muscle. This reduces tissue catabolism and urea formation, and promotes potassium, magnesium, and phosphate homeostasis. The branched-chain ketogenic amino acids valine, leucine, and isoleucine may be of particular importance. When indicated, administration of renal failure hyperalimentation and peritoneal or hemodialysis can be expected to complement each other and accelerate recovery. This intravenous fluid therapy, in turn, must be coordinated with proper hemodynamics, usually requiring a colloidal solution to maintain intravascular volume, and cardiotrophic agents such as digitalis and dopamine. Early use of renal failure can be expected to demonstrate the most striking response in terms of survival, early recovery from acute renal failure, and the preservation of physiological homeostasis.  (+info)

Effects of dietary mixtures of amino acids on fetal growth and maternal and fetal amino acid pools in experimental maternal phenylketonuria. (3/531)

BACKGROUND: Branched-chain amino acids have been reported to improve fetal brain development in a rat model in which maternal phenylketonuria (PKU) is induced by the inclusion of an inhibitor of phenylalanine hydroxylase, DL-p-chlorophenylalanine, and L-phenylalanine in the diet. OBJECTIVE: We studied whether a dietary mixture of several large neutral amino acids (LNAAs) would improve fetal brain growth and normalize the fetal brain amino acid profile in a rat model of maternal PKU induced by DL-alpha-methylphenylalanine (AMPhe). DESIGN: Long-Evans rats were fed a basal diet or a similar diet containing 0.5% AMPhe + 3.0% L-phenylalanine (AMPhe + Phe diet) from day 11 until day 20 of gestation in experiments to test various mixtures of LNAAs. Maternal weight gains and food intakes to day 20, fetal body and brain weights at day 20, and fetal brain and fetal and maternal plasma amino acid concentrations at day 20 were measured. RESULTS: Concentrations of phenylalanine and tyrosine in fetal brain and in maternal and fetal plasma were higher and fetal brain weights were lower in rats fed the AMPhe + Phe diet than in rats fed the basal diet. However, fetal brain growth was higher and concentrations of phenylalanine and tyrosine in fetal brain and in maternal and fetal plasma were lower in rats fed the AMPhe + Phe diet plus LNAAs than in rats fed the diet containing AMPhe + Phe alone. CONCLUSION: LNAA supplementation of the diet improved fetal amino acid profiles and alleviated most, but not all, of the depression in fetal brain growth observed in this model of maternal PKU.  (+info)

In vitro transcriptional studies of the bkd operon of Pseudomonas putida: L-branched-chain amino acids and D-leucine are the inducers. (4/531)

BkdR is the transcriptional activator of the bkd operon, which encodes the four proteins of the branched-chain keto acid dehydrogenase multienzyme complex of Pseudomonas putida. In this study, hydroxyl radical footprinting revealed that BkdR bound to only one face of DNA over the same region identified in DNase I protection assays. Deletions of even a few bases in the 5' region of the BkdR-binding site greatly reduced transcription, confirming that the entire protected region is necessary for transcription. In vitro transcription of the bkd operon was obtained by using a vector containing the bkdR-bkdA1 intergenic region plus the putative rho-independent terminator of the bkd operon. Substrate DNA, BkdR, and any of the L-branched-chain amino acids or D-leucine was required for transcription. Branched-chain keto acids, D-valine, and D-isoleucine did not promote transcription. Therefore, the L-branched-chain amino acids and D-leucine are the inducers of the bkd operon. The concentration of L-valine required for half-maximal transcription was 2.8 mM, which is similar to that needed to cause half-maximal proteolysis due to a conformational change in BkdR. A model for transcriptional activation of the bkd operon by BkdR during enzyme induction which incorporates these results is presented.  (+info)

Serum hepatocyte growth factor as an index of extensive catabolism of patients awaiting liver transplantation. (5/531)

BACKGROUND: Whole body catabolism as the result of intrahepatic metabolic derangement is common in liver transplant candidates. However, individual nutritional assessment parameters lack sensitivity and specificity in determining energy status of these patients. Recently, serum hepatocyte growth factor (HGF) has been shown to reflect the recovery of hepatic energy metabolism after liver transplantation. AIMS: The relation between preoperative levels of serum HGF and metabolic variables was investigated to clarify the clinical value of measuring HGF in evaluations of the catabolism. PATIENTS/METHODS: Blood samples were obtained from 30 liver transplant recipients, and biopsy specimens were taken from each recipient's rectus muscle and the explanted liver. Preoperative serum concentration of HGF was determined. Whole body energy metabolism was assessed by measuring glycogen contents of biopsy specimens and plasma or serum levels of glucose, insulin, total ketone bodies, total carnitine, and amino acids. RESULTS: Serum HGF concentration was elevated in 22 of 30 patients and correlated with the Child-Pugh score. It showed a negative association with muscle glycogen content, and a positive correlation with serum levels of glucose, total carnitine, and total ketone bodies. Patients with elevated serum HGF concentrations had higher preoperative plasma levels of aromatic amino acids and branched chain amino acids, associated with lower branched chain to aromatic amino acid ratios. CONCLUSIONS: The elevated serum concentration of HGF in liver transplant candidates reflected inhibition of peripheral glucose storage, enhanced lipid oxidation, and increased peripheral release of branched chain amino acids, and thus extensive energy catabolism.  (+info)

Splanchnic and leg substrate exchange after ingestion of a natural mixed meal in humans. (6/531)

The disposal of a mixed meal was examined in 11 male subjects by multiple (splanchnic and femoral) catheterization combined with double-isotope technique (intravenous [2-3H]glucose plus oral U-[14C]starch). Glucose kinetics and organ substrate balance were measured basally and for 5 h after eating pizza (600 kcal) containing carbohydrates 75 g as starch, proteins 37 g, and lipids 17 g. The portal appearance of ingested carbohydrate was maximal (1.0 mmol/min) between 30 and 60 min after the meal and gradually declined thereafter, but was still incomplete at 300 min (0.46+/-0.08 mmol/min). The total amount of glucose absorbed by the gut over the 5 h of the study was 247+/-26 mmol (45+/-6 g), corresponding to 60+/-6% of the ingested starch. Net splanchnic glucose balance (-6.7+/-0.5 micromol x kg(-1) x min(-1), basal) rose by 250-300% between 30 and 60 min and then returned to baseline. Hepatic glucose production (HGP) was suppressed slightly and only tardily in response to meal ingestion (approximately 30% between 120 and 300 min). Splanchnic glucose uptake (3.7+/-0.6 micromol x kg(-1) x min(-1), basal) peaked to 9.8+/-2.0 micromol x kg(-1) x min(-1) (P<0.001) at 120 min and then returned slowly to baseline. Leg glucose uptake (34+/-5 micromol x leg(-1) x min(-1), basal) rose to 151+/-29 micromol x leg(-1) x min(-1) at 30 min (P<0.001) and remained above baseline until the end of the study, despite no increase in leg blood flow. The total amount of glucose taken up by the splanchnic area and total muscle mass was 161+/-16 mmol (29+/-3 g) and 128 mmol (23 g), respectively, which represent 39 and 30% of the ingested starch. Arterial blood lactate increased by 30% after meal ingestion. Net splanchnic lactate balance switched from a basal net uptake (3.2+/-0.6 micromol kg(-1) x min(-1) to a net output between 60 and 120 min and tended to zero thereafter. Leg lactate release (25+/-11 micromol x leg(-1) x min(-1), basal) drastically decreased postprandially. Arterial concentration of both branched-chain amino acids (BCAA) and non-branched-chain amino acids (N-BCAA) increased significantly after meal ingestion (P<0.001). The splanchnic area switched from a basal net amino acid uptake (31+/-16 and 92+/-48 micromol/min for BCAA and N-BCAA, respectively) to a net amino acid release postprandially. The net splanchnic amino acid release over 5 h was 11.3+/-4.2 mmol for BCAA and 37.8+/-9.7 mmol for N-BCAA. Basally, the net leg balance of BCAA was neutral (-3+/-5 micromol x leg(-1) x min(-1)), whereas that of N-BCAA indicated a net release (54+/-14 micromol x leg(-1) x min(-1)). After meal ingestion, there was a net leg uptake of BCAA (20+/-6 micromol x leg(-1) x min(-1)), whereas leg release of N-BCAA decreased by 50%. It is concluded that in human subjects, 1) the absorption of a natural mixed meal is still incomplete at 5 h after ingestion; 2) HGP is only marginally and tardily inhibited; 3) splanchnic and peripheral tissues contribute to the disposal of meal carbohydrate to approximately the same extent; 4) the splanchnic area transfers >30% of the ingested proteins to the systemic circulation; and 5) after meal ingestion, skeletal muscle takes up BCAA to replenish muscle protein stores.  (+info)

Branched-chain amino acid therapy for spinocerebellar degeneration: a pilot clinical crossover trial. (7/531)

OBJECT: The potential effects of branched-chain amino acids (BCAAs) on spinocerebellar degeneration (SCD) were explored in eleven patients. METHODS: The patients received 200 ml of BCAA-rich solution, 2 mg of thyrotropin-releasing hormone (TRH; protirelin), or a placebo daily for 7 days each in a random order. An SCD score was used to quantify the severity of symptoms. PATIENTS: Eleven patients with SCD (7 male, 4 female; mean age 60+/-11; mean disease duration 5.5 years) participated in this study. RESULTS: The mean SCD score of the eleven patients improved significantly by the BCAA treatment compared with the baseline. The conditions of five of the eleven patients (45%) were clearly improved by the BCAA treatment. All of the responders manifested predominantly cerebellar symptoms, but no prominent parkinsonian symptoms. Two patients with marked rigidity and akinesia did not respond to the treatment. CONCLUSION: We concluded that BCAAs do have a beneficial effect on functional improvement in patients with SCD, and that further large scale studies are needed.  (+info)

Contribution of branched-chain amino acids to uteroplacental ammonia production in sheep. (8/531)

The uteroplacental tissues are a principal site of ammonia production for the conceptus. The goal of this study was to examine the effect of the composition of maternal amino acid (AA) infusate on uteroplacental ammonia production. Seven pregnant ewes (126 +/- 1. 4 days gestation) were infused through the maternal femoral vein (duration 3.5 h, rate 240 ml per hour) with three solutions of AAs. The first infusate was comparable to commercial parenteral nutrition preparations, the second infusate contained the same solution without branched-chain AAs (BCAAs), and the third infusate contained only BCAAs. Blood samples were simultaneously collected from the maternal artery, uterine vein, fetal artery, and umbilical vein to determine plasma AA concentrations and whole blood ammonia concentrations, before (control) and 2 h after (experimental) the start of infusion. Uterine and umbilical blood flows were measured using the ethanol steady-state diffusion method. Results showed that fetal arterial and venous ammonia concentrations increased significantly after infusions with all AAs or only BCAAs, but not without BCAAs. Uteroplacental ammonia production increased in response to each of the three infusates. However, this increase was much greater when the BCAAs were present in infusates. We conclude that there is a significant contribution of BCAAs to the uteroplacental ammonia production. Maternal AA infusions containing BCAAs can result in increased fetal blood ammonia concentrations.  (+info)

Heavy chain disease is also known as:

* Heavy chain defect
* Immunoglobulin (IgG) heavy chain disease
* Kappa chain disease
* Lambda chain disease

The main causes of heavy chain disease include:

* Genetic mutations in the IGH genes that code for the heavy chains of immunoglobulins
* Autoantibodies against the heavy chains of immunoglobulins
* Infections such as HIV, which can lead to the overproduction of certain types of immunoglobulins

The symptoms of heavy chain disease can vary depending on the type of heavy chain that is affected and the severity of the disease. Some common symptoms include:

* Fatigue
* Weight loss
* Fever
* Night sweats
* Swollen lymph nodes
* Enlarged spleen

Heavy chain disease can be diagnosed through a variety of tests, including:

* Blood tests to measure the levels of different types of immunoglobulins in the blood
* Genetic testing to identify genetic mutations in the IGH genes
* Immunophenotyping to study the expression of heavy chains on the surface of B cells

There is no cure for heavy chain disease, but treatment options are available to manage the symptoms and prevent complications. Some common treatments include:

* Corticosteroids to reduce inflammation and suppress the immune system
* Immunoglobulin therapy to replace deficient or abnormal immunoglobulins
* Chemotherapy to reduce the production of abnormal immunoglobulins

The prognosis for heavy chain disease varies depending on the type and severity of the disease. In general, the prognosis is good for patients with light chain disease who receive prompt and appropriate treatment. However, the prognosis is poorer for patients with heavy chain disease, particularly those with a high level of immunoglobulin M (IgM) production.

The causes of heavy chain disease are not well understood, but it is believed to be related to genetic mutations in the IGH genes. There is no known prevention for heavy chain disease, and it is usually diagnosed in adults between the ages of 30 and 60.

Overall, heavy chain disease is a rare and complex disorder that can have a significant impact on quality of life. While there is no cure, early diagnosis and appropriate treatment can improve outcomes for patients with this condition.

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.

Some common effects of chromosomal deletions include:

1. Genetic disorders: Chromosomal deletions can lead to a variety of genetic disorders, such as Down syndrome, which is caused by a deletion of a portion of chromosome 21. Other examples include Prader-Willi syndrome (deletion of chromosome 15), and Williams syndrome (deletion of chromosome 7).
2. Birth defects: Chromosomal deletions can increase the risk of birth defects, such as heart defects, cleft palate, and limb abnormalities.
3. Developmental delays: Children with chromosomal deletions may experience developmental delays, learning disabilities, and intellectual disability.
4. Increased cancer risk: Some chromosomal deletions can increase the risk of developing certain types of cancer, such as chronic myelogenous leukemia (CML) and breast cancer.
5. Reproductive problems: Chromosomal deletions can lead to reproductive problems, such as infertility or recurrent miscarriage.

Chromosomal deletions can be diagnosed through a variety of techniques, including karyotyping (examination of the chromosomes), fluorescence in situ hybridization (FISH), and microarray analysis. Treatment options for chromosomal deletions depend on the specific effects of the deletion and may include medication, surgery, or other forms of therapy.

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.

Cystinuria is caused by mutations in the SLC7A9 gene, which codes for a protein involved in the transport of cystine across the brush border membrane of renal tubular cells. The disorder is inherited in an autosomal recessive pattern, meaning that affected individuals must inherit two copies of the mutated gene (one from each parent) to develop symptoms.

There is no cure for cystinuria, but various treatments can help manage its symptoms. These may include medications to reduce the acidity of the urine and prevent infection, as well as surgical procedures to remove stones or repair damaged kidneys. In some cases, a kidney transplant may be necessary.

It's important for individuals with cystinuria to drink plenty of water and maintain good hydration to help flush out the urinary tract and prevent stone formation. They should also avoid certain foods that may increase the risk of stone formation, such as oxalate-rich foods like spinach and rhubarb.

Overall, while there is no cure for cystinuria, with proper management and care, individuals with this disorder can lead relatively normal lives and minimize the complications associated with it.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

Hartnup disease is a rare genetic disorder that affects the body's ability to absorb vitamin B12 (cobalamin) and other nutrients. It is caused by a mutation in the HCN1 gene, which codes for a protein involved in the transport of cobalamin into the cells.

Symptoms of Hartnup Disease:

The symptoms of Hartnup disease can vary in severity and may include:

* Fatigue
* Weakness
* Pale skin
* Shortness of breath
* Dizziness
* Headaches
* Numbness or tingling in the hands and feet
* Seizures
* Poor appetite
* Diarrhea

Complications of Hartnup Disease:

If left untreated, Hartnup disease can lead to complications such as:

* Anemia (low red blood cell count)
* Nerve damage
* Skin problems
* Eye problems
* Hearing loss
* Increased risk of infections

Treatment of Hartnup Disease:

The treatment of Hartnup disease typically involves a combination of dietary changes and supplements. Patients with the condition may need to follow a strict diet that includes foods high in vitamin B12, such as meat, fish, and dairy products. They may also need to take supplements to ensure they are getting enough of this important nutrient. In some cases, medication may be prescribed to help manage symptoms.

Prognosis of Hartnup Disease:

The prognosis for Hartnup disease is generally good if the condition is diagnosed and treated early. With proper management, most patients with Hartnup disease can lead active and healthy lives. However, if left untreated, the condition can have serious complications that can be difficult to reverse.

Inheritance Pattern of Hartnup Disease:

Hartnup disease is an autosomal recessive disorder, which means that a person must inherit two copies of the mutated HCN1 gene (one from each parent) in order to develop the condition. If a person inherits only one copy of the mutated gene, they will be a carrier of the condition but are unlikely to develop symptoms themselves. Carriers of Hartnup disease can pass the mutated gene on to their children, who have a 25% chance of inheriting two copies of the gene and developing the condition.

Prevention of Hartnup Disease:

There is no known prevention for Hartnup disease. However, if a person knows they are a carrier of the condition, they can work with their healthcare provider to ensure they are getting enough vitamin B12 and monitoring their diet to prevent any complications.

In conclusion, Hartnup disease is a rare genetic disorder that affects the absorption of vitamin B12 in the small intestine. It can cause a range of symptoms, including diarrhea, abdominal pain, and fatigue. Treatment typically involves a combination of dietary changes and supplements, and early diagnosis and management can lead to a good prognosis. However, if left untreated, the condition can have serious complications. If you suspect you or someone you know may be experiencing symptoms of Hartnup disease, it is important to speak with a healthcare provider for proper diagnosis and treatment.

Plasmacytoma is a type of plasma cell dyscrasia, which is a group of diseases that affect the production and function of plasma cells. Plasma cells are a type of white blood cell that produces antibodies to fight infections. In plasmacytoma, the abnormal plasma cells grow and multiply out of control, leading to a tumor.

There are several subtypes of plasmacytoma, including:

* solitary plasmacytoma: A single tumor that occurs in one location.
* multiple myeloma: A type of cancer that affects the bones and is characterized by an overgrowth of malignant plasma cells in the bone marrow.
* extramedullary plasmacytoma: A tumor that occurs outside of the bone marrow, such as in soft tissue or organs.

Plasmacytoma is usually diagnosed through a combination of physical examination, imaging tests such as X-rays or CT scans, and biopsy. Treatment typically involves chemotherapy and/or radiation therapy to destroy the abnormal cells. In some cases, surgery may be necessary to remove the tumor.

Plasmacytoma is a relatively rare cancer, but it can be aggressive and potentially life-threatening if left untreated. It is important for patients with symptoms of plasmacytoma to seek medical attention as soon as possible to receive an accurate diagnosis and appropriate treatment.

There are two main types of hemolysis:

1. Intravascular hemolysis: This type occurs within the blood vessels and is caused by factors such as mechanical injury, oxidative stress, and certain infections.
2. Extravascular hemolysis: This type occurs outside the blood vessels and is caused by factors such as bone marrow disorders, splenic rupture, and certain medications.

Hemolytic anemia is a condition that occurs when there is excessive hemolysis of RBCs, leading to a decrease in the number of healthy red blood cells in the body. This can cause symptoms such as fatigue, weakness, pale skin, and shortness of breath.

Some common causes of hemolysis include:

1. Genetic disorders such as sickle cell anemia and thalassemia.
2. Autoimmune disorders such as autoimmune hemolytic anemia (AIHA).
3. Infections such as malaria, babesiosis, and toxoplasmosis.
4. Medications such as antibiotics, nonsteroidal anti-inflammatory drugs (NSAIDs), and blood thinners.
5. Bone marrow disorders such as aplastic anemia and myelofibrosis.
6. Splenic rupture or surgical removal of the spleen.
7. Mechanical injury to the blood vessels.

Diagnosis of hemolysis is based on a combination of physical examination, medical history, and laboratory tests such as complete blood count (CBC), blood smear examination, and direct Coombs test. Treatment depends on the underlying cause and may include supportive care, blood transfusions, and medications to suppress the immune system or prevent infection.

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.

There are several types of amyloidosis, each with different causes and symptoms. The most common types include:

1. Primary amyloidosis: This type is caused by the production of abnormal proteins in the bone marrow. It mainly affects older adults and can lead to symptoms such as fatigue, weight loss, and numbness or tingling in the hands and feet.
2. Secondary amyloidosis: This type is caused by other conditions, such as rheumatoid arthritis, tuberculosis, or inflammatory bowel disease. It can also be caused by long-term use of certain medications, such as antibiotics or chemotherapy.
3. Familial amyloid polyneuropathy: This type is inherited and affects the nerves in the body, leading to symptoms such as muscle weakness, numbness, and pain.
4. Localized amyloidosis: This type affects a specific area of the body, such as the tongue or the skin.

The symptoms of amyloidosis can vary depending on the organs affected and the severity of the condition. Some common symptoms include:

1. Fatigue
2. Weakness
3. Pain
4. Numbness or tingling in the hands and feet
5. Swelling in the legs, ankles, and feet
6. Difficulty with speech or swallowing
7. Seizures
8. Heart problems
9. Kidney failure
10. Liver failure

The diagnosis of amyloidosis is based on a combination of physical examination, medical history, laboratory tests, and imaging studies. Laboratory tests may include blood tests to measure the levels of certain proteins in the body, as well as biopsies to examine tissue samples under a microscope. Imaging studies, such as X-rays, CT scans, and MRI scans, may be used to evaluate the organs affected by the condition.

There is no cure for amyloidosis, but treatment can help manage the symptoms and slow the progression of the disease. Treatment options may include:

1. Medications to control symptoms such as pain, swelling, and heart problems
2. Chemotherapy to reduce the production of abnormal proteins
3. Autologous stem cell transplantation to replace damaged cells with healthy ones
4. Dialysis to remove excess fluids and waste products from the body
5. Nutritional support to ensure adequate nutrition and hydration
6. Physical therapy to maintain muscle strength and mobility
7. Supportive care to manage pain, improve quality of life, and reduce stress on the family.

In conclusion, amyloidosis is a complex and rare group of diseases that can affect multiple organs and systems in the body. Early diagnosis and treatment are essential to managing the symptoms and slowing the progression of the disease. It is important for patients with suspected amyloidosis to seek medical attention from a specialist, such as a hematologist or nephrologist, for proper evaluation and treatment.

There are several types of PKU, including classic PKU, mild PKU, and hyperphenylalaninemia (HPA). Classic PKU is the most severe form of the disorder and is characterized by a complete deficiency of the enzyme phenylalanine hydroxylase (PAH), which is necessary for the breakdown of Phe. Mild PKU is characterized by a partial deficiency of PAH, while HPA is caused by a variety of other genetic defects that affect the breakdown of Phe.

Symptoms of PKU can vary depending on the severity of the disorder, but may include developmental delays, intellectual disability, seizures, and behavioral problems. If left untreated, PKU can lead to serious health complications such as brain damage, seizures, and even death.

The primary treatment for PKU is a strict diet that limits the intake of Phe. This typically involves avoiding foods that are high in Phe, such as meat, fish, eggs, and dairy products, and consuming specialized medical foods that are low in Phe. In some cases, medication may also be prescribed to help manage symptoms.

PKU is an autosomal recessive disorder, which means that it is inherited in an unusual way. Both parents must carry the genetic mutation that causes PKU, and each child has a 25% chance of inheriting the disorder. PKU can be diagnosed through newborn screening, which is typically performed soon after birth. Early diagnosis and treatment can help prevent or minimize the symptoms of PKU and improve quality of life for individuals with the disorder.

Explanation: Neoplastic cell transformation is a complex process that involves multiple steps and can occur as a result of genetic mutations, environmental factors, or a combination of both. The process typically begins with a series of subtle changes in the DNA of individual cells, which can lead to the loss of normal cellular functions and the acquisition of abnormal growth and reproduction patterns.

Over time, these transformed cells can accumulate further mutations that allow them to survive and proliferate despite adverse conditions. As the transformed cells continue to divide and grow, they can eventually form a tumor, which is a mass of abnormal cells that can invade and damage surrounding tissues.

In some cases, cancer cells can also break away from the primary tumor and travel through the bloodstream or lymphatic system to other parts of the body, where they can establish new tumors. This process, known as metastasis, is a major cause of death in many types of cancer.

It's worth noting that not all transformed cells will become cancerous. Some forms of cellular transformation, such as those that occur during embryonic development or tissue regeneration, are normal and necessary for the proper functioning of the body. However, when these transformations occur in adult tissues, they can be a sign of cancer.

See also: Cancer, Tumor

Word count: 190

1. Bone fractures: The most common symptom of OI is an increased risk of fractures, which can occur with minimal trauma or even without any apparent cause.
2. Dental problems: People with OI may have poorly formed teeth, tooth decay, and gum disease.
3. Short stature: Many individuals with OI are short in stature, due to the effects of chronic fractures and pain on growth and development.
4. Muscle weakness: Some people with OI may experience muscle weakness, particularly in the limbs.
5. Joint problems: OI can cause issues with joint mobility and stability, leading to arthritis and other degenerative conditions.
6. Scoliosis: Curvature of the spine is common in people with OI, which can lead to back pain and respiratory problems.
7. Blue sclerae: A distinctive feature of OI is the presence of blue-colored sclerae (the white part of the eye).
8. Other symptoms: Some people with OI may experience hearing loss, vision problems, and delayed development.

There are several types of OI, each caused by a mutation in a specific gene. The most common forms of OI are type I, type II, and type III. Type I is the mildest form and type III is the most severe. There is no cure for OI, but treatment focuses on managing symptoms and preventing complications. This may include:

1. Bracing and orthotics: To support weakened bones and improve posture.
2. Physical therapy: To maintain muscle strength and flexibility.
3. Pain management: To reduce the risk of chronic pain and improve quality of life.
4. Dental care: Regular dental check-ups and appropriate treatment to prevent tooth decay and gum disease.
5. Respiratory care: To manage breathing problems and prevent respiratory infections.
6. Monitoring for hearing loss: Regular hearing tests to detect any hearing loss and provide appropriate intervention.
7. Early intervention: To help children with OI develop skills and abilities to their full potential.
8. Genetic counseling: For families with a history of OI, to understand the risks and implications for future pregnancies.

It's important for people with OI to work closely with their healthcare provider to manage their condition and prevent complications. With proper care and support, many people with OI can lead active and fulfilling lives.

Also known as: aminoacyl-tRNA synthetase deficiency, aminoacyl-tRNA synthetase/tRNA synthetase deficiency, and amino acid transporter defects.

https://www.medicinenet.com › Medical Dictionary › G

A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.

Genetic Translocation | Definition & Facts | Britannica
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Genetic translocation, also called chromosomal translocation, a type of chromosomal aberration in which a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material. Genetic translocations are often found in cancer cells and may play a role in the development and progression of cancer.

Translocation, Genetic | health Encyclopedia - UPMC
https://www.upmc.com › health-library › gene...

A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.

Genetic Translocation | Genetics Home Reference - NIH
https://ghr.nlm.nih.gov › condition › ge...

A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.

In conclusion, Genetic Translocation is an abnormality in the number or arrangement of chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome, resulting in a gain or loss of genetic material that can have significant effects on the individual.

1. Activation of oncogenes: Some viruses contain genes that code for proteins that can activate existing oncogenes in the host cell, leading to uncontrolled cell growth.
2. Inactivation of tumor suppressor genes: Other viruses may contain genes that inhibit the expression of tumor suppressor genes, allowing cells to grow and divide uncontrollably.
3. Insertional mutagenesis: Some viruses can insert their own DNA into the host cell's genome, leading to disruptions in normal cellular function and potentially causing cancer.
4. Epigenetic changes: Viral infection can also cause epigenetic changes, such as DNA methylation or histone modification, that can lead to the silencing of tumor suppressor genes and the activation of oncogenes.

Viral cell transformation is a key factor in the development of many types of cancer, including cervical cancer caused by human papillomavirus (HPV), and liver cancer caused by hepatitis B virus (HBV). In addition, some viruses are specifically known to cause cancer, such as Kaposi's sarcoma-associated herpesvirus (KSHV) and Merkel cell polyomavirus (MCV).

Early detection and treatment of viral infections can help prevent the development of cancer. Vaccines are also available for some viruses that are known to cause cancer, such as HPV and hepatitis B. Additionally, antiviral therapy can be used to treat existing infections and may help reduce the risk of cancer development.

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 risk factors for developing HCC, including:

* Cirrhosis, which can be caused by heavy alcohol consumption, viral hepatitis (such as hepatitis B and C), or fatty liver disease
* Family history of liver disease
* Chronic obstructive pulmonary disease (COPD)
* Diabetes
* Obesity

HCC can be challenging to diagnose, as the symptoms are non-specific and can be similar to those of other conditions. However, some common symptoms of HCC include:

* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Loss of appetite
* Abdominal pain or discomfort
* Weight loss

If HCC is suspected, a doctor may perform several tests to confirm the diagnosis, including:

* Imaging tests, such as ultrasound, CT scan, or MRI, to look for tumors in the liver
* Blood tests to check for liver function and detect certain substances that are produced by the liver
* Biopsy, which involves removing a small sample of tissue from the liver to examine under a microscope

Once HCC is diagnosed, treatment options will depend on several factors, including the stage and location of the cancer, the patient's overall health, and their personal preferences. Treatment options may include:

* Surgery to remove the tumor or parts of the liver
* Ablation, which involves destroying the cancer cells using heat or cold
* Chemoembolization, which involves injecting chemotherapy drugs into the hepatic artery to reach the cancer cells
* Targeted therapy, which uses drugs or other substances to target specific molecules that are involved in the growth and spread of the cancer

Overall, the prognosis for HCC is poor, with a 5-year survival rate of approximately 20%. However, early detection and treatment can improve outcomes. It is important for individuals at high risk for HCC to be monitored regularly by a healthcare provider, and to seek medical attention if they experience any symptoms.

There are several different types of weight gain, including:

1. Clinical obesity: This is defined as a BMI of 30 or higher, and is typically associated with a range of serious health problems, such as heart disease, type 2 diabetes, and certain types of cancer.
2. Central obesity: This refers to excess fat around the waistline, which can increase the risk of health problems such as heart disease and type 2 diabetes.
3. Muscle gain: This occurs when an individual gains weight due to an increase in muscle mass, rather than fat. This type of weight gain is generally considered healthy and can improve overall fitness and athletic performance.
4. Fat gain: This occurs when an individual gains weight due to an increase in body fat, rather than muscle or bone density. Fat gain can increase the risk of health problems such as heart disease and type 2 diabetes.

Weight gain can be measured using a variety of methods, including:

1. Body mass index (BMI): This is a widely used measure of weight gain that compares an individual's weight to their height. A BMI of 18.5-24.9 is considered normal, while a BMI of 25-29.9 is considered overweight, and a BMI of 30 or higher is considered obese.
2. Waist circumference: This measures the distance around an individual's waistline and can be used to assess central obesity.
3. Skinfold measurements: These involve measuring the thickness of fat at specific points on the body, such as the abdomen or thighs.
4. Dual-energy X-ray absorptiometry (DXA): This is a non-invasive test that uses X-rays to measure bone density and body composition.
5. Bioelectrical impedance analysis (BIA): This is a non-invasive test that uses electrical impulses to measure body fat percentage and other physiological parameters.

Causes of weight gain:

1. Poor diet: Consuming high amounts of processed foods, sugar, and saturated fats can lead to weight gain.
2. Lack of physical activity: Engaging in regular exercise can help burn calories and maintain a healthy weight.
3. Genetics: An individual's genetic makeup can affect their metabolism and body composition, making them more prone to weight gain.
4. Hormonal imbalances: Imbalances in hormones such as insulin, thyroid, and cortisol can contribute to weight gain.
5. Medications: Certain medications, such as steroids and antidepressants, can cause weight gain as a side effect.
6. Sleep deprivation: Lack of sleep can disrupt hormones that regulate appetite and metabolism, leading to weight gain.
7. Stress: Chronic stress can lead to emotional eating and weight gain.
8. Age: Metabolism slows down with age, making it more difficult to maintain a healthy weight.
9. Medical conditions: Certain medical conditions such as hypothyroidism, Cushing's syndrome, and polycystic ovary syndrome (PCOS) can also contribute to weight gain.

Treatment options for obesity:

1. Lifestyle modifications: A combination of diet, exercise, and stress management techniques can help individuals achieve and maintain a healthy weight.
2. Medications: Prescription medications such as orlistat, phentermine-topiramate, and liraglutide can aid in weight loss.
3. Bariatric surgery: Surgical procedures such as gastric bypass surgery and sleeve gastrectomy can be effective for severe obesity.
4. Behavioral therapy: Cognitive-behavioral therapy (CBT) and other forms of counseling can help individuals develop healthy eating habits and improve their physical activity levels.
5. Meal replacement plans: Meal replacement plans such as Medifast can provide individuals with a structured diet that is high in protein, fiber, and vitamins, and low in calories and sugar.
6. Weight loss supplements: Supplements such as green tea extract, garcinia cambogia, and forskolin can help boost weight loss efforts.
7. Portion control: Using smaller plates and measuring cups can help individuals regulate their portion sizes and maintain a healthy weight.
8. Mindful eating: Paying attention to hunger and fullness cues, eating slowly, and savoring food can help individuals develop healthy eating habits.
9. Physical activity: Engaging in regular physical activity such as walking, running, swimming, or cycling can help individuals burn calories and maintain a healthy weight.

It's important to note that there is no one-size-fits-all approach to treating obesity, and the most effective treatment plan will depend on the individual's specific needs and circumstances. Consulting with a healthcare professional such as a registered dietitian or a physician can help individuals develop a personalized treatment plan that is safe and effective.

Multiple myeloma is the second most common type of hematologic cancer after non-Hodgkin's lymphoma, accounting for approximately 1% of all cancer deaths worldwide. It is more common in older adults, with most patients being diagnosed over the age of 65.

The exact cause of multiple myeloma is not known, but it is believed to be linked to genetic mutations that occur in the plasma cells. There are several risk factors that have been associated with an increased risk of developing multiple myeloma, including:

1. Family history: Having a family history of multiple myeloma or other plasma cell disorders increases the risk of developing the disease.
2. Age: The risk of developing multiple myeloma increases with age, with most patients being diagnosed over the age of 65.
3. Race: African Americans are at higher risk of developing multiple myeloma than other races.
4. Obesity: Being overweight or obese may increase the risk of developing multiple myeloma.
5. Exposure to certain chemicals: Exposure to certain chemicals such as pesticides, solvents, and heavy metals has been linked to an increased risk of developing multiple myeloma.

The symptoms of multiple myeloma can vary depending on the severity of the disease and the organs affected. Common symptoms include:

1. Bone pain: Pain in the bones, particularly in the spine, ribs, or long bones, is a common symptom of multiple myeloma.
2. Fatigue: Feeling tired or weak is another common symptom of the disease.
3. Infections: Patients with multiple myeloma may be more susceptible to infections due to the impaired functioning of their immune system.
4. Bone fractures: Weakened bones can lead to an increased risk of fractures, particularly in the spine, hips, or ribs.
5. Kidney problems: Multiple myeloma can cause damage to the kidneys, leading to problems such as kidney failure or proteinuria (excess protein in the urine).
6. Anemia: A low red blood cell count can cause anemia, which can lead to fatigue, weakness, and shortness of breath.
7. Increased calcium levels: High levels of calcium in the blood can cause symptoms such as nausea, vomiting, constipation, and confusion.
8. Neurological problems: Multiple myeloma can cause neurological problems such as headaches, numbness or tingling in the arms and legs, and difficulty with coordination and balance.

The diagnosis of multiple myeloma typically involves a combination of physical examination, medical history, and laboratory tests. These may include:

1. Complete blood count (CBC): A CBC can help identify abnormalities in the numbers and characteristics of different types of blood cells, including red blood cells, white blood cells, and platelets.
2. Serum protein electrophoresis (SPEP): This test measures the levels of different proteins in the blood, including immunoglobulins (antibodies) and abnormal proteins produced by myeloma cells.
3. Urine protein electrophoresis (UPEP): This test measures the levels of different proteins in the urine.
4. Immunofixation: This test is used to identify the type of antibody produced by myeloma cells and to rule out other conditions that may cause similar symptoms.
5. Bone marrow biopsy: A bone marrow biopsy involves removing a sample of tissue from the bone marrow for examination under a microscope. This can help confirm the diagnosis of multiple myeloma and determine the extent of the disease.
6. Imaging tests: Imaging tests such as X-rays, CT scans, or MRI scans may be used to assess the extent of bone damage or other complications of multiple myeloma.
7. Genetic testing: Genetic testing may be used to identify specific genetic abnormalities that are associated with multiple myeloma and to monitor the response of the disease to treatment.

It's important to note that not all patients with MGUS or smoldering myeloma will develop multiple myeloma, and some patients with multiple myeloma may not have any symptoms at all. However, if you are experiencing any of the symptoms listed above or have a family history of multiple myeloma, it's important to talk to your doctor about your risk and any tests that may be appropriate for you.

Explanation: Genetic predisposition to disease is influenced by multiple factors, including the presence of inherited genetic mutations or variations, environmental factors, and lifestyle choices. The likelihood of developing a particular disease can be increased by inherited genetic mutations that affect the functioning of specific genes or biological pathways. For example, inherited mutations in the BRCA1 and BRCA2 genes increase the risk of developing breast and ovarian cancer.

The expression of genetic predisposition to disease can vary widely, and not all individuals with a genetic predisposition will develop the disease. Additionally, many factors can influence the likelihood of developing a particular disease, such as environmental exposures, lifestyle choices, and other health conditions.

Inheritance patterns: Genetic predisposition to disease can be inherited in an autosomal dominant, autosomal recessive, or multifactorial pattern, depending on the specific disease and the genetic mutations involved. Autosomal dominant inheritance means that a single copy of the mutated gene is enough to cause the disease, while autosomal recessive inheritance requires two copies of the mutated gene. Multifactorial inheritance involves multiple genes and environmental factors contributing to the development of the disease.

Examples of diseases with a known genetic predisposition:

1. Huntington's disease: An autosomal dominant disorder caused by an expansion of a CAG repeat in the Huntingtin gene, leading to progressive neurodegeneration and cognitive decline.
2. Cystic fibrosis: An autosomal recessive disorder caused by mutations in the CFTR gene, leading to respiratory and digestive problems.
3. BRCA1/2-related breast and ovarian cancer: An inherited increased risk of developing breast and ovarian cancer due to mutations in the BRCA1 or BRCA2 genes.
4. Sickle cell anemia: An autosomal recessive disorder caused by a point mutation in the HBB gene, leading to defective hemoglobin production and red blood cell sickling.
5. Type 1 diabetes: An autoimmune disease caused by a combination of genetic and environmental factors, including multiple genes in the HLA complex.

Understanding the genetic basis of disease can help with early detection, prevention, and treatment. For example, genetic testing can identify individuals who are at risk for certain diseases, allowing for earlier intervention and preventive measures. Additionally, understanding the genetic basis of a disease can inform the development of targeted therapies and personalized medicine."


The signs and symptoms of CE can vary depending on the location of the tumor, but they may include:

* Lumps or swelling in the neck, underarm, or groin area
* Fever
* Fatigue
* Weight loss
* Night sweats
* Swollen lymph nodes
* Pain in the affected area

CE is caused by a genetic mutation that leads to uncontrolled cell growth and division. The exact cause of the mutation is not fully understood, but it is believed to be linked to exposure to certain viruses or chemicals.

Diagnosis of CE typically involves a combination of physical examination, imaging tests such as CT scans or PET scans, and biopsy to confirm the presence of cancer cells. Treatment options for CE depend on the stage and location of the tumor, but may include:

* Chemotherapy to kill cancer cells
* Radiation therapy to shrink the tumor
* Surgery to remove the tumor
* Immunotherapy to boost the immune system's ability to fight the cancer

Overall, CE is a rare and aggressive form of cancer that requires prompt diagnosis and treatment to improve outcomes.

The hallmark symptom of RA is an inability to reabsorb these amino acids, leading to their excessive excretion in the urine. This can cause a range of health problems, including:

1. Cystinuria: excessive excretion of cystine in the urine, which can form stones and damage the kidneys.
2. Glutaric aciduria type 1 (GA1): excessive excretion of glutaric acid and other branched-chain amino acids in the urine, which can lead to developmental delays, intellectual disability, and seizures.
3. Aminoaciduria: excessive excretion of various amino acids in the urine, including alanine, glycine, and proline.
4. Kidney damage: chronic exposure to high levels of certain amino acids in the urine can cause damage to the kidneys, leading to chronic kidney disease and potentially end-stage renal disease (ESRD).
5. Other complications: RA can also lead to other health problems, such as electrolyte imbalances, bone disease, and metabolic acidosis.

RA is diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment typically involves a combination of dietary restrictions, medications, and kidney transplantation in severe cases.

Types of experimental neoplasms include:

* Xenografts: tumors that are transplanted into animals from another species, often humans.
* Transgenic tumors: tumors that are created by introducing cancer-causing genes into an animal's genome.
* Chemically-induced tumors: tumors that are caused by exposure to certain chemicals or drugs.

The use of experimental neoplasms in research has led to significant advances in our understanding of cancer biology and the development of new treatments for the disease. However, the use of animals in cancer research is a controversial topic and alternatives to animal models are being developed and implemented.

Liver neoplasms, also known as liver tumors or hepatic tumors, are abnormal growths of tissue in the liver. These growths can be benign (non-cancerous) or malignant (cancerous). Malignant liver tumors can be primary, meaning they originate in the liver, or metastatic, meaning they spread to the liver from another part of the body.

There are several types of liver neoplasms, including:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and arises from the main cells of the liver (hepatocytes). HCC is often associated with cirrhosis and can be caused by viral hepatitis or alcohol abuse.
2. Cholangiocarcinoma: This type of cancer arises from the cells lining the bile ducts within the liver (cholangiocytes). Cholangiocarcinoma is rare and often diagnosed at an advanced stage.
3. Hemangiosarcoma: This is a rare type of cancer that originates in the blood vessels of the liver. It is most commonly seen in dogs but can also occur in humans.
4. Fibromas: These are benign tumors that arise from the connective tissue of the liver (fibrocytes). Fibromas are usually small and do not spread to other parts of the body.
5. Adenomas: These are benign tumors that arise from the glandular cells of the liver (hepatocytes). Adenomas are usually small and do not spread to other parts of the body.

The symptoms of liver neoplasms vary depending on their size, location, and whether they are benign or malignant. Common symptoms include abdominal pain, fatigue, weight loss, and jaundice (yellowing of the skin and eyes). Diagnosis is typically made through a combination of imaging tests such as CT scans, MRI scans, and ultrasound, and a biopsy to confirm the presence of cancer cells.

Treatment options for liver neoplasms depend on the type, size, location, and stage of the tumor, as well as the patient's overall health. Surgery may be an option for some patients with small, localized tumors, while others may require chemotherapy or radiation therapy to shrink the tumor before surgery can be performed. In some cases, liver transplantation may be necessary.

Prognosis for liver neoplasms varies depending on the type and stage of the cancer. In general, early detection and treatment improve the prognosis, while advanced-stage disease is associated with a poorer prognosis.

Examples of inborn errors of metabolism include:

1. Phenylketonuria (PKU): A disorder that affects the body's ability to break down the amino acid phenylalanine, leading to a buildup of this substance in the blood and brain.
2. Hypothyroidism: A condition in which the thyroid gland does not produce enough thyroid hormones, leading to developmental delays, intellectual disability, and other health problems.
3. Maple syrup urine disease (MSUD): A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
4. Glycogen storage diseases: A group of disorders that affect the body's ability to store and use glycogen, a form of carbohydrate energy.
5. Mucopolysaccharidoses (MPS): A group of disorders that affect the body's ability to produce and break down certain sugars, leading to a buildup of these substances in the body.
6. Citrullinemia: A disorder that affects the body's ability to break down the amino acid citrulline, leading to a buildup of this substance in the blood and urine.
7. Homocystinuria: A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
8. Tyrosinemia: A disorder that affects the body's ability to break down the amino acid tyrosine, leading to a buildup of this substance in the blood and liver.

Inborn errors of metabolism can be diagnosed through a combination of physical examination, medical history, and laboratory tests such as blood and urine tests. Treatment for these disorders varies depending on the specific condition and may include dietary changes, medication, and other therapies. Early detection and treatment can help manage symptoms and prevent complications.

1. Parvovirus (Parvo): A highly contagious viral disease that affects dogs of all ages and breeds, causing symptoms such as vomiting, diarrhea, and severe dehydration.
2. Distemper: A serious viral disease that can affect dogs of all ages and breeds, causing symptoms such as fever, coughing, and seizures.
3. Rabies: A deadly viral disease that affects dogs and other animals, transmitted through the saliva of infected animals, and causing symptoms such as aggression, confusion, and paralysis.
4. Heartworms: A common condition caused by a parasitic worm that infects the heart and lungs of dogs, leading to symptoms such as coughing, fatigue, and difficulty breathing.
5. Ticks and fleas: These external parasites can cause skin irritation, infection, and disease in dogs, including Lyme disease and tick-borne encephalitis.
6. Canine hip dysplasia (CHD): A genetic condition that affects the hip joint of dogs, causing symptoms such as arthritis, pain, and mobility issues.
7. Osteosarcoma: A type of bone cancer that affects dogs, often diagnosed in older dogs and causing symptoms such as lameness, swelling, and pain.
8. Allergies: Dog allergies can cause skin irritation, ear infections, and other health issues, and may be triggered by environmental factors or specific ingredients in their diet.
9. Gastric dilatation-volvulus (GDV): A life-threatening condition that occurs when a dog's stomach twists and fills with gas, causing symptoms such as vomiting, pain, and difficulty breathing.
10. Cruciate ligament injuries: Common in active dogs, these injuries can cause joint instability, pain, and mobility issues.

It is important to monitor your dog's health regularly and seek veterinary care if you notice any changes or abnormalities in their behavior, appetite, or physical condition.

Treatment for uremia typically involves dialysis or kidney transplantation to remove excess urea from the blood and restore normal kidney function. In some cases, medications may be prescribed to help manage symptoms such as high blood pressure, anemia, or electrolyte imbalances.

The term "uremia" is derived from the Greek words "oura," meaning "urea," and "emia," meaning "in the blood." It was first used in the medical literature in the late 19th century to describe a condition caused by excess urea in the blood. Today, it remains an important diagnostic term in nephrology and is often used interchangeably with the term "uremic syndrome."

There are several types of lymphoma, including:

1. Hodgkin lymphoma: This is a type of lymphoma that originates in the white blood cells called Reed-Sternberg cells. It is characterized by the presence of giant cells with multiple nucleoli.
2. Non-Hodgkin lymphoma (NHL): This is a type of lymphoma that does not meet the criteria for Hodgkin lymphoma. There are many subtypes of NHL, each with its own unique characteristics and behaviors.
3. Cutaneous lymphoma: This type of lymphoma affects the skin and can take several forms, including cutaneous B-cell lymphoma and cutaneous T-cell lymphoma.
4. Primary central nervous system (CNS) lymphoma: This is a rare type of lymphoma that develops in the brain or spinal cord.
5. Post-transplantation lymphoproliferative disorder (PTLD): This is a type of lymphoma that develops in people who have undergone an organ transplant, often as a result of immunosuppressive therapy.

The symptoms of lymphoma can vary depending on the type and location of the cancer. Some common symptoms include:

* Swollen lymph nodes
* Fever
* Fatigue
* Weight loss
* Night sweats
* Itching

Lymphoma is diagnosed through a combination of physical examination, imaging tests (such as CT scans or PET scans), and biopsies. Treatment options for lymphoma depend on the type and stage of the cancer, and may include chemotherapy, radiation therapy, immunotherapy, or stem cell transplantation.

Overall, lymphoma is a complex and diverse group of cancers that can affect people of all ages and backgrounds. While it can be challenging to diagnose and treat, advances in medical technology and research have improved the outlook for many patients with lymphoma.

Some common poultry diseases include:

1. Avian influenza (bird flu): A highly contagious viral disease that affects birds and can be transmitted to humans.
2. Newcastle disease: A viral disease that causes respiratory and gastrointestinal symptoms in birds.
3. Infectious bronchitis: A viral disease that causes respiratory symptoms in birds.
4. Marek's disease: A viral disease that affects the nervous system of birds.
5. Coccidiosis: A parasitic disease caused by the Eimeria protozoa, which can cause diarrhea and weight loss in birds.
6. Chicken anemia virus: A viral disease that causes anemia and weakened immune systems in chickens.
7. Fowl pox: A viral disease that causes skin lesions and other symptoms in birds.
8. Avian encephalomyelitis (AE): A viral disease that affects the brain and spinal cord of birds, causing neurological symptoms such as paralysis and death.
9. Mycoplasmosis: A bacterial disease caused by the Mycoplasma bacteria, which can cause respiratory and other symptoms in birds.
10. Aspergillosis: A fungal disease that affects the respiratory system of birds, causing symptoms such as coughing and difficulty breathing.

Poultry diseases can have a significant impact on bird health and productivity, and can also be transmitted to humans in some cases. It is important for poultry farmers and owners to monitor their flocks closely and take steps to prevent the spread of disease, such as providing clean water and feed, maintaining good hygiene, and vaccinating birds against certain diseases.

A disease that affects pigs, including viral, bacterial, and parasitic infections, as well as genetic disorders and nutritional deficiencies. Some common swine diseases include:

1. Porcine Reproductive and Respiratory Syndrome (PRRS): A highly contagious viral disease that can cause reproductive failure, respiratory problems, and death.
2. Swine Influenza: A viral infection similar to human influenza, which can cause fever, coughing, and pneumonia in pigs.
3. Erysipelas: A bacterial infection that causes high fever, loss of appetite, and skin lesions in pigs.
4. Actinobacillosis: A bacterial infection that can cause pneumonia, arthritis, and abscesses in pigs.
5. Parasitic infections: Such as gastrointestinal parasites like roundworms and tapeworms, which can cause diarrhea, anemia, and weight loss in pigs.
6. Scrapie: A degenerative neurological disorder that affects pigs and other animals, causing confusion, aggression, and eventually death.
7. Nutritional deficiencies: Such as a lack of vitamin E or selenium, which can cause a range of health problems in pigs, including muscular dystrophy and anemia.
8. Genetic disorders: Such as achondroplasia, a condition that causes dwarfism and deformities in pigs.
9. Environmental diseases: Such as heat stress, which can cause a range of health problems in pigs, including respiratory distress and death.

It's important to note that many swine diseases have similar symptoms, making accurate diagnosis by a veterinarian essential for effective treatment and control.

Neoplasm refers to an abnormal growth of cells that can be benign (non-cancerous) or malignant (cancerous). Neoplasms can occur in any part of the body and can affect various organs and tissues. The term "neoplasm" is often used interchangeably with "tumor," but while all tumors are neoplasms, not all neoplasms are tumors.

Types of Neoplasms

There are many different types of neoplasms, including:

1. Carcinomas: These are malignant tumors that arise in the epithelial cells lining organs and glands. Examples include breast cancer, lung cancer, and colon cancer.
2. Sarcomas: These are malignant tumors that arise in connective tissue, such as bone, cartilage, and fat. Examples include osteosarcoma (bone cancer) and soft tissue sarcoma.
3. Lymphomas: These are cancers of the immune system, specifically affecting the lymph nodes and other lymphoid tissues. Examples include Hodgkin lymphoma and non-Hodgkin lymphoma.
4. Leukemias: These are cancers of the blood and bone marrow that affect the white blood cells. Examples include acute myeloid leukemia (AML) and chronic lymphocytic leukemia (CLL).
5. Melanomas: These are malignant tumors that arise in the pigment-producing cells called melanocytes. Examples include skin melanoma and eye melanoma.

Causes and Risk Factors of Neoplasms

The exact causes of neoplasms are not fully understood, but there are several known risk factors that can increase the likelihood of developing a neoplasm. These include:

1. Genetic predisposition: Some people may be born with genetic mutations that increase their risk of developing certain types of neoplasms.
2. Environmental factors: Exposure to certain environmental toxins, such as radiation and certain chemicals, can increase the risk of developing a neoplasm.
3. Infection: Some neoplasms are caused by viruses or bacteria. For example, human papillomavirus (HPV) is a common cause of cervical cancer.
4. Lifestyle factors: Factors such as smoking, excessive alcohol consumption, and a poor diet can increase the risk of developing certain types of neoplasms.
5. Family history: A person's risk of developing a neoplasm may be higher if they have a family history of the condition.

Signs and Symptoms of Neoplasms

The signs and symptoms of neoplasms can vary depending on the type of cancer and where it is located in the body. Some common signs and symptoms include:

1. Unusual lumps or swelling
2. Pain
3. Fatigue
4. Weight loss
5. Change in bowel or bladder habits
6. Unexplained bleeding
7. Coughing up blood
8. Hoarseness or a persistent cough
9. Changes in appetite or digestion
10. Skin changes, such as a new mole or a change in the size or color of an existing mole.

Diagnosis and Treatment of Neoplasms

The diagnosis of a neoplasm usually involves a combination of physical examination, imaging tests (such as X-rays, CT scans, or MRI scans), and biopsy. A biopsy involves removing a small sample of tissue from the suspected tumor and examining it under a microscope for cancer cells.

The treatment of neoplasms depends on the type, size, location, and stage of the cancer, as well as the patient's overall health. Some common treatments include:

1. Surgery: Removing the tumor and surrounding tissue can be an effective way to treat many types of cancer.
2. Chemotherapy: Using drugs to kill cancer cells can be effective for some types of cancer, especially if the cancer has spread to other parts of the body.
3. Radiation therapy: Using high-energy radiation to kill cancer cells can be effective for some types of cancer, especially if the cancer is located in a specific area of the body.
4. Immunotherapy: Boosting the body's immune system to fight cancer can be an effective treatment for some types of cancer.
5. Targeted therapy: Using drugs or other substances to target specific molecules on cancer cells can be an effective treatment for some types of cancer.

Prevention of Neoplasms

While it is not always possible to prevent neoplasms, there are several steps that can reduce the risk of developing cancer. These include:

1. Avoiding exposure to known carcinogens (such as tobacco smoke and radiation)
2. Maintaining a healthy diet and lifestyle
3. Getting regular exercise
4. Not smoking or using tobacco products
5. Limiting alcohol consumption
6. Getting vaccinated against certain viruses that are associated with cancer (such as human papillomavirus, or HPV)
7. Participating in screening programs for early detection of cancer (such as mammograms for breast cancer and colonoscopies for colon cancer)
8. Avoiding excessive exposure to sunlight and using protective measures such as sunscreen and hats to prevent skin cancer.

It's important to note that not all cancers can be prevented, and some may be caused by factors that are not yet understood or cannot be controlled. However, by taking these steps, individuals can reduce their risk of developing cancer and improve their overall health and well-being.

Also known as Burkitt's Lymphoma.

The term "lathyrism" was first used in the medical field in the early 20th century to describe this condition. It is considered a rare disease and is mostly seen in countries where sweet peas are consumed as a food source. The condition is usually diagnosed through a combination of clinical evaluation, laboratory tests, and imaging studies.

Treatment for lathyrism typically involves supportive care to manage symptoms, such as physical therapy to improve muscle strength and mobility, and medication to relieve twitching and spasticity. In severe cases, surgery may be necessary to release contracted muscles or tendons.

Prevention of lathyrism is key to avoiding the condition altogether. This can be achieved by avoiding the consumption of sweet peas and products made from them, especially in areas where the plant is known to be toxic. Education and awareness about the risks of consuming sweet peas can also help prevent the condition.

Cattle diseases refer to any health issues that affect cattle, including bacterial, viral, and parasitic infections, as well as genetic disorders and environmental factors. These diseases can have a significant impact on the health and productivity of cattle, as well as the livelihoods of farmers and ranchers who rely on them for their livelihood.

Types of Cattle Diseases

There are many different types of cattle diseases, including:

1. Bacterial diseases, such as brucellosis, anthrax, and botulism.
2. Viral diseases, such as bovine viral diarrhea (BVD) and bluetongue.
3. Parasitic diseases, such as heartwater and gapeworm.
4. Genetic disorders, such as polledness and cleft palate.
5. Environmental factors, such as heat stress and nutritional deficiencies.

Symptoms of Cattle Diseases

The symptoms of cattle diseases can vary depending on the specific disease, but may include:

1. Fever and respiratory problems
2. Diarrhea and vomiting
3. Weight loss and depression
4. Swelling and pain in joints or limbs
5. Discharge from the eyes or nose
6. Coughing or difficulty breathing
7. Lameness or reluctance to move
8. Changes in behavior, such as aggression or lethargy

Diagnosis and Treatment of Cattle Diseases

Diagnosing cattle diseases can be challenging, as the symptoms may be similar for different conditions. However, veterinarians use a combination of physical examination, laboratory tests, and medical history to make a diagnosis. Treatment options vary depending on the specific disease and may include antibiotics, vaccines, anti-inflammatory drugs, and supportive care such as fluids and nutritional supplements.

Prevention of Cattle Diseases

Preventing cattle diseases is essential for maintaining the health and productivity of your herd. Some preventative measures include:

1. Proper nutrition and hydration
2. Regular vaccinations and parasite control
3. Sanitary living conditions and frequent cleaning
4. Monitoring for signs of illness and seeking prompt veterinary care if symptoms arise
5. Implementing biosecurity measures such as isolating sick animals and quarantining new animals before introduction to the herd.

It is important to work closely with a veterinarian to develop a comprehensive health plan for your cattle herd, as they can provide guidance on vaccination schedules, parasite control methods, and disease prevention strategies tailored to your specific needs.

Conclusion
Cattle diseases can have a significant impact on the productivity and profitability of your herd, as well as the overall health of your animals. It is essential to be aware of the common cattle diseases, their symptoms, diagnosis, treatment, and prevention methods to ensure the health and well-being of your herd.

By working closely with a veterinarian and implementing preventative measures such as proper nutrition and sanitary living conditions, you can help protect your cattle from disease and maintain a productive and profitable herd. Remember, prevention is key when it comes to managing cattle diseases.

HIV (human immunodeficiency virus) infection is a condition in which the body is infected with HIV, a type of retrovirus that attacks the body's immune system. HIV infection can lead to AIDS (acquired immunodeficiency syndrome), a condition in which the immune system is severely damaged and the body is unable to fight off infections and diseases.

There are several ways that HIV can be transmitted, including:

1. Sexual contact with an infected person
2. Sharing of needles or other drug paraphernalia with an infected person
3. Mother-to-child transmission during pregnancy, childbirth, or breastfeeding
4. Blood transfusions ( although this is rare in developed countries due to screening processes)
5. Organ transplantation (again, rare)

The symptoms of HIV infection can be mild at first and may not appear until several years after infection. These symptoms can include:

1. Fever
2. Fatigue
3. Swollen glands in the neck, armpits, and groin
4. Rash
5. Muscle aches and joint pain
6. Night sweats
7. Diarrhea
8. Weight loss

If left untreated, HIV infection can progress to AIDS, which is a life-threatening condition that can cause a wide range of symptoms, including:

1. Opportunistic infections (such as pneumocystis pneumonia)
2. Cancer (such as Kaposi's sarcoma)
3. Wasting syndrome
4. Neurological problems (such as dementia and seizures)

HIV infection is diagnosed through a combination of blood tests and physical examination. Treatment typically involves antiretroviral therapy (ART), which is a combination of medications that work together to suppress the virus and slow the progression of the disease.

Prevention methods for HIV infection include:

1. Safe sex practices, such as using condoms and dental dams
2. Avoiding sharing needles or other drug-injecting equipment
3. Avoiding mother-to-child transmission during pregnancy, childbirth, or breastfeeding
4. Post-exposure prophylaxis (PEP), which is a short-term treatment that can prevent infection after potential exposure to the virus
5. Pre-exposure prophylaxis (PrEP), which is a daily medication that can prevent infection in people who are at high risk of being exposed to the virus.

It's important to note that HIV infection is manageable with proper treatment and care, and that people living with HIV can lead long and healthy lives. However, it's important to be aware of the risks and take steps to prevent transmission.

In birds, the virus can cause respiratory, gastrointestinal, and nervous system disorders. It is transmitted through contact with infected birds or contaminated feces or water. Wild birds and domestic poultry are susceptible to influenza infection. The H5N1 subtype of the virus has caused widespread outbreaks in poultry and wild birds, leading to significant economic losses and public health concerns.

Prevention methods include vaccination, biosecurity measures, and surveillance programs. Vaccines are available for chickens, turkeys, ducks, and other domesticated birds, but the effectiveness of these vaccines can be limited in protecting against certain subtypes of the virus. Biosecurity measures such as sanitation, isolation, and disinfection can help prevent the spread of the disease in poultry flocks. Surveillance programs monitor the presence of the virus in wild and domestic bird populations to detect outbreaks early and prevent the spread of the disease.

The impact of avian influenza on human health is generally minimal, but it can be severe in certain cases. Direct transmission of the virus from birds to humans is rare, but it can occur through close contact with infected birds or contaminated surfaces. Indirect transmission may occur through the handling of contaminated poultry products. People with weakened immune systems, such as young children, the elderly, and those with chronic diseases, are at a higher risk of developing severe symptoms from avian influenza.

Overall, avian influenza is an important disease in birds that can have significant economic and public health implications. Prevention and control measures are essential to minimize the impact of the disease on both bird populations and human health.

Examples of syndromes include:

1. Down syndrome: A genetic disorder caused by an extra copy of chromosome 21 that affects intellectual and physical development.
2. Turner syndrome: A genetic disorder caused by a missing or partially deleted X chromosome that affects physical growth and development in females.
3. Marfan syndrome: A genetic disorder affecting the body's connective tissue, causing tall stature, long limbs, and cardiovascular problems.
4. Alzheimer's disease: A neurodegenerative disorder characterized by memory loss, confusion, and changes in personality and behavior.
5. Parkinson's disease: A neurological disorder characterized by tremors, rigidity, and difficulty with movement.
6. Klinefelter syndrome: A genetic disorder caused by an extra X chromosome in males, leading to infertility and other physical characteristics.
7. Williams syndrome: A rare genetic disorder caused by a deletion of genetic material on chromosome 7, characterized by cardiovascular problems, developmental delays, and a distinctive facial appearance.
8. Fragile X syndrome: The most common form of inherited intellectual disability, caused by an expansion of a specific gene on the X chromosome.
9. Prader-Willi syndrome: A genetic disorder caused by a defect in the hypothalamus, leading to problems with appetite regulation and obesity.
10. Sjogren's syndrome: An autoimmune disorder that affects the glands that produce tears and saliva, causing dry eyes and mouth.

Syndromes can be diagnosed through a combination of physical examination, medical history, laboratory tests, and imaging studies. Treatment for a syndrome depends on the underlying cause and the specific symptoms and signs presented by the patient.

There are several types of melanoma, including:

1. Superficial spreading melanoma: This is the most common type of melanoma, accounting for about 70% of cases. It usually appears as a flat or slightly raised discolored patch on the skin.
2. Nodular melanoma: This type of melanoma is more aggressive and accounts for about 15% of cases. It typically appears as a raised bump on the skin, often with a darker color.
3. Acral lentiginous melanoma: This type of melanoma affects the palms of the hands, soles of the feet, or nail beds and accounts for about 5% of cases.
4. Lentigo maligna melanoma: This type of melanoma usually affects the face and is more common in older adults.

The risk factors for developing melanoma include:

1. Ultraviolet (UV) radiation exposure from the sun or tanning beds
2. Fair skin, light hair, and light eyes
3. A history of sunburns
4. Weakened immune system
5. Family history of melanoma

The symptoms of melanoma can vary depending on the type and location of the cancer. Common symptoms include:

1. Changes in the size, shape, or color of a mole
2. A new mole or growth on the skin
3. A spot or sore that bleeds or crusts over
4. Itching or pain on the skin
5. Redness or swelling around a mole

If melanoma is suspected, a biopsy will be performed to confirm the diagnosis. Treatment options for melanoma depend on the stage and location of the cancer and may include surgery, chemotherapy, radiation therapy, or a combination of these. Early detection and treatment are key to successful outcomes in melanoma cases.

In conclusion, melanoma is a type of skin cancer that can be deadly if not detected early. It is important to practice sun safety, perform regular self-exams, and seek medical attention if any suspicious changes are noticed on the skin. By being aware of the risk factors, symptoms, and treatment options for melanoma, individuals can take steps to protect themselves from this potentially deadly disease.

Some common types of fish diseases include:

1. Bacterial infections: These are caused by bacteria such as Aeromonas, Pseudomonas, and Mycobacterium. Symptoms can include fin and tail rot, body slime, and ulcers.
2. Viral infections: These are caused by viruses such as viral hemorrhagic septicemia (VHS) and infectious hematopoietic necrosis (IHN). Symptoms can include lethargy, loss of appetite, and rapid death.
3. Protozoan infections: These are caused by protozoa such as Cryptocaryon and Ichthyophonus. Symptoms can include flashing, rapid breathing, and white spots on the body.
4. Fungal infections: These are caused by fungi such as Saprolegnia and Achlya. Symptoms can include fuzzy growths on the body and fins, and sluggish behavior.
5. Parasitic infections: These are caused by parasites such as Ichthyophonus and Cryptocaryon. Symptoms can include flashing, rapid breathing, and white spots on the body.

Diagnosis of fish diseases is typically made through a combination of physical examination, laboratory tests, and observation of the fish's behavior and environment. Treatment options vary depending on the type of disease and the severity of symptoms, and can include antibiotics, antifungals, and medicated baths. Prevention is key in managing fish diseases, and this includes maintaining good water quality, providing a balanced diet, and keeping the fish in a healthy environment.

Note: The information provided is a general overview of common fish diseases and their symptoms, and should not be considered as professional medical advice. If you suspect your fish has a disease, it is recommended that you consult with a veterinarian or a qualified aquarium expert for proper diagnosis and treatment.

Mitochondrial diseases can affect anyone, regardless of age or gender, and they can be caused by mutations in either the mitochondrial DNA (mtDNA) or the nuclear DNA (nDNA). These mutations can be inherited from one's parents or acquired during embryonic development.

Some of the most common symptoms of mitochondrial diseases include:

1. Muscle weakness and wasting
2. Seizures
3. Cognitive impairment
4. Vision loss
5. Hearing loss
6. Heart problems
7. Neurological disorders
8. Gastrointestinal issues
9. Liver and kidney dysfunction

Some examples of mitochondrial diseases include:

1. MELAS syndrome (Mitochondrial Myopathy, Encephalopathy, Lactic Acidosis, and Stroke-like episodes)
2. Kearns-Sayre syndrome (a rare progressive disorder that affects the nervous system and other organs)
3. Chronic progressive external ophthalmoplegia (CPEO), which is characterized by weakness of the extraocular muscles and vision loss
4. Mitochondrial DNA depletion syndrome, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
5. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
6. Leigh syndrome, which is a rare genetic disorder that affects the brain and spinal cord.
7. LHON (Leber's Hereditary Optic Neuropathy), which is a rare form of vision loss that can lead to blindness in one or both eyes.
8. Mitochondrial DNA mutation, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
9. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
10. Kearns-Sayre syndrome, which is a rare progressive disorder that affects the nervous system and other organs.

It's important to note that this is not an exhaustive list and there are many more mitochondrial diseases and disorders that can affect individuals. Additionally, while these diseases are rare, they can have a significant impact on the quality of life of those affected and their families.

There are different types of Breast Neoplasms such as:

1. Fibroadenomas: These are benign tumors that are made up of glandular and fibrous tissues. They are usually small and round, with a smooth surface, and can be moved easily under the skin.

2. Cysts: These are fluid-filled sacs that can develop in both breast tissue and milk ducts. They are usually benign and can disappear on their own or be drained surgically.

3. Ductal Carcinoma In Situ (DCIS): This is a precancerous condition where abnormal cells grow inside the milk ducts. If left untreated, it can progress to invasive breast cancer.

4. Invasive Ductal Carcinoma (IDC): This is the most common type of breast cancer and starts in the milk ducts but grows out of them and invades surrounding tissue.

5. Invasive Lobular Carcinoma (ILC): It originates in the milk-producing glands (lobules) and grows out of them, invading nearby tissue.

Breast Neoplasms can cause various symptoms such as a lump or thickening in the breast or underarm area, skin changes like redness or dimpling, change in size or shape of one or both breasts, discharge from the nipple, and changes in the texture or color of the skin.

Treatment options for Breast Neoplasms may include surgery such as lumpectomy, mastectomy, or breast-conserving surgery, radiation therapy which uses high-energy beams to kill cancer cells, chemotherapy using drugs to kill cancer cells, targeted therapy which uses drugs or other substances to identify and attack cancer cells while minimizing harm to normal cells, hormone therapy, immunotherapy, and clinical trials.

It is important to note that not all Breast Neoplasms are cancerous; some are benign (non-cancerous) tumors that do not spread or grow.

Neuroblastoma is caused by a genetic mutation that affects the development and growth of nerve cells. The cancerous cells are often sensitive to chemotherapy, but they can be difficult to remove surgically because they are deeply embedded in the nervous system.

There are several different types of neuroblastoma, including:

1. Infantile neuroblastoma: This type of neuroblastoma occurs in children under the age of one and is often more aggressive than other types of the cancer.
2. Juvenile neuroblastoma: This type of neuroblastoma occurs in children between the ages of one and five and tends to be less aggressive than infantile neuroblastoma.
3. Adult neuroblastoma: This type of neuroblastoma occurs in adults and is rare.
4. Metastatic neuroblastoma: This type of neuroblastoma has spread to other parts of the body, such as the bones or liver.

Symptoms of neuroblastoma can vary depending on the location and size of the tumor, but they may include:

* Abdominal pain
* Fever
* Loss of appetite
* Weight loss
* Fatigue
* Bone pain
* Swelling in the abdomen or neck
* Constipation
* Increased heart rate

Diagnosis of neuroblastoma typically involves a combination of imaging tests, such as CT scans and MRI scans, and biopsies to confirm the presence of cancerous cells. Treatment for neuroblastoma usually involves a combination of chemotherapy, surgery, and radiation therapy. The prognosis for neuroblastoma varies depending on the type of cancer, the age of the child, and the stage of the disease. In general, the younger the child and the more aggressive the treatment, the better the prognosis.

There are several types of colonic neoplasms, including:

1. Adenomas: These are benign growths that are usually precursors to colorectal cancer.
2. Carcinomas: These are malignant tumors that arise from the epithelial lining of the colon.
3. Sarcomas: These are rare malignant tumors that arise from the connective tissue of the colon.
4. Lymphomas: These are cancers of the immune system that can affect the colon.

Colonic neoplasms can cause a variety of symptoms, including bleeding, abdominal pain, and changes in bowel habits. They are often diagnosed through a combination of medical imaging tests (such as colonoscopy or CT scan) and biopsy. Treatment for colonic neoplasms depends on the type and stage of the tumor, and may include surgery, chemotherapy, and/or radiation therapy.

Overall, colonic neoplasms are a common condition that can have serious consequences if left untreated. It is important for individuals to be aware of their risk factors and to undergo regular screening for colon cancer to help detect and treat any abnormal growths or tumors in the colon.

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... (BCAT), also known as branched-chain amino acid transaminase, is an aminotransferase ... Wikimedia Commons has media related to Branched-chain amino acid aminotransferase. branched-chain-amino-acid+transaminase at ... of branched-chain amino acid aminotransferases is to catalyse the synthesis or degradation of the branched chain amino acids ... Branched-chain amino acids (BCAA) are ubiquitous in many organisms, comprising 35% of all proteins and 40% of the amino acids ...
"Entrez Gene: Branched chain amino acid transaminase 1". Retrieved 2016-04-21. "BCAT1 - Branched-chain-amino-acid ... This enzyme catalyzes the reversible transamination of branched-chain alpha-keto acids (BCKAs) to the branched-chain amino ... Branched chain amino acid transaminase 1 is a protein that in humans is encoded by the BCAT1 gene. It is the first enzyme in ... July 2017). "The branched-chain amino acid transaminase 1 sustains growth of antiestrogen-resistant and ERα-negative breast ...
The branched chain amino acid:cation symporter (LIVCS) family (TC# 2.A.26) is a member of the APC superfamily. Characterized ... "2.A.26 The Branched Chain Amino Acid:Cation Symporter (LIVCS) Family". Transporter Classification Database. Braun, Peter R.; Al ... "Competitive inhibition of amino acid uptake suppresses chlamydial growth: involvement of the chlamydial amino acid transporter ... members of this family transport all three of the branched chain aliphatic amino acids (leucine (L), isoleucine (I) and valine ...
Aki K, Ogawa K, Ichihara A (1968). "Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes ... Ikeda T, Konishi Y, Ichihara A (1976). "Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of ...
Branched-chained amino acids like l-leucine, l-isoleucine, and l-valine have many functions in the central nervous system. They ... Gabapentinoids are structurally similar to the Branched-chained amino acids L-leucine, and L-isoleucine, both of which also ... ISBN 978-0-323-17080-2. Fernstrom, John D. (June 2005). "Branched-chain amino acids and brain function". The Journal of ... and the Excitatory amino acid transporter 3 (EAAT3). They are one of the few drugs that use these amino acid transporters. ...
Massey LK, Sokatch JR, Conrad RS (1976). "Branched-chain amino acid catabolism in bacteria". Bacteriol. Rev. 40 (1): 42-54. doi ... "In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain alpha-keto acid dehydrogenase ... "Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid ...
... for a polypeptide is to list its constituent amino acid residues as they occur from the amino terminus to the carboxylic acid ... Polysaccharides are linear or branched chains of sugar carbohydrates; examples include starch, cellulose and alginate. Other ... The amino acid residues are always joined by peptide bonds. Protein, though used colloquially to refer to any polypeptide, ... Polyglyconic acid Starch > (fermentation) > Lactic acid > Polylactic acid (PLA) Biomass > (fermentation) > Bioethanol > Ethene ...
"Branched-Chain Amino Acids Have Equivalent Effects to Other Essential Amino Acids on Lifespan and Aging-Related Traits in ... Restriction of the branched-chain amino acids is sufficient to extend the lifespan of Drosophila fruit flies and male mice. ... Specifically restricting consumption of the three branched-chain amino acids leucine, isoleucine and valine is sufficient to ... "Decreased Consumption of Branched-Chain Amino Acids Improves Metabolic Health". Cell Reports. 16 (2): 520-30. doi:10.1016/j. ...
... particularly branched-chain amino acids, causing a buildup of acids which are usually not present. The branched-chain amino ... Organic acids refer to the amino acids and certain odd-chained fatty acids which are affected by these disorders. The four main ... Organic acidemia, is a term used to classify a group of metabolic disorders which disrupt normal amino acid metabolism, ... Most of the organic acidemias result from defective autosomal genes for various enzymes important to amino acid metabolism. ...
... that catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. ... but also reacts significantly with other 2-methyl branched chain substrates and with short straight chain acyl-CoAs. The ... Short/branched chain acyl-CoA dehydrogenase (ACADSB) is a member of the acyl-CoA dehydrogenase family of enzymes ... ACADSB is a human gene that encodes short/branched chain specific acyl-CoA dehydrogenase (SBCAD), an enzyme in the acyl CoA ...
Dietary branched chain amino acids ameliorate injury-induced cognitive impairment. Proceedings of the National Academy of ... The synthesis of adrenocortical steroid hormones involves a chain of oxidation-reduction reactions catalyzed by a series of ... Through shared intermediates and pathways branching off those shared intermediates, the different classes of steroids are ...
May 2021). "The adverse metabolic effects of branched-chain amino acids are mediated by isoleucine and valine". Cell Metabolism ... February 2018). "Restoration of metabolic health by decreased consumption of branched-chain amino acids". The Journal of ... July 2016). "Decreased Consumption of Branched-Chain Amino Acids Improves Metabolic Health". Cell Reports. 16 (2): 520-530. doi ... or with reduced levels of branched-chain amino acids. Interestingly, methionine restriction can increase circulating FGF21 ...
Davis JM (1995). "Carbohydrates, branched-chain amino acids, and endurance: the central fatigue hypothesis". International ... Newsholme, E. A., Acworth, I. N., & Blomstrand, E. 1987, 'Amino acids, brain neurotransmitters and a functional link between ... producing lactic acid as a metabolic byproduct. Contrary to common belief, lactic acid accumulation doesn't actually cause the ... The insufficiency of energy, i.e. sub-optimal aerobic metabolism, generally results in the accumulation of lactic acid and ...
Davis JM (1995). "Carbohydrates, branched-chain amino acids, and endurance: the central fatigue hypothesis". International ... Newsholme, E. A., Acworth, I. N., & Blomstrand, E. 1987, 'Amino acids, brain neurotransmitters and a functional link between ... producing lactic acid as a metabolic byproduct. Contrary to common belief, lactic acid accumulation doesn't actually cause the ... It was once believed that lactic acid build-up was the cause of muscle fatigue. The assumption was lactic acid had a "pickling ...
... functions in catabolism of the branched-chain amino acid valine. ACAD8 functions as a homotetramer and has an overall ... ACAD8 is an isobutyryl-CoA dehydrogenase that functions in the catabolism of branched-chain amino acids including valine, and ... function to catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branched-chain amino acids ... "Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new ...
Branched-chain amino acids, Proteinogenic amino acids, Glucogenic amino acids, Essential amino acids, Isopropyl compounds, ... like other branched-chain amino acids, is synthesized by plants, but not by animals. It is therefore an essential amino acid in ... April 2016). "A branched-chain amino acid metabolite drives vascular fatty acid transport and limits insulin resistance". ... Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase Valine aminotransferase Like other branched-chain amino acids, the ...
Proteinogenic amino acids, Glucogenic amino acids, Ketogenic amino acids, Branched-chain amino acids, Essential amino acids, ... or fatty acids. Isoleucine, like other branched-chain amino acids, is associated with insulin resistance: higher levels of ... Branched Chain Amino Acids in Clinical Nutrition. Vol. 1. ISBN 978-1-4939-1923-9. Lynch CJ, Adams SH (December 2014). "Branched ... May 2021). "The adverse metabolic effects of branched-chain amino acids are mediated by isoleucine and valine". Cell Metabolism ...
Both enzymes are needed for plants to make branched-chain amino acids. Many other enzymes are inhibited by herbicides, ... "Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops". Amino Acids. 30 (2): 195-204. doi:10.1007/ ... These electrophilic groups react with amino acid side chains to form covalent adducts. The residues modified are those with ... side chains containing nucleophiles such as hydroxyl or sulfhydryl groups; these include the amino acids serine (that reacts ...
The branched-chain amino acids leucine and valine may have potential in inhibiting overexpression of protein breakdown pathways ... Eley HL, Russell ST, Tisdale MJ (October 2007). "Effect of branched-chain amino acids on muscle atrophy in cancer cachexia". ... The amino acid glutamine has been used as a component of oral supplementation to reverse cachexia in people with advanced ... Administration of exogenous amino acids have been investigated to serve as a protein-sparing metabolic fuel by providing ...
Sep 2015). "Regulation of indole-3-acetic acid biosynthesis by branched-chain amino acids in Enterobacter cloacae UW5". FEMS ... Enterobacter cloacae can produce IAA, from aromatic and branched-chain amino acids. Fungi can form a fungal mantle around roots ... 5, p. 654 Fox, Sidney W.; Bullock, Milon W. (1951). "Synthesis of Indoleacetic Acid from Glutamic Acid and a Proposed Mechanism ... 4-dichlorophenoxyacetic acid (2,4-D) and 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), both phenoxy herbicides and analogs of ...
Specifically, two essential branched-chain amino acids (leucine and isoleucine) are metabolized differently.[citation needed] ...
Holeček M (August 2020). "Branched-Chain Amino Acids and Branched-Chain Keto Acids in Hyperammonemic States: Metabolism and as ... Branched-chain amino acids, leucine, isoleucine and valine are commonly used for their muscle fueling properties and relief of ... The improvement in muscle recovery is associated with the branched chain amino acids (BCAAs) found in pre-workout, particularly ... Fedewa MV, Spencer SO, Williams TD, Becker ZE, Fuqua CA (November 2019). "Effect of branched-Chain Amino Acid Supplementation ...
Degradation of branched-chain ketogenic amino acids such as valine, leucine, and isoleucine occurs. These amino acids are ... The cycle produces a new fatty acid chain with two fewer carbons and acetyl-CoA as a byproduct. In Cellular Respiration Citric ... At low glucose levels, the production of acetyl-CoA is linked to β-oxidation of fatty acids. Fatty acids are first converted to ... Unlike free fatty acids, ketone bodies can cross the blood-brain barrier and are therefore available as fuel for the cells of ...
"Lactating Porcine Mammary Tissue Catabolizes Branched-Chain Amino Acids for Glutamine and Aspartate Synthesis". The Journal of ... Side branches form from the primary ducts and begin to fill the mammary fat pad. Ductal development decreases with the arrival ... When side branches develop, it is a much more "pushing-forward" working process including extending through myoepithelial cells ... Estrogen promotes branching differentiation, whereas in males testosterone inhibits it. A mature duct tree reaching the limit ...
Pátek M (2007). "Branched-chain amino acids.". Amino Acid Biosynthesis: Pathways, Regulation and Metabolic Engineering. ... The ilvGMEDA operon encodes the ilvGM (ALS II) pair as well as a branched-chain-amino-acid transaminase (ilvE), dihydroxy-acid ... the branched-chain amino acids. The ilvBNC operon encodes the ilvBN (ALS I) pair and a ketol-acid reductoisomerase (ilvC). It ... ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). A human ...
... isoleucine is measured relative to other amino acids to determine if the newborn has a high level of branched-chain amino acids ... Once the newborn is 2-3 days old the blood concentration of branched-chain amino acids like leucine is greater than 1000 μmol/L ... Early detection, diet low in branched-chain amino acids, and close monitoring of blood chemistry can lead to a good prognosis ... The levels of these branched chain amino acids will become elevated and lead to the symptoms associated with MSUD. Glutamate ...
Proteinogenic amino acids, Ketogenic amino acids, Branched-chain amino acids, Essential amino acids, E-number additives). ... hydrophobic amino acid valine also includes the initial part of this pathway. Leucine is a branched-chain amino acid (BCAA) ... July 2016). "Branched-chain amino acid restriction in Zucker-fatty rats improves muscle insulin sensitivity by enhancing ... Like valine and isoleucine, leucine is a branched-chain amino acid. The primary metabolic end products of leucine metabolism ...
Also, Isovaleryl-coenzyme A is an intermediate in the metabolism of branched-chain amino acids. Isovaleric acid is a major ... 3-Methylbutanoic acid, also known as β-methylbutyric acid or more commonly isovaleric acid, is a branched-chain alkyl ... It is classified as a short-chain fatty acid. Like other low-molecular-weight carboxylic acids, it has an unpleasant odor. The ... The acid has been used to synthesize β-hydroxyisovaleric acid - otherwise known as β-hydroxy β-methylbutyric acid - via ...
Amari, Shoichiro; Shahrook, Sadequa; Namba, Fumihiko; Ota, Erika; Mori, Rintaro (2 October 2020). "Branched-chain amino acid ... and branched-chain amino acids. Conversely, there is some indication that preterm babies who cannot breastfeed may do better if ... Preconceptional intake of folic acid is recommended to reduce birth defects. There is also some evidence that folic acid ... there is some weak evidence that the infant may benefit from including amino acids and fats in the intravenous nutrition at a ...
... which is then transaminated to form an amino acid. Amino acids are made into proteins by being joined in a chain of peptide ... the polysaccharides produced can have straight or branched structures. The polysaccharides produced can have structural or ... lack all amino acid synthesis and take their amino acids directly from their hosts. All amino acids are synthesized from ... amino acids can be linked in varying sequences to form a huge variety of proteins. Proteins are made from amino acids that have ...
Metabolites of nonsulfur amino acid constituents (simple and branched-chain hydrocarbons) such as ethylene (produced by mycelia ... Fatty acid-derived volatiles (C8-alcohols and aldehydes with a characteristic fungal odor, such as 1-octen-3-ol and 2-octenal ... The former is derived from linoleic acid, and produced by mature white truffle T. borchii. Thiophene derivatives appear to be ...
These chains may be linear or branched, and different regulatory signals may be sent by differences in the length and branching ... which has 76 amino acid residues arranged into a "beta-grasp" protein fold consisting of a five-strand antiparallel beta sheet ... Although not all UBL families are known to form chains, SUMO, NEDD8, and URM1 chains have all been experimentally detected. ... Ubiquitin is capable of forming polymeric chains, with additional ubiquitin molecules covalently attached to the first, which ...
In fatty acid (FA) metabolism, long chain fatty acids in the cytosol cannot cross the mitochondrial membrane because they are ... "Branches and Representative Offices". Grindeks. Archived from the original on 10 March 2016. Retrieved 9 March 2016. "AS " ... It is a structural analogue of γ-butyrobetaine, with an amino group replacing the C-4 methylene of γ-butyrobetaine. γ- ... Long chain FA are first activated via esterification with coenzyme A to produce a fatty acid-coA complex which can then cross ...
... a derivative of amino acid beta-alanine), oil of lemon eucalyptus (OLE, a natural compound) and OLE's active ingredient para- ... Polymerase chain reaction (PCR) tests for Lyme disease have also been developed to detect the genetic material (DNA) of the ... eds.). Baron's Medical Microbiology (4th ed.). Univ of Texas Medical Branch. ISBN 978-0-9631172-1-2. PMID 21413339. Archived ... The spirochetes may also induce host cells to secrete quinolinic acid, which stimulates the NMDA receptor on nerve cells, which ...
... to be used for locomotion as well as prey detection on the seafloor via chemoreception highly sensitive to the amino acids ... There are 9 or 10 branched rays in the caudal fin. The smallest species is the spotwing gurnard (Lepidotrigla spiloptera) which ... ISBN 0-12-547665-5. Petersen, Jarrod C.; Ramsay, Jason B. (2020-09-15). "Walking on chains: the morphology and mechanics behind ...
... that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, ... Baker ME, Billheimer JT, Strauss JF (1992). "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier ... Huang H, Ball JM, Billheimer JT, Schroeder F (1999). "The sterol carrier protein-2 amino terminus: a membrane interaction ... 1997). "The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic ...
... may refer to: Branched-chain amino acid Belgian Civil Aviation Authority Bermuda Civil Aviation Authority British Columbia ...
The α and β-tubulin subunits are ~50% identical at the amino acid level, and both have a molecular weight of approximately 50 ... TTL3 and 8 add the initial branching glycine, while TTL10 lengthens the polyglycine chain. Tubulin is also known to be ... These long chains (protofilaments) now gradually accumulate next to each other so that a tube-like structure is formed, which ... Enzymes related to TTL add the initial branching glutamate (TTL4,5 and 7), while other enzymes that belong to the same family ...
... a TPP-dependent enzyme responsible for the biosynthesis of branched chain amino acids in certain organisms. Sequence alignments ... which has raised questions about whether TDP must be deprotonated by a basic amino acid at a second site away from the ... Dailey FE, Cronan JE (February 1986). "Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis ... Chipman D, Barak Z, Schloss JV (June 1998). "Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and ...
Barbituric acid is the parent compound of barbiturate drugs although barbituric acid itself is not pharmacologically active. ... Generally alkyl branching in position 5 means less lipid solubility and less activity. Unsaturation show less activity in ... Analogues 5 and 6 (Figure 10) are weak modulators of GABAA receptor function because the flexible side chains in these ... pyrimidinone and 3-amino-1,2,4-triazole derivatives". Bioorganic & Medicinal Chemistry. 23 (3): 480-7. doi:10.1016/j.bmc. ...
The DLD homodimer functions as the E3 component of the pyruvate, α-ketoglutarate, α-adipate and branched-chain amino acid- ... Several amino acids within the catalytic pocket have been identified as important to DLD function, including R281 and N473. ... January 2008). "The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase". Journal of Biomedical Science. ... January 2008). "The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase". Journal of Biomedical Science. ...
... together with contributions from medium chain fatty acids (caprylic and heptanoic acids), lactate, acetate, and possibly amino ... The brain is also the most important organ studied in psychiatry, the branch of medicine that works to study, prevent, and ... ISBN 978-0-19-514008-8. McGeer, PL; McGeer, EG (1989). "Chapter 15, Amino acid neurotransmitters". In G. Siegel; et al. (eds ... Although the same basic components are present in all vertebrate brains, some branches of vertebrate evolution have led to ...
Bergeron, M; Layrargues, GP; Butterworth, RF (September 1989). "Aromatic and branched-chain amino acids in autopsied brain ... "The role of plasma amino acids in hepatic encephalopathy". Surgery. 78 (3): 276-90. PMID 807982. Loock, J; Stange, J; Mitzner, ... "Albumin dialysis improves hepatic encephalopathy and decreases circulating phenolic aromatic amino acids in patients with ... "Removal of bile acids by two different extracorporeal liver support systems in acute-on-chronic liver failure". ASAIO Journal. ...
α-KIC is produced in one of the first steps of the pathway by branched-chain amino acid aminotransferase by transferring the ... HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB ... along with other branched-chain amino acids. Derivatives of α-KIC have been studied in humans for their ability to improve ... which leads to a buildup of branched-chain alpha-keto acids, including α-KIC and HMB. These keto-acids build up in the liver, ...
Branched and aliphatic amino acids (valine and isoleucine) prove to generate the most stable aminoacyl-tRNAs upon their ... In order to prevent translational errors, in which the wrong amino acid is incorporated into the polypeptide chain, evolution ... the adenylation of the amino acid, which forms aminoacyl-AMP: Amino Acid + ATP → Aminoacyl-AMP + PPi Second, the amino acid ... Instead, amino acids must be "charged" or aminoacylated with a tRNA to form their respective aa-tRNA. Every amino acid has its ...
Detection of convergent and parallel evolution at the amino acid sequence level Archived 2016-03-03 at the Wayback Machine. Mol ... A number of examples of parallel evolution are provided by the two main branches of the mammals, the placentals and marsupials ... Again, in the image above, note that since serine and threonine possess similar structures with an alcohol side chain, the ... if the amino acids were grouped by similarity instead of being considered individually. As another example, if genes in two ...
α-Acetolactic acid is a precursor in the biosynthesis of the branched chain amino acids valine and leucine. α-Acetolactic acid ... Wood, B. J. B.; Holzapfel, W. H. (1995). "Carbohydrate Metabolism". The Lactic Acid Bacteria: The genera of lactic acid ... α-Acetolactic acid can also be decarboxylated by alpha-acetolactate decarboxylase to produce acetoin. The name α-acetolactate ... ISBN 978-0-7514-0215-5. Marth, E. H.; Steele, J. L. (2001). "Genetics of Lactic acid bacteria". Applied dairy microbiology. Vol ...
Takanaga H, Mackenzie B, Peng JB, Hediger MA (Nov 2005). "Characterization of a branched-chain amino-acid transporter SBAT1 ( ... Sodium-dependent neutral amino acid transporter B(0)AT2 is a protein that in humans is encoded by the SLC6A15 gene. SLC6A15 ... Zaia KA, Reimer RJ (Mar 2009). "Synaptic Vesicle Protein NTT4/XT1 (SLC6A17) Catalyzes Na+-coupled Neutral Amino Acid Transport ... "Entrez Gene: solute carrier family 6 (neutral amino acid transporter)". Farmer MK, Robbins MJ, Medhurst AD, Campbell DA, ...
... reacts readily with amino acids that have amino group side-chains, with the chlorine from HClO displacing a ... Stroman, D. W; Mintun, K; Epstein, A. B; Brimer, C. M; Patel, C. R; Branch, J. D; Najafi-Tagol, K (2017). "Reduction in ... The reaction of aqueous hypochlorous acid with alpha-amino acids and dipeptides". Biochimica et Biophysica Acta. 313 (1): 170- ... The first reaction yields sulfenic acid (R-SOH) then sulfinic acid (R-SO2H) and finally R-SO3H. Sulfenic acids form disulfides ...
The hydrophobic chains belong either to: two fatty acids (FA) - in the case of the phosphoglycerides, or one FA and the ... Sphingosine is an amino alcohol that contains a long, unsaturated hydrocarbon chain. In sphingomyelin and glycolipids, the ... More complex glycolipids, such as gangliosides, contain a branched chain of as many as seven sugar residues. The best known ... due to the abundance of 18-carbon fatty acyl chains with three double bonds, linolenic acid, as has been revealed by 13-C NMR ...
Bateson, G. (1955). "How the Deviant Sees His Society". In Branch, C.H.H. (ed.). The Epidemiology of Mental Health: An ... Mental process requires circular (or more complex) chains of determination. In mental process the effects of difference are to ... Conference on d-Lysergic Acid Diethylamide (LSD-25). Josiah Macy, Jr. Foundation. pp. 10, 19, 25, 28, 35-36, 37, 39-40, 48, 51 ... Bateson, G. (1 May 1960). "Minimal Requirements for a Theory of Schizophrenia". AMA Archives of General Psychiatry. 2 (5): 477- ...
The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa in muscle cells. ... In addition, the enzyme transferase shifts a block of 3 glucosyl residues from the outer branch to the other end, and then a α1 ... The enzyme is specific to α1-4 chains, as the molecule contains a 30-angstrom-long crevice with the same radius as the helix ... Residues 397-437 form this structure, which allows the protein to covalently bind to the glycogen chain a full 30 Å from the ...
... branched chain fatty acids, bile acid intermediates (in the liver), D-amino acids, and polyamines, the reduction of reactive ... In animal cells, the long fatty acids are converted to medium chain fatty acids, which are subsequently shuttled to ... of very-long-chain and polyunsaturated fatty acids biosynthesis of plasmalogens conjugation of cholic acid as part of bile acid ... such as D-amino acid oxidase and uric acid oxidase. However the last enzyme is absent in humans, explaining the disease known ...
... dehydrogenase enzyme reaction in the neurons is transaminated into α-ketoisocaproate to form the branched-chain amino acid ... The amino acid moves in the opposite direction of glutamine. In the opposite direction of the amino acid, a corresponding ... Once the vesicle is released, glutamate is removed from the synaptic cleft by excitatory amino-acid transporters (EAATs). This ... amino acids) might be employed. Certainly, ammonia can diffuse across lipid membranes, and it has been shown that ammonia can ...
The primary bile acids cholic acid (CA) and chenodeoxycholic acid (CDCA) are synthesized in the liver and undergo conjugation ... which inhibits myosin light chain phosphatase (MLCP), and in turn, increases myosin light chain phosphorylation by MLC kinase ... Clinically, diagnosis generally requires a 1:40 or greater titer of anti-mitochondrial antibody (AMA) against PDC-E2 and ... similar to the terminal branches of a tree. The canaliculi join each other to form larger and larger structures, sometimes ...
... whereas the function of other lysine chains, mixed chains, branched chains, M1-linked linear chains, and heterologous chains ( ... The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.6 kDa. Key features include its C- ... Branched ubiquitin chains containing multiple linkage types can be formed. The function of these chains is unknown. Differently ... Lysine 48-linked chains were the first identified and are the best-characterised type of ubiquitin chain. K63 chains have also ...
Patients with BCKDK deficiency have low levels of branched chain amino acids (BCAA) in their organism due to accelerated ... Branched-chain keto acid dehydrogenase kinase deficiency (BCKDK deficiency) is a disease resulting from mutations of the BCKDK ... Branched-chain keto acid dehydrogenase kinase deficiency - a record in OMIM (Articles with short description, Short description ... branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral deficit in two pediatric unrelated ...
Differential effects of insulin-induced Hypoglycaemia on the plasma branched-chain and non-branched-chain amino acid ... Decreased branched-chain amino acids and elevated fatty acids during antecedent hypoglycemia in type 1 diabetes Rui She 1 2 , ... Decreased branched-chain amino acids and elevated fatty acids during antecedent hypoglycemia in type 1 diabetes Rui She et al. ... On day 1, concentrations of the branched-chain amino acids, leucine (p=3.8×10-3) and isoleucine (p=2.2×10-3), decreased during ...
Explored promoting multi-disciplinary research on branched chain amino acids (BCAA) actions and metabolism over a broad ... Branched-chain Amino Acids in Exercise. Stuart Phillips, Ph.D., McMaster University. 10:40 a.m. - 11:15 a.m.. BCAA and Recovery ... Emerging Role of Branched-Chain Amino Acids in Human Diseases. May 25. - 26, 2017. Contacts ... The branched chain amino acids (BCAA) leucine, isoleucine and valine are essential nutrients, required for normal growth and ...
GPRC5C Drives Branched-Chain Amino Acid Metabolism in Leukemogenesis Yu Wei Zhang 1 , Talia Velasco-Hernandez 2 , Julian Mess 3 ... GPRC5C Drives Branched-Chain Amino Acid Metabolism in Leukemogenesis Yu Wei Zhang et al. Blood Adv. 2023. . ... which resulted in an altered metabolic state with increased levels of intracellular branched-chain amino acids (BCAAs). This ...
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Branched-chain amino acids (BCAA) and carbohydrate (CHO) are commonly recommended postexercise supplements. However, no study ... Effect of infused branched-chain amino acids on muscle and whole-body amino acid metabolism in man. . Clinical Science,. 79. ( ... Effect of infused branched-chain amino acids on muscle and whole-body amino acid metabolism in man. . Clinical Science,. 79. ( ... Branched-chain amino acid and branched-chain ketoacid ingestion increases muscle protein synthesis rates in vivo in older ...
Life Extension Branched Chain Amino Acids (BCAAs) contains L-leucine, L-isoleucine, and L-valine. BCAAs aid in a healthy ... Life Extension Branched Chain Amino Acids supplement is comprised of three essential branched chain amino acids (BCAAs) - L- ... Benefits and Effects of Branched Chain Amino Acids. The three branched chain amino acids (BCAAs) L-valine, L-leucine, and L- ... Life Extension Branched Chain Amino Acids, Metabolism & Muscle Formation Aid, 90 Capsules. List Price: $20.00. Our Price: $ ...
Branched Chain Amino Acids Market, By Type (2:1:1 and Others), By End-use (Sports Nutrition, Pharmaceutical, and Others), and ... Branched Chain Amino Acids Market. Branched Chain Amino Acids Market, By Type (2:1:1 and Others), By End-use (Sports Nutrition ...
Circulating branched-chain amino acids (BCAAs) are linked with mortality in population-based studies. Whether they also predict ... 418-P: The Branched-Chain Amino Acids Valine and Leucine Predict All-Cause Mortality in Cardiovascular Disease Patients ... Circulating branched-chain amino acids (BCAAs) are linked with mortality in population-based studies. Whether they also predict ... The Branched-Chain Amino Acids Valine and Leucine Predict All-Cause Mortality in Cardiovascular Disease Patients Independently ...
Performance Hydration Thrive Recovery Branch Chain Amino Acid Supplement ... Performance Hydration Thrive Recovery Branch Chain Amino Acid Supplement CamelBak Performance Hydration Thrive Recovery Branch ... THRIVE contains the critical branch chain amino acids and glutamine to support the repair and building of elan muscle while ...
"Branched-chain amino acid enriched supplements as therapy for liver disease",. abstract = "Altered amino acid metabolism is a ... Branched-chain amino acid enriched supplements as therapy for liver disease. In: Journal of Nutrition. 2006 ; Vol. 136, No. 1. ... Charlton M. Branched-chain amino acid enriched supplements as therapy for liver disease. Journal of Nutrition. 2006 Jan;136(1): ... Charlton, M. (2006). Branched-chain amino acid enriched supplements as therapy for liver disease. Journal of Nutrition, 136(1 ...
NMR; branched chain amino acids; grape polyphenols; human trials; metabolism; metabolomics; obesity; overfeeding ... Grape polyphenols decrease circulating branched chain amino acids in overfed adults. Grape polyphenols decrease circulating ... Changes in plasma levels of many metabolic markers, including branched chain amino acids (BCAA), ketone bodies and glucose in ... branched chain amino acids in overfed adults. Bartova, Simona; Madrid-Gambin, Francisco; Fernández, Luis; Carayol, Jerome; ...
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BCAA (branched-chain amino acids) supplements are by gym goers and fitness professional who engage in intense physical activity ... Get ready to fuel your workouts with Royalty BCAA! Our 2:1:1 combination of branched-chain amino acids is intended to support ... BCAAs are made up of three amino acids: leucine, isoleucine, and valine. The ratio of these amino acids can vary between brands ... Royalty BCAA has essential amino acids that the body cannot produce on its own, making it necessary to get them through the ...
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... * 95 Lei. *Contine L-Glutamina si alti aminoacizi esentiali pentru sustinerea ... Glutamina este un aminoacid semiesential, care poate fi sintetizat de organism, dar in perioade de stres, traume, efort ...
BCAAs are a source of amino acids involved in muscle protein synthesis. Typical uses include: Protecting muscle mass while on ... BCAA (Branched Chain Amino Acids). $ 28.00 BCAAs are a source of amino acids involved in muscle protein synthesis. Typical ...
GO:0015803: branched-chain amino acid transport (Biological process). The directed movement of branched-chain amino acids into ... Branched-chain amino acids are amino acids with a branched carbon skeleton without rings. [GOC:ai, GOC:bf] ...
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The branched chain amino acids Leucine, Isoleucine and Valine are three of the eight essential amino acids that the human body ... These amino acids cannot be synthesized in the liver. Ingredients ... are 3 essential amino acids which are abundant in muscles. ... Branched Chain Amino Acids (BCAAs) are 3 essential amino acids ... Branched Chain Amino Acids (BCAAs) are 3 essential amino acids which are abundant in muscles. The branched chain amino acids ...
Branched Chain. Attributes. Strength. 213. Dexterity. 411. Vitality. 2851. Intelligence. 410. Mind. 2974. ...
... the branched-chain amino acids valine, isoleucine, and leucine (VIL), and a mixture of all large neutral amino acids (LNAA), ... Branched-chain amino acids: valine, leucine, isoleucin (VIL). Oral VIL treatment was designed to inhibit influx of Phe into the ... why these three branched-chain amino acids were chosen and other LNAAs were neglected.The rate of protein synthesis depends on ... Pietz J, Kreis R, Rupp A, Mayatepek E, Rating D, Boesch C, et al.Large neutral amino acids block phenylalanine transport into ...
... the benefits of amino acid supplements are largely unproven, and what health benefits they may offer come with side effects. ... Hypertension: "Concentration of Branched-Chain Amino Acids Is a Strong Risk Marker for Incident Hypertension" ... Supplement-makers claim that branched-chain amino acids (BCAAs) - which include leucine, isoleucine and valine - are energy- ... Whats left once protein is digested? Amino acids. And as the U.S. National Library of Medicine explains, amino acids are used ...
支鏈胺基酸 Branched Chain Amino Acids (BCAAs). *運動後喝水是最好嗎? ...
Branched Chain Amino Acids (BCAAs) from Well Fit Protein Shops will reduce fatigue, accelerate recovery, reduce muscle soreness ... Branched Chain Amino Acids (BCAAs) will help reduce fatigue, accelerate your recovery, reduce muscle soreness and improve the ...
Branch Chain Amino Acids (BCAAs). BCAAs trigger an insulin response and thus stop autophagy…and the fast. That said, many ... Theres evidence that glycine-the most prominent amino acid in collagen-can inhibit autophagy, but it was a convoluted animal ...
Branched-chain amino acids (BCAAs) are three essential amino acids (leucine, isoleucine, and valine) that support strength, ... What do the branched-chain amino acids (BCAAs) in Re-Lyte Muscle Recovery Capsules do?. BCAAs can support the creation of ... Article: 5 Proven Benefits of BCAAs (Branched-Chain Amino Acids). *Article: Health benefits of BCAAs ...
"Branched Chain Amino Acids are marketed to help you improve muscle growth and strength. Amino acids are the building blocks ... It wont hurt you to take branched chain amino acid supplements, it just may be expensive and unnecessary and I suggest making ... Still, companies that sell branched chain amino acid supplements often cite research that uses subjects whose diets lack ... and so taking a branched chain amino acid supplement likely will not improve your performance or muscle growth if you simply ...
  • Life Extension Branched Chain Amino Acids supplement is comprised of three essential branched chain amino acids (BCAAs) - L-leucine, L-isoleucine, and L-valine. (drvitaminsolutions.com)
  • The three branched chain amino acids (BCAAs) L-valine, L-leucine, and L-isoleucine are integral components of protein synthesis within liver cells and muscle cells. (drvitaminsolutions.com)
  • Circulating branched-chain amino acids (BCAAs) are linked with mortality in population-based studies. (diabetesjournals.org)
  • Altered amino acid metabolism is a hallmark of liver disease, characterized by low levels of circulating BCAAs and elevated levels of circulating aromatic amino acids, and methionine. (elsevier.com)
  • BCAAs are made up of three amino acids: leucine, isoleucine, and valine. (royaltysupps.com)
  • Supplement-makers claim that branched-chain amino acids (BCAAs) - which include leucine, isoleucine and valine - are energy-boosters, ODS notes. (livestrong.com)
  • However, con- sumption of essential amino acids, particularly leucine and other branched- chain amino acids (BCAAs), along with resistance exercise has been shown to improve muscle synthesis.4, 5 Figure 1 provides an overview of contrast- ing lifestyles that impact healthy aging. (nih.gov)
  • Branched Chain Amino Acids (BCAAs) will help reduce fatigue, accelerate your recovery, reduce muscle soreness and improve the use of fat for energy during exercise. (wellfitproteinshops.com)
  • What do the branched-chain amino acids (BCAAs) in Re-Lyte Muscle Recovery Capsules do? (redmond.life)
  • Branched-chain amino acids (BCAAs) are three essential amino acids (leucine, isoleucine, and valine) that support strength, speed, endurance, and muscle recovery. (redmond.life)
  • The branched chain amino acids (BCAA) leucine, isoleucine and valine are essential nutrients, required for normal growth and protein balance. (nih.gov)
  • Branched-chain amino acids (BCAA) and carbohydrate (CHO) are commonly recommended postexercise supplements. (humankinetics.com)
  • Changes in plasma levels of many metabolic markers, including branched chain amino acids (BCAA), ketone bodies and glucose in both placebo as well as upon polyphenol intervention were identified in the Lyon study. (bvsalud.org)
  • BCAA (branched-chain amino acids) supplements are by gym goers and fitness professional who engage in intense physical activity or workouts. (royaltysupps.com)
  • Royalty BCAA has essential amino acids that the body cannot produce on its own, making it necessary to get them through the diet or supplements. (royaltysupps.com)
  • BACKGROUND: Branched-chain amino acids (BCAA: leucine, isoleucine, and valine) are essential amino acids involved in biological functions of brain development and recently linked with autism. (nih.gov)
  • 27. Branched-chain amino acids (BCAA) administration increases autophagy and the autophagic pathway in brain tissue of rats submitted to a Maple Syrup Urine Disease (MSUD) protocol. (nih.gov)
  • Contains 3 essential amino acids, L-valine, L-leucine and isoleucine. (nutritioncompany.eu)
  • The branched chain amino acids Leucine, Isoleucine and Valine are three of the eight essential amino acids that the human body must receive in food. (naturalvibe.ca)
  • Amino acids are the 'building blocks' of protein, and there are three that are classified as branched chain based on their chemical structure: leucine, isoleucine and valine. (eatthis.com)
  • Leucine and isoleucine are perhaps the more important amino acids in this mix, as they are important for stimulation of muscle protein synthesis and glucose uptake uptake by muscles. (eatthis.com)
  • Maple syrup urine disease (MSUD), also known as branched-chain ketoaciduria, is an aminoacidopathy due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. (medscape.com)
  • Maple syrup urine disease is caused by a deficiency of the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex, which catalyses the decarboxylation of the alpha-keto acids of leucine, isoleucine, and valine to their respective branched-chain acyl-CoAs. (medscape.com)
  • 7. Effects of branched-chain-enriched amino acids and insulin on forearm leucine kinetics. (nih.gov)
  • The protein complex is essential for breaking down the amino acids leucine, isoleucine, and valine, which are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. (nih.gov)
  • Americana Whey is a source of essential branched-chain amino acids (BCASS) leucine, isoleucine, and valine. (nih.gov)
  • Valinemia is an inherited disorder that increases levels of the amino acid valine in the blood. (nih.gov)
  • Individuals with ALS or disorders impairing the metabolism of branched chain amino acids should not use this product. (drvitaminsolutions.com)
  • 9. Trauma metabolism and the heart: studies of heart and leg amino acid flux after cardiac surgery. (nih.gov)
  • 12. Amino acid metabolism in patients with severe burns. (nih.gov)
  • 23. Branched-Chain Amino Acids and Brain Metabolism. (nih.gov)
  • 31. Branched-chain amino acids sustain pancreatic cancer growth by regulating lipid metabolism. (nih.gov)
  • 37. Tissue of origin dictates branched-chain amino acid metabolism in mutant Kras-driven cancers. (nih.gov)
  • Branched-chain amino acid metabolism: from rare Mendelian diseases to more common disorders. (nih.gov)
  • [ 7 ] The branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex was purified and characterized in 1978. (medscape.com)
  • Oyarzabal A, Martinez-Pardo M, Merinero B, Navarrete R, Desviat LR, Ugarte M, Rodriguez-Pombo P. A novel regulatory defect in the branched-chain alpha-keto acid dehydrogenase complex due to a mutation in the PPM1K gene causes a mild variant phenotype of maple syrup urine disease. (nih.gov)
  • Charlton, M 2006, ' Branched-chain amino acid enriched supplements as therapy for liver disease ', Journal of Nutrition , vol. 136, no. 1, pp. 295S-298S. (elsevier.com)
  • The composition of GAT Amino GT contains the 1 energy supplements, 1 electrolytes, 1 hydration supplements, 2 vitamins, 1 minerals. (vsprotein.com)
  • But does that mean amino acid supplements are good for your health? (livestrong.com)
  • Who Needs Amino Acid Supplements? (livestrong.com)
  • Amino acid supplements are sold with the promise of doing many things," says Connie Diekman, MEd, RD , a St. Louis, Missouri-based food and nutrition consultant, former president of the American Dietetic Association and former director of university nutrition at Washington University in St. Louis. (livestrong.com)
  • But if amino acid supplements are on your radar, Diekman strongly advises first consulting with a registered dietitian or certified specialist in sports dietetics (CSSD). (livestrong.com)
  • It won't hurt you to take branched chain amino acid supplements, it just may be expensive and unnecessary and I suggest making sure you are eating enough protein throughout the day. (eatthis.com)
  • International surveys found that two-thirds of 3,887 adult and adolescent elite track and field athletes participating in world-championship competitions took one or more dietary supplements containing such ingredients as vitamins, minerals, creatine, caffeine, and amino acids [ 4 ]. (nih.gov)
  • A survey of 106,698 U.S. military personnel in 2007-2008 found that 22.8% of the men and 5.3% of the women reported using bodybuilding supplements, such as creatine and amino acids, and 40.5% of the men and 35.5% of the women reported using energy supplements that might contain caffeine and/or energy-enhancing herbs [ 8 ]. (nih.gov)
  • What's important to note is that a diet that is already adequate in protein provides enough of these amino acids, and so taking a branched chain amino acid supplement likely will not improve your performance or muscle growth if you simply eat enough protein throughout the day. (eatthis.com)
  • BCAA's are a source of amino acids involved in muscle protein synthesis. (smfmwellness.net)
  • NOW® Branched Chain Amino Acids (BCAA's) are 3 essential amino acids which are abundant in muscles. (naturalvibe.ca)
  • Our 2:1:1 combination of branched-chain amino acids is intended to support muscle growth, protein synthesis, and recovery. (royaltysupps.com)
  • You can meet your amino acid needs through diet if you consume plenty of healthy, high-protein foods. (livestrong.com)
  • And amino acids are the building blocks of protein. (livestrong.com)
  • 10. Response of muscle protein and glutamine kinetics to branched-chain-enriched amino acids in intensive care patients after radical cancer surgery. (nih.gov)
  • Maple syrup urine disease is an inherited disorder in which the body is unable to process certain protein building blocks (amino acids) properly. (nih.gov)
  • 21. Plasma amino acid and urine organic acid profiles of Filipino patients with maple syrup urine disease (MSUD) and correlation with their neurologic features. (nih.gov)
  • 29. [Metabolic disorders of amino acids due to enzyme mutation--branched-chain amino acids]. (nih.gov)
  • It also contains omega 6 and 9 fatty acids which are inflammatory. (eatthis.com)
  • It's best to take omega 3 fatty acids - known as fish oils - for the anti-inflammatory and pro-cognition benefits of taking epa and dha. (eatthis.com)
  • There's evidence that glycine-the most prominent amino acid in collagen-can inhibit autophagy, but it was a convoluted animal study where inhibiting autophagy with large doses of glycine after brain injury actually improved outcomes. (marksdailyapple.com)
  • [ 4 ] In 1960, Dancis et al demonstrated that the enzymatic defect in maple syrup urine disease was at the level of the decarboxylation of the branched-chain amino acids. (medscape.com)
  • [ 5 ] Snyderman et al initiated the first successful dietary treatment of maple syrup urine disease by restricting oral intake of branched-chain amino acids. (medscape.com)
  • 22. Maple syrup urine disease: clinical, EEG, and plasma amino acid correlations with a theoretical mechanism of acute neurotoxicity. (nih.gov)
  • 28. Brain Branched-Chain Amino Acids in Maple Syrup Urine Disease: Implications for Neurological Disorders. (nih.gov)
  • 30. Evaluation of branched-chain amino acid intake in children with maple syrup urine disease and methylmalonic aciduria. (nih.gov)
  • 20. Preoperative oral supplementation with carbohydrate and branched-chain amino acid-enriched nutrient improves insulin resistance in patients undergoing a hepatectomy: a randomized clinical trial using an artificial pancreas. (nih.gov)
  • 35. The Relationship between Branched-Chain Amino Acid Related Metabolomic Signature and Insulin Resistance: A Systematic Review. (nih.gov)
  • The directed movement of branched-chain amino acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. (ntu.edu.sg)
  • 1. Effects of insulin on myocardial uptake of branched chain amino acids soon after cardiac operations. (nih.gov)
  • 3. Effect of hyperinsulinemia on myocardial amino acid uptake in patients with coronary artery disease. (nih.gov)
  • 5. Myocardial uptake of amino acids and other substrates in relation to myocardial oxygen consumption four hours after cardiac operations. (nih.gov)
  • These amino acids cannot be synthesized in the liver. (naturalvibe.ca)
  • 26. Branched-chain amino acids: Abundance of their transporters and metabolizing enzymes in adipose tissue, skeletal muscle, and liver of dairy cows at high or normal body condition. (nih.gov)
  • Amino acids ( Milk ), Capsule wall (Gelatin (Bovine)), Anti-caking agent (Fatty acid). (nutritioncompany.eu)
  • Gelatin (capsule) and Stearic Acid (vegetable source). (naturalvibe.ca)
  • Although ICD-9-CM codes are fairly specific, in certain cases, the same ICD-9-CM code might apply to several disorders in the same group (e.g. amino acid disorders). (nih.gov)
  • THRIVE contains the critical branch chain amino acids and glutamine to support the repair and building of elan muscle while helping to reduce post-workout soreness. (dallasbikeworks.com)
  • Meghan Pendleton, RD at www.meghanpendleton.com says, "Branched Chain Amino Acids are marketed to help you improve muscle growth and strength. (eatthis.com)
  • 11. Regulation of myocardial amino acid balance in the conscious dog. (nih.gov)
  • Grape polyphenols decrease circulating branched chain amino acids in overfed adults. (bvsalud.org)
  • Possible alternatives are Amino Gram Forte Plus (Douglas) and Amino Complete (NOW Foods) . (nutritioncompany.eu)
  • The serving of Now Foods Branched Chain Amino Acids contains 2900 mg amino acids as against 8000 mg in one GAT Amino GT serving. (vsprotein.com)
  • For a serving of Now Foods Branched Chain Amino Acids you will pay $ 0.48 , and a for a serving of GAT Amino GT you will have to pay $ 1.21. (vsprotein.com)
  • Now Foods Branched Chain Amino Acids has no taste, the manufacturer produces it unflavored. (vsprotein.com)
  • Now Foods makes available 2 different sizes of Branched Chain Amino Acids. (vsprotein.com)
  • University of Lyon, CarMeN Laboratory and Centre de Recherche en Nutrition Humaine Rhône-Alpes (CRNH-RA), INSERM, INRAE, Claude Bernard University Lyon 1, Pierre-Bénite, France. (bvsalud.org)
  • Maternal and cord plasma branched-chain amino acids and child risk of attention-deficit hyperactivity disorder: a prospective birth cohort study. (nih.gov)
  • 36. Maternal Obesity/Diabetes, Plasma Branched-Chain Amino Acids, and Autism Spectrum Disorder Risk in Urban Low-Income Children: Evidence of Sex Difference. (nih.gov)
  • And as the U.S. National Library of Medicine explains, amino acids are used to perform many body functions. (livestrong.com)
  • As a result, these amino acids and their byproducts build up in the body. (nih.gov)
  • 6. Effects of branched-chain amino acids on placental amino acid transfer and insulin and glucagon release in the ovine fetus. (nih.gov)

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