A high-affinity, low capacity system y+ amino acid transporter found ubiquitously. It has specificity for the transport of ARGININE; LYSINE; and ORNITHINE. It may also act as an ecotropic leukemia retroviral receptor.
A high-affinity, low capacity system y+ amino acid transporter with strong similarity to CATIONIC AMINO ACID TRANSPORTER 1. The two isoforms of the protein, CAT-2A and CAT-2B, exist due to alternative mRNA splicing. The transporter has specificity for the transport of ARGININE; LYSINE; and ORNITHINE.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
Cellular proteins and protein complexes that transport amino acids across biological membranes.
An essential amino acid that is physiologically active in the L-form.
The Amino Acid Transport System y+L is a group of transport proteins that facilitate the uptake and transport of amino acids across cell membranes.
The Amino Acid Transport System y+ is a group of transport proteins found in the mitochondria of cells that facilitate the transport of certain amino acids into the mitochondria for energy production.
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.
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.
Transport proteins that carry specific substances in the blood or across cell membranes.
A ureahydrolase that catalyzes the hydrolysis of arginine or canavanine to yield L-ornithine (ORNITHINE) and urea. Deficiency of this enzyme causes HYPERARGININEMIA. EC 3.5.3.1.
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.
A transmembrane glycoprotein subunit that can dimerize with a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS). This protein subunit serves a diverse array of functions including amino acid transport and cell fusion. Its function is altered depending which of the light chain subunits it interacts with.
Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).
A heterodimeric protein that is a cell surface antigen associated with lymphocyte activation. The initial characterization of this protein revealed one identifiable heavy chain (ANTIGENS, CD98 HEAVY CHAIN) and an indeterminate smaller light chain. It is now known that a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS) can dimerize with the heavy chain. Depending upon its light chain composition a diverse array of functions can be found for this protein. Functions include: type L amino acid transport, type y+L amino acid transport and regulation of cellular fusion.
A family of light chains that bind to the CD98 heavy chain (ANTIGENS, CD98 HEAVY CHAIN) to form a heterodimer. They convey functional specificity to the protein.
A glial type glutamate plasma membrane transporter protein found predominately in ASTROCYTES. It is also expressed in HEART and SKELETAL MUSCLE and in the PLACENTA.
Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.
A ubiquitous sodium-dependent neutral amino acid transporter. The preferred substrates for this transporter system include ALANINE; SERINE; and CYSTEINE.
A neuronal and epithelial type glutamate plasma membrane transporter protein.
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.
A glutamate plasma membrane transporter protein found in ASTROCYTES and in the LIVER.
A glutamate plasma membrane transporter protein that is primarily expressed in cerebellar PURKINJE CELLS on postsynaptic DENDRITIC SPINES.
Amino acids with uncharged R groups or side chains.
An essential amino acid. It is often added to animal feed.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
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.
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.
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.
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.
Diamino acids are a type of amino acid that contain two amino groups (-NH2) attached to the same carbon atom.
Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.
An NADPH-dependent enzyme that catalyzes the conversion of L-ARGININE and OXYGEN to produce CITRULLINE and NITRIC OXIDE.
A family of plasma membrane neurotransmitter transporter proteins that couple the uptake of GLUTAMATE with the import of SODIUM ions and PROTONS and the export of POTASSIUM ions. In the CENTRAL NERVOUS SYSTEM they regulate neurotransmission through synaptic reuptake of the excitatory neurotransmitter glutamate. Outside the central nervous system they function as signal mediators and regulators of glutamate metabolism.
A CALCIUM-independent subtype of nitric oxide synthase that may play a role in immune function. It is an inducible enzyme whose expression is transcriptionally regulated by a variety of CYTOKINES.
A sodium-independent neutral amino acid transporter system with specificity for large amino acids. One of the functions of the transporter system is to supply large neutral amino acids to the brain.
A glutamate plasma membrane transporter protein that is primarily expressed in the RETINA.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
A family of POTASSIUM and SODIUM-dependent acidic amino acid transporters that demonstrate a high affinity for GLUTAMIC ACID and ASPARTIC ACID. Several variants of this system are found in neuronal tissue.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
An essential branched-chain amino acid important for hemoglobin formation.
Glycoproteins found on the membrane or surface of cells.
Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
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.
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 subclass of ORGANIC ANION TRANSPORTERS whose transport of organic anions is driven either directly or indirectly by a gradient of sodium ions.
Proteins involved in the transport of organic anions. They play an important role in the elimination of a variety of endogenous substances, xenobiotics and their metabolites from the body.
The rate dynamics in chemical or physical systems.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
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.
A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
A family of plasma membrane neurotransmitter transporter proteins that regulates extracellular levels of the inhibitory neurotransmitter GAMMA-AMINOBUTYRIC ACID. They differ from GABA RECEPTORS, which signal cellular responses to GAMMA-AMINOBUTYRIC ACID. They control GABA reuptake into PRESYNAPTIC TERMINALS in the CENTRAL NERVOUS SYSTEM through high-affinity sodium-dependent transport.
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.
An inherited disorder due to defective reabsorption of CYSTINE and other BASIC AMINO ACIDS by the PROXIMAL RENAL TUBULES. This form of aminoaciduria is characterized by the abnormally high urinary levels of cystine; LYSINE; ARGININE; and ORNITHINE. Mutations involve the amino acid transport protein gene SLC3A1.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Established cell cultures that have the potential to propagate indefinitely.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
A sulfhydryl reagent that is widely used in experimental biochemical studies.
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.
A class of amino acids characterized by a closed ring structure.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
A metabolic disease characterized by the defective transport of CYSTINE across the lysosomal membrane due to mutation of a membrane protein cystinosin. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. In the KIDNEY, nephropathic cystinosis is a common cause of RENAL FANCONI SYNDROME.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
A group of inherited kidney disorders characterized by the abnormally elevated levels of AMINO ACIDS in URINE. Genetic mutations of transport proteins result in the defective reabsorption of free amino acids at the PROXIMAL RENAL TUBULES. Renal aminoaciduria are classified by the specific amino acid or acids involved.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
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 toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.
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.
A family of proteins involved in the transport of monocarboxylic acids such as LACTIC ACID and PYRUVIC ACID across cellular membranes.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
An autosomal recessive disorder due to defective absorption of NEUTRAL AMINO ACIDS by both the intestine and the PROXIMAL RENAL TUBULES. The abnormal urinary loss of TRYPTOPHAN, a precursor of NIACIN, leads to a NICOTINAMIDE deficiency, PELLAGRA-like light-sensitive rash, CEREBELLAR ATAXIA, emotional instability, and aminoaciduria. Mutations involve the neurotransmitter transporter gene SLC6A19.
Amino acids containing an aromatic side chain.
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 family of vesicular neurotransmitter transporter proteins that sequester the inhibitory neurotransmitters GLYCINE; GAMMA-AMINOBUTYRIC ACID; and possibly GAMMA-HYDROXYBUTYRATE into SECRETORY VESICLES.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Proteins involved in the transport of NUCLEOTIDES across cellular membranes.
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)
Polyamines are biogenic amines that are involved in various cellular processes, including cell growth and division, and have been implicated in the development and progression of several diseases.
Biogenic amines having more than one amine group. These are long-chain aliphatic compounds that contain multiple amino and/or imino groups. Because of the linear arrangement of positive charge on these molecules, polyamines bind electrostatically to ribosomes, DNA, and RNA.
Disorders characterized by defective transport of amino acids across cell membranes. These include deficits in transport across brush-border epithelial cell membranes of the small intestine (MICROVILLI) and KIDNEY TUBULES; transport across the basolateral membrane; and transport across the membranes of intracellular organelles. (From Nippon Rinsho 1992 Jul;50(7):1587-92)
An amino acid formed in vivo by the degradation of dihydrouracil and carnosine. Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, the compound may be a false transmitter replacing GAMMA-AMINOBUTYRIC ACID. A rare genetic disorder, hyper-beta-alaninemia, has been reported.
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.
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.
Species of GAMMARETROVIRUS, containing many well-defined strains, producing leukemia in mice. Disease is commonly induced by injecting filtrates of propagable tumors into newborn mice.
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.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
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.
Proteins prepared by recombinant DNA technology.

Two-way arginine transport in human endothelial cells: TNF-alpha stimulation is restricted to system y(+). (1/75)

Human umbilical vein endothelial cells transport arginine through two Na(+)-independent systems. System y(+)L is insensitive to N-ethylmaleimide (NEM), inhibited by L-leucine in the presence of Na(+), and referable to the expression of SLC7A6/y(+)LAT2, SLC7A7/y(+)LAT1, and SLC3A2/4F2hc. System y(+) is referable to the expression of SLC7A1/CAT1 and SLC7A2/CAT2B. Tumor necrosis factor-alpha (TNF-alpha) and bacterial lipopolysaccharide induce a transient stimulation of arginine influx and efflux through system y(+). Increased expression of SLC7A2/CAT2B is detectable from 3 h of treatment, while SLC7A1 expression is inhibited at later times of incubation. System y(+)L activity and expression remain unaltered. Nitric oxide synthase type 2 mRNA is not detected in the absence or presence of TNF-alpha, while the latter condition lowers nitric oxide synthase type 3 expression at the mRNA and the protein level. Nitrite accumulation is comparable in cytokine-treated and control cells up to 48 h of treatment. It is concluded that modulation of endothelial arginine transport by TNF-alpha or lipopolysaccharide occurs exclusively through changes in CAT2B and CAT1 expression and is dissociated from stimulation of nitric oxide production.  (+info)

Fv1-like restriction of N-tropic replication-competent murine leukaemia viruses in mCAT-1-expressing human cells. (2/75)

To study the replication of murine leukaemia viruses in human cells we have used full-length as well as EGFP-tagged ecotropic viruses in combination with mCAT-1-expressing human cells. We present results showing that N-tropic murine leukaemia viruses are restricted in both infection and replication in such cells while B-tropic viruses, modified at capsid position 110, escape restriction. These results support a recently reported Fv1-like restriction in mammalian cells. We extend the analysis of Fv1-like restriction by demonstrating that NB-tropic viruses also escape restriction and human mCAT-1-expressing cells are thus similar to murine Fv1(b) cells with respect to infection though the ecotropic receptor pathway.  (+info)

Garlic attenuates nitric oxide production in rat cardiac myocytes through inhibition of inducible nitric oxide synthase and the arginine transporter CAT-2 (cationic amino acid transporter-2). (3/75)

It is now accepted that allicin, the main biologically active compound in garlic, exhibits antioxidant activity. The present study was designed to test the hypothesis that the antioxidant activity of garlic can be partially attributed to the inhibition of nitric oxide (NO) production by cytokine-induced NO synthase (iNOS). Cardiac myocytes cultured from neonatal Wistar rats were stimulated by lipopolysaccharide (LPS) and incubated for 24 h with various concentrations of allicin. This resulted in marked inhibition of nitrite production. Interestingly, a low concentration of allicin (10 microM) was significantly more potent in abrogating the effect of LPS on nitrite production than a higher concentration (40 microM). Allicin decreased steady-state iNOS mRNA levels, and this effect was maximal when a lower concentration was used (10 microM compared with 40 microM). In order to explore additional effects of allicin on NO generation that might counteract the effect on iNOS, we assessed the effects of higher allicin concentrations on arginine transport. Allicin inhibited the uptake of 1 mM extracellular arginine in a concentration-dependent manner. The expression of the two arginine transporters that are expressed in cardiac myocytes [CAT-1 (cationic amino acid transporter-1) and CAT-2] was studied using reverse transcription-PCR. A concentration of 200 microM allicin abolished the expression of CAT-2 mRNA, 100 microM significantly attenuated it, whereas 50 microM had no effect. Allicin had no effect on steady-state CAT-1 mRNA levels. Our results suggest that allicin inhibits iNOS activity through two different mechanisms: at lower concentrations it decreases iNOS mRNA levels, whereas at higher concentrations it inhibits arginine transport through down-regulation of CAT-2 mRNA.  (+info)

Intrauterine growth retardation is associated with reduced activity and expression of the cationic amino acid transport systems y+/hCAT-1 and y+/hCAT-2B and lower activity of nitric oxide synthase in human umbilical vein endothelial cells. (4/75)

Intrauterine growth retardation (IUGR) is associated with vascular complications leading to hypoxia and abnormal fetal development. The effect of IUGR on L-arginine transport and nitric oxide (NO) synthesis was investigated in cultures of human umbilical vein endothelial cells (HUVECs). IUGR was associated with membrane depolarization and reduced L-arginine transport (V(max)= 5.8+/-0.2 versus 3.3+/-0.1 pmol/microg protein per minute), with no significant changes in transport affinity (K(m)=159+/-15 versus 137+/-14 micromol/L). L-Arginine transport was trans-stimulated (8- to 9-fold) in cells from normal and IUGR pregnancies. IUGR was associated with reduced production of L-[3H]citrulline from L-[3H] arginine, lower nitrite and intracellular L-arginine, L-citrulline, and cGMP. IUGR decreased hCAT-1 and hCAT-2B mRNA, and increased eNOS mRNA and protein levels. IUGR-associated inhibition of L-arginine transport and NO synthesis, and membrane depolarization were reversed by the NO donor S-nitroso-N-acetyl-L,D-penicillamine. In summary, endothelium from fetuses with IUGR exhibit altered L-arginine transport and NO synthesis (L-arginine/NO pathway), reduced expression and activity of hCAT-1 and hCAT-2B and reduced eNOS activity. Alterations in L-arginine/NO pathway could be critical for the physiological processes involved in the etiology of IUGR in human pregnancies.  (+info)

Nutritional control of mRNA stability is mediated by a conserved AU-rich element that binds the cytoplasmic shuttling protein HuR. (5/75)

The cationic amino acid transporter, Cat-1, is a high affinity transporter of the essential amino acids, arginine and lysine. Expression of the cat-1 gene increases during nutritional stress as part of the adaptive response to starvation. Amino acid limitation induces coordinate increases in stability and translation of the cat-1 mRNA, at a time when global protein synthesis decreases. It is shown here that increased cat-1 mRNA stability requires an 11 nucleotide AU-rich element within the distal 217 bases of the 3'-untranslated region. When this 217-nucleotide nutrient sensor AU-rich element (NS-ARE) is present in a chimeric mRNA it confers mRNA stabilization during amino acid starvation. HuR is a member of the ELAV family of RNA-binding proteins that has been implicated in regulating the stability of ARE-containing mRNAs. We show here that the cytoplasmic concentration of HuR increases during amino acid starvation, at a time when total cellular HuR levels decrease. In addition, RNA gel shift experiments in vitro demonstrated that HuR binds to the NS-ARE and binding was dependent on the 11 residue AU-rich element. Moreover, HuR binding to the NS-ARE in extracts from amino acid-starved cells increased in parallel with the accumulation of cytoplasmic HuR. It is proposed that an adaptive response of cells to nutritional stress results in increased mRNA stability mediated by HuR binding to the NS-ARE.  (+info)

L-Arginine transport is augmented through up-regulation of tubular CAT-2 mRNA in ischemic acute renal failure in rats. (6/75)

BACKGROUND: Ischemic acute renal failure (iARF) is associated with increased nitric oxide (NO) production during the reperfusion period, as endothelial nitric oxide synthase (eNOS) is maximally activated, and renal tubular inducible NOS (iNOS) is stimulated. Increased NO production leads to augmented tubular injury, probably through the formation of peroxynitrite. l-Arginine (l-Arg), the only precursor for NO, is transported into cells by cationic amino acid transporters, CAT-1 and CAT-2. We hypothesized that the increased NO production observed in iARF may result from increased l-Arg uptake, which would be reflected in the augmented expression of l-Arg transporter(s). METHODS: Ischemic acute renal failure was induced in rats by right nephrectomy + left renal artery clamping for 60 minutes. l-Arg uptake was examined in freshly harvested glomeruli and tubuli from control, sham operated, and animals subjected to 15, 30, and 60 minutes, and 24 hours of reperfusion, following 60 minutes of ischemia. Using RT-PCR, renal tissues were examined further for the expression of iNOS, CAT-1, CAT-2, arginase I and arginase II. RESULTS: Tubular expression of iNOS mRNA was initiated by ischemia, continued to increase after 60 minutes of reperfusion, and decreased after 24 hours. l-Arg transport into glomeruli was similar in all experimental groups. l-Arg uptake into tubuli was markedly augmented following the 60-minute reperfusion, while it moderately increased after 24 hours of reperfusion. This was accompanied by a parallel, preferential increase in tubular CAT-2 mRNA expression at 60 minutes of reperfusion. CAT-1 mRNA expression was unchanged, as detected by RT-PCR. In addition, the expression of arginase II and arginase I mRNA was attenuated by 30 minutes and one hour of reperfusion, and returned to baseline values after 24 hours of reperfusion. CONCLUSIONS: Ischemic ARF is associated with augmented tubular CAT-2 mRNA expression, which leads to enhanced l-Arg transport and increased NO production. This may contribute to the renal injury exhibited in iARF.  (+info)

System y+ localizes to different membrane subdomains in the basolateral plasma membrane of epithelial cells. (7/75)

We report here that the system y+ cationic amino acid transporter ATRC1 localized to clusters within the basolateral membrane of polarized Madin-Darby canine kidney and human embryonic kidney (HEK) cells, suggesting that the transporters are restricted to discrete membrane microdomains in epithelial cells. Based on solubility in nonionic detergents, two populations of ATRC1 molecules existed: approximately half of the total ATRC1 in HEK cells associated with the actin membrane cytoskeleton, whereas another one-fourth resided in detergent-resistant membranes (DRM). In agreement with these findings, cytochalasin D reduced the amount of ATRC1 associated with the actin membrane cytoskeleton. Although some ATRC1 clusters in HEK cells colocalized with caveolin, the majority of ATRC1 did not colocalize with this marker protein for a type of DRM called caveolae. This distribution of ATRC1 is somewhat different from that reported for pulmonary artery endothelial cells in which transporters cluster predominantly in caveolae, suggesting that differences in the proportion of ATRC1 in specific membrane microdomains correlate with differences in the physiological role of the transporter in polarized kidney epithelial vs. vascular endothelial cells.  (+info)

Regulation of the S100B gene by alpha 1-adrenergic stimulation in cardiac myocytes. (8/75)

We previously reported that S100B, a 20-kDa Ca(2+)-binding homodimer, inhibited the postinfarct myocardial hypertrophic response mediated by alpha(1)-adrenergic stimulation through the protein kinase C (PKC) signaling pathway. In the present study, we examined whether the same pathway induced the S100B gene, supporting the hypothesis that S100B is a feedback negative regulator of this pathway. We transfected cultured neonatal rat cardiac myocytes with a luciferase reporter gene driven by the maximal human S100B promoter and progressively shorter segments of this promoter sequentially deleted from the 5' end. We identified a basic promoter essential for transcription spanning 162 bp upstream of the transcription initiation site and positive (at -782/-162 and -6,689/-4,463) and negative (at -4,463/-782) myocyte-selective regulatory elements. We showed that the basic and maximal S100B promoters were activated specifically by alpha(1)-adrenergic agonists through the alpha(1A)-adrenergic receptor, but not by any other trophic hormonal stimuli. The activation of the S100B promoter was mediated through the PKC signaling pathway. Transcription enhancer factor-1 (TEF-1) and related to TEF-1 (RTEF-1) influenced transcription from the maximal, but not the basic, promoter implicating active MCAT elements upstream from the basic promoter. Acting in opposing fashions, TEF-1 transrepressed the S100B promoter and RTEF-1 transactivated the promoter. Our results suggest that alpha(1)-adrenergic stimulation induces the S100B gene after myocardial infarction through the PKC signaling pathway and that this induction is modulated by TEF-1 and RTEF-1.  (+info)

Cationic Amino Acid Transporter 1 (CAT-1) is a protein that plays a crucial role in the transport of basic amino acids, such as arginine, lysine, and histidine, across the plasma membrane of cells. It is primarily expressed in the small intestine, kidney, and placenta, where it facilitates the absorption of dietary amino acids and their reabsorption from the urine. CAT-1 is a member of the solute carrier family 7 (SLC7) of transporters and is encoded by the SLC7A1 gene. It functions as a sodium-dependent symporter, using the energy from the sodium gradient to transport amino acids into the cell. CAT-1 is also involved in the transport of certain drugs and toxins, making it an important target for drug delivery and chemotherapy. Disruptions in CAT-1 function have been linked to various diseases, including lysinuric protein intolerance, a rare genetic disorder characterized by the accumulation of toxic levels of arginine in the blood and urine. Additionally, some studies have suggested that CAT-1 may play a role in the development of certain types of cancer, as well as in the regulation of immune function and inflammation.

Cationic Amino Acid Transporter 2 (CAT-2) is a protein that plays a role in the transport of basic amino acids across cell membranes. It is primarily expressed in the small intestine, kidney, and placenta, where it is involved in the absorption and reabsorption of amino acids from the gut and the regulation of amino acid homeostasis in the body. CAT-2 is a member of the solute carrier family of transporters, which are responsible for the transport of a wide variety of molecules across cell membranes. It is a transmembrane protein that uses energy from the proton gradient across the membrane to transport amino acids from the extracellular space into the cell. Disruptions in the function of CAT-2 can lead to a number of health problems, including impaired amino acid absorption and transport, which can result in malnutrition and other complications. In addition, mutations in the CAT-2 gene have been associated with certain genetic disorders, such as Hartnup disease, which is characterized by a deficiency in the transport of certain amino acids across the gut and skin.

Amino Acid Transport Systems, Basic refers to the various mechanisms by which amino acids are transported across cell membranes. These transport systems are essential for the proper functioning of cells and the maintenance of homeostasis in the body. There are several types of amino acid transport systems, including passive transport, facilitated diffusion, and active transport. Passive transport occurs naturally and does not require energy, while facilitated diffusion and active transport require energy in the form of ATP. These transport systems play a crucial role in the absorption and utilization of amino acids in the body, as well as in the regulation of amino acid levels in various tissues and fluids.

Amino acid transport systems are a group of proteins that facilitate the movement of amino acids across cell membranes. These transport systems play a crucial role in maintaining the proper balance of amino acids within cells and between cells and the extracellular environment. There are two main types of amino acid transport systems: passive transport systems and active transport systems. Passive transport systems, such as facilitated diffusion and cotransport, do not require energy to move amino acids across the membrane. Active transport systems, such as primary active transport and secondary active transport, require energy in the form of ATP to move amino acids against their concentration gradient. Amino acid transport systems are important for a variety of physiological processes, including protein synthesis, metabolism, and the regulation of blood pressure. Mutations in amino acid transport genes can lead to a variety of disorders, including inborn errors of metabolism, neurological disorders, and kidney disease.

Arginine is an amino acid that plays a crucial role in various physiological processes in the human body. It is an essential amino acid, meaning that it cannot be synthesized by the body and must be obtained through the diet. In the medical field, arginine is used to treat a variety of conditions, including: 1. Erectile dysfunction: Arginine is a precursor to nitric oxide, which helps to relax blood vessels and improve blood flow to the penis, leading to improved sexual function. 2. Cardiovascular disease: Arginine has been shown to improve blood flow and reduce the risk of cardiovascular disease by lowering blood pressure and improving the function of the endothelium, the inner lining of blood vessels. 3. Wound healing: Arginine is involved in the production of collagen, a protein that is essential for wound healing. 4. Immune function: Arginine is involved in the production of antibodies and other immune system components, making it important for maintaining a healthy immune system. 5. Cancer: Arginine has been shown to have anti-cancer properties and may help to slow the growth of tumors. However, it is important to note that the use of arginine as a supplement is not without risks, and it is important to consult with a healthcare provider before taking any supplements.

Amino Acid Transport System y+L (also known as System y+ or y+ system) is a group of transport proteins found in the plasma membrane of cells that are responsible for the uptake of amino acids from the bloodstream into the cells. The y+ system is particularly important for the transport of large neutral amino acids (LNAA), such as leucine, isoleucine, and valine, which are essential for protein synthesis. The y+ system is composed of two main transporters: the y+L transporter (SLC7A5) and the y+L2 transporter (SLC7A8). These transporters are members of the solute carrier family 7 (SLC7) and are located in the plasma membrane of cells in various tissues, including the liver, kidney, and muscle. The y+ system plays a critical role in maintaining the balance of amino acids in the body and is involved in various physiological processes, including protein synthesis, energy metabolism, and neurotransmitter synthesis. Dysregulation of the y+ system has been implicated in various diseases, including liver disease, kidney disease, and neurodegenerative disorders.

The Amino Acid Transport System y+ (also known as the y+ system or System y+) is a group of transport proteins found in the mitochondria of cells. These proteins are responsible for transporting amino acids into the mitochondria, where they are used for energy production through a process called oxidative phosphorylation. The y+ system is important for maintaining the proper balance of amino acids in the cell and for ensuring that the mitochondria have access to the amino acids they need to produce energy. Mutations in the genes encoding the y+ system proteins have been linked to a number of genetic disorders, including Leigh syndrome and MELAS (Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like episodes). In summary, the Amino Acid Transport System y+ is a group of transport proteins that play a critical role in energy production and amino acid metabolism in the cell.

Amino acids are organic compounds that are the building blocks of proteins. They are composed of an amino group (-NH2), a carboxyl group (-COOH), and a side chain (R group) that varies in size and structure. There are 20 different amino acids that are commonly found in proteins, each with a unique side chain that gives it distinct chemical and physical properties. In the medical field, amino acids are important for a variety of functions, including the synthesis of proteins, enzymes, and hormones. They are also involved in energy metabolism and the maintenance of healthy tissues. Deficiencies in certain amino acids can lead to a range of health problems, including muscle wasting, anemia, and neurological disorders. In some cases, amino acids may be prescribed as supplements to help treat these conditions or to support overall health and wellness.

In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.

Arginase is an enzyme that plays a role in the metabolism of the amino acid arginine. It is found in a variety of tissues throughout the body, including the liver, kidneys, and spleen. In the medical field, arginase is of interest because it is involved in the production of nitric oxide, a molecule that helps to regulate blood pressure and inflammation. Arginase inhibitors are being studied as potential treatments for a variety of conditions, including hypertension, atherosclerosis, and inflammatory diseases. Arginase is also involved in the metabolism of ornithine, another amino acid, and is important for the production of polyamines, which are essential for cell growth and division.

Large Neutral Amino Acid-Transporter 1 (LAT1) is a protein that plays a crucial role in the transport of large neutral amino acids across cell membranes. It is primarily expressed in tissues with high protein synthesis rates, such as the brain, kidneys, and placenta. LAT1 is a heterodimeric protein composed of two subunits, SLC7A5 and SLC3A2. The transporter is located in the plasma membrane of cells and uses energy from the sodium gradient to transport large neutral amino acids, such as leucine, isoleucine, and valine, into the cell. In the brain, LAT1 is involved in the transport of amino acids that are essential for the synthesis of neurotransmitters, such as dopamine and serotonin. It also plays a role in the transport of amino acids across the blood-brain barrier, which is a critical process for maintaining proper brain function. In the kidneys, LAT1 is involved in the reabsorption of amino acids from the urine, which helps to maintain the body's amino acid balance. In the placenta, LAT1 is involved in the transport of amino acids from the mother to the developing fetus. Disruptions in LAT1 function have been linked to several diseases, including neurodegenerative disorders, cancer, and kidney disease. Therefore, understanding the role of LAT1 in amino acid transport is important for developing new treatments for these conditions.

CD98 heavy chain is a type of protein that is found on the surface of many different types of cells in the body. It is a component of a protein complex called the 4F2hc heterodimer, which is involved in the transport of certain molecules across the cell membrane. CD98 heavy chain is also known as the 4F2 heavy chain or the SLC3A2 gene product. It is expressed on the surface of cells in the immune system, as well as on cells in the digestive tract, liver, and other organs. In the medical field, CD98 heavy chain is often studied in the context of cancer and other diseases, as it has been implicated in a number of different cellular processes that are relevant to disease pathogenesis.

Amino Acid Transport Systems, Neutral refers to a group of proteins that are responsible for transporting neutral amino acids across cell membranes. These transporters play a crucial role in the metabolism of amino acids, as they allow cells to take up amino acids from the bloodstream and use them for various cellular processes, such as protein synthesis and energy production. There are several types of neutral amino acid transporters, including the System A, System N, and System L transporters. These transporters are found in various tissues throughout the body, including the liver, kidney, and brain. Disruptions in the function of neutral amino acid transporters can lead to a variety of health problems, including aminoacidopathies, which are disorders caused by defects in the metabolism of amino acids. For example, maple syrup urine disease is a genetic disorder caused by a deficiency in the branched-chain alpha-keto acid dehydrogenase complex, which is involved in the metabolism of branched-chain amino acids. This deficiency leads to the accumulation of toxic levels of branched-chain amino acids and their metabolites in the blood and urine.

CD98 is a protein that is expressed on the surface of many different types of cells in the body. It is a member of a family of proteins called the transmembrane 4 superfamily (TM4SF), which are involved in a variety of cellular processes, including cell adhesion, migration, and signaling. In the context of the immune system, CD98 is an antigen, which means that it can be recognized by the immune system as foreign and trigger an immune response. Antigens are typically proteins or other molecules that are found on the surface of pathogens, such as viruses or bacteria, or on the surface of abnormal cells, such as cancer cells. CD98 is expressed on the surface of many different types of immune cells, including T cells, B cells, and natural killer (NK) cells. It is thought to play a role in the activation and function of these cells, and it has been implicated in a variety of immune-related disorders, including autoimmune diseases and cancer.

CD98 light chains are a type of protein found on the surface of certain cells in the human body. They are also known as the low-affinity immunoglobulin-like receptor, or LAIR-1. CD98 light chains are part of a larger protein complex called CD98, which is involved in the transport of certain molecules into and out of cells. In the context of the immune system, CD98 light chains can help to regulate the activity of immune cells, such as T cells and macrophages. They can also play a role in the development of certain types of cancer.

Excitatory Amino Acid Transporter 1 (EAAT1) is a protein that plays a crucial role in the regulation of glutamate, an excitatory neurotransmitter in the central nervous system. EAAT1 is responsible for the reuptake of glutamate from the synaptic cleft back into the presynaptic neuron, which helps to terminate glutamate signaling and prevent overstimulation of postsynaptic neurons. EAAT1 is a member of the solute carrier family of transporters and is expressed primarily in astrocytes, which are a type of glial cell that play a critical role in maintaining the homeostasis of the extracellular glutamate concentration. EAAT1 is also expressed in some neurons and oligodendrocytes. Disruption of EAAT1 function has been implicated in several neurological disorders, including epilepsy, stroke, and neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Therefore, understanding the regulation and function of EAAT1 is important for developing new therapeutic strategies for these conditions.

Receptors, Virus are proteins on the surface of host cells that recognize and bind to specific viral proteins, allowing the virus to enter and infect the cell. These receptors play a crucial role in the viral life cycle and are often targeted by antiviral drugs and vaccines. Examples of viral receptors include the ACE2 receptor for SARS-CoV-2 (the virus that causes COVID-19) and the CD4 receptor for HIV.

The Amino Acid Transport System ASC (Amino Acid Transporter ASC) is a protein complex that plays a crucial role in the transport of amino acids across cell membranes. It is composed of three subunits: ASC1, ASC2, and ASC3. The ASC system is responsible for the transport of neutral and basic amino acids, such as alanine, arginine, and lysine, across the plasma membrane of cells. It is particularly important in the transport of these amino acids into cells, as they are essential for various cellular processes, including protein synthesis, energy metabolism, and cellular signaling. Defects in the ASC system can lead to various medical conditions, including aminoaciduria, which is the abnormal excretion of amino acids in the urine. This can result in a deficiency of certain amino acids in the body, leading to various symptoms, such as muscle weakness, fatigue, and developmental delays.

Excitatory Amino Acid Transporter 3 (EAAT3) is a protein that plays a crucial role in regulating the levels of excitatory neurotransmitters, such as glutamate, in the brain. It is a member of the excitatory amino acid transporter (EAAT) family of proteins, which are responsible for the reuptake of glutamate from the synaptic cleft back into the presynaptic neuron or glial cells. EAAT3 is primarily expressed in astrocytes, which are a type of glial cell that play a key role in maintaining the homeostasis of neurotransmitters in the brain. It is located on the plasma membrane of astrocytes and functions to transport glutamate from the extracellular space back into the cytoplasm, where it can be metabolized or recycled. The function of EAAT3 is important for maintaining the proper balance of glutamate in the brain, which is critical for normal brain function. Dysregulation of EAAT3 activity has been implicated in a number of neurological disorders, including stroke, epilepsy, and neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

Amino Acid Transport System A (AAT System A) is a group of transport proteins found in the plasma membrane of cells that facilitate the transport of amino acids across the cell membrane. This system is responsible for the uptake of neutral and basic amino acids, such as alanine, serine, and glycine, from the extracellular environment into the cell. AAT System A is a sodium-dependent transporter that uses the energy from the movement of sodium ions across the cell membrane to transport amino acids into the cell. This system is important for the uptake of amino acids by cells, particularly in tissues with high protein turnover, such as muscle and liver. Disruptions in AAT System A function can lead to various medical conditions, including aminoaciduria (excretion of amino acids in the urine), hyperammonemia (elevated levels of ammonia in the blood), and impaired protein synthesis.

Excitatory Amino Acid Transporter 2 (EAAT2) is a protein that plays a crucial role in regulating the levels of excitatory neurotransmitters, such as glutamate, in the brain. It is a type of sodium-dependent glutamate transporter that is primarily expressed in astrocytes, which are a type of glial cell that support neurons in the central nervous system. EAAT2 is responsible for clearing glutamate from the extracellular space, where it is released by neurons during synaptic transmission. This process helps to prevent overstimulation of glutamate receptors and reduces the risk of excitotoxicity, which can lead to neuronal damage and death. In addition to its role in regulating glutamate levels, EAAT2 has also been implicated in a number of neurological disorders, including stroke, epilepsy, and neurodegenerative diseases such as Alzheimer's and Parkinson's. Therefore, understanding the function and regulation of EAAT2 is an important area of research in the field of neuroscience.

Excitatory Amino Acid Transporter 4 (EAAT4) is a protein that plays a crucial role in the regulation of glutamate, an excitatory neurotransmitter in the central nervous system. EAAT4 is a type of glutamate transporter that is expressed primarily in astrocytes, which are a type of glial cell that support and nourish neurons. EAAT4 is responsible for clearing excess glutamate from the synaptic cleft, the space between neurons where they communicate with each other. This process is essential for preventing overstimulation of neurons and preventing the development of excitotoxicity, a condition in which excessive glutamate causes damage to neurons. EAAT4 is also involved in the regulation of the blood-brain barrier, which is a barrier that protects the brain from harmful substances in the bloodstream. EAAT4 helps to maintain the balance of ions and neurotransmitters in the brain, which is essential for proper brain function. Disruptions in EAAT4 function have been linked to several neurological disorders, including epilepsy, stroke, and neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Therefore, understanding the role of EAAT4 in the brain is important for developing new treatments for these conditions.

In the medical field, "Amino Acids, Neutral" refers to a group of amino acids that do not have a charged side chain. These amino acids are called "neutral" because they do not have a positive or negative charge. Examples of neutral amino acids include alanine, glycine, valine, leucine, isoleucine, serine, threonine, cysteine, and proline. Neutral amino acids are important building blocks of proteins and are essential for many bodily functions. They can be obtained from the diet or synthesized by the body.

Lysine is an essential amino acid that is required for the growth and maintenance of tissues in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. Lysine plays a crucial role in the production of proteins, including enzymes, hormones, and antibodies. It is also involved in the absorption of calcium and the production of niacin, a B vitamin that is important for energy metabolism and the prevention of pellagra. In the medical field, lysine is used to treat and prevent various conditions, including: 1. Herpes simplex virus (HSV): Lysine supplements have been shown to reduce the frequency and severity of outbreaks of HSV-1 and HSV-2, which cause cold sores and genital herpes, respectively. 2. Cold sores: Lysine supplements can help reduce the frequency and severity of cold sore outbreaks by inhibiting the replication of the herpes simplex virus. 3. Depression: Lysine has been shown to increase levels of serotonin, a neurotransmitter that regulates mood, in the brain. 4. Hair loss: Lysine is important for the production of hair, and deficiency in lysine has been linked to hair loss. 5. Wound healing: Lysine is involved in the production of collagen, a protein that is important for wound healing. Overall, lysine is an important nutrient that plays a crucial role in many aspects of human health and is used in the treatment and prevention of various medical conditions.

In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.

Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.

In the medical field, "Amino Acids, Diamino" refers to a class of amino acids that contain two amino groups (-NH2) attached to a carbon atom. These amino acids are also known as diamines or diamino acids. Examples of diamino acids include ornithine and citrulline, which are important intermediates in the urea cycle, a metabolic pathway that helps to remove nitrogen waste from the body. Diamino acids are also found in some dietary supplements and are believed to have potential health benefits, such as improving athletic performance and supporting immune function. However, more research is needed to confirm these potential benefits and to fully understand the role of diamino acids in the body.

In the medical field, cations are positively charged ions that are found in the body fluids, such as blood and extracellular fluid. They are important for maintaining the proper balance of electrolytes in the body and for regulating various physiological processes, such as nerve function, muscle contraction, and fluid balance. Cations are classified based on their charge and chemical properties. The most common cations in the body include sodium (Na+), potassium (K+), calcium (Ca2+), magnesium (Mg2+), and hydrogen (H+). These ions play important roles in various bodily functions, and imbalances in their levels can lead to a range of health problems, such as muscle cramps, heart arrhythmias, and seizures. In medical testing, cations are often measured in blood or urine samples using various analytical techniques, such as ion-selective electrodes or atomic absorption spectroscopy. Monitoring cation levels is important for diagnosing and treating various medical conditions, such as kidney disease, acid-base disorders, and electrolyte imbalances.

Nitric oxide synthase (NOS) is an enzyme that plays a crucial role in the production of nitric oxide (NO) in the body. There are three main types of NOS: endothelial NOS (eNOS), neuronal NOS (nNOS), and inducible NOS (iNOS). eNOS is primarily found in the endothelial cells that line blood vessels and is responsible for producing NO in response to various stimuli, such as shear stress, hormones, and neurotransmitters. NO produced by eNOS helps to relax blood vessels and improve blood flow, which is important for maintaining cardiovascular health. nNOS is found in neurons and is involved in neurotransmission and synaptic plasticity. iNOS is induced in response to inflammation and is involved in the production of NO in immune cells and other tissues. Abnormal regulation of NOS activity has been implicated in a variety of diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. Therefore, understanding the mechanisms that regulate NOS activity is an important area of research in the medical field.

Glutamate plasma membrane transport proteins are a group of proteins that are responsible for transporting the neurotransmitter glutamate across the plasma membrane of neurons. These proteins play a crucial role in regulating the levels of glutamate in the synaptic cleft, which is the space between neurons where communication occurs. There are several different types of glutamate plasma membrane transport proteins, including the excitatory amino acid transporters (EAATs) and the vesicular glutamate transporters (VGLUTs). The EAATs are responsible for removing glutamate from the synaptic cleft and transporting it back into the neuron, while the VGLUTs are responsible for loading glutamate into synaptic vesicles for release. Disruptions in the function of glutamate plasma membrane transport proteins have been implicated in a number of neurological disorders, including epilepsy, stroke, and neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

Nitric Oxide Synthase Type II (NOS II) is an enzyme that is primarily found in the cells of the immune system, particularly in macrophages and neutrophils. It is responsible for producing nitric oxide (NO), a gas that plays a key role in the immune response by regulating inflammation and blood flow. NOS II is activated in response to various stimuli, such as bacterial or viral infections, and it produces large amounts of NO, which can help to kill invading pathogens and promote the recruitment of immune cells to the site of infection. However, excessive production of NO by NOS II can also lead to tissue damage and contribute to the development of chronic inflammatory diseases. In the medical field, NOS II is often studied in the context of inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and asthma, as well as in the development of cancer and cardiovascular disease. In some cases, drugs that inhibit NOS II activity have been used to treat these conditions, although their effectiveness and potential side effects are still being studied.

The Amino Acid Transport System L (LAT) is a group of transport proteins found in the plasma membrane of cells that facilitate the transport of large neutral amino acids (LNAA) across the membrane. These amino acids include alanine, arginine, cysteine, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, and valine. The LAT system is important for the uptake of amino acids from the bloodstream into cells, as well as for the export of amino acids from cells into the bloodstream. This system plays a crucial role in maintaining the balance of amino acids in the body and is particularly important for the proper functioning of the brain, muscles, and immune system. Disruptions in the LAT system can lead to a variety of medical conditions, including inborn errors of metabolism, such as maple syrup urine disease, and neurodegenerative diseases, such as Parkinson's disease.

Excitatory Amino Acid Transporter 5 (EAAT5) is a protein that plays a role in the regulation of the levels of excitatory neurotransmitters, such as glutamate, in the brain. It is a member of the excitatory amino acid transporter (EAAT) family of proteins, which are responsible for the reuptake of glutamate from the synaptic cleft back into neurons. EAAT5 is primarily expressed in astrocytes, which are a type of glial cell that play a key role in supporting and maintaining the function of neurons. It is thought that EAAT5 helps to regulate the levels of glutamate in the brain by facilitating the uptake of glutamate from the extracellular space back into astrocytes, where it can be metabolized or stored. Disruptions in the function of EAAT5 have been implicated in a number of neurological disorders, including epilepsy, stroke, and neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

Ornithine is an amino acid that is naturally present in the body and is involved in various metabolic processes. In the medical field, ornithine is sometimes used as a dietary supplement or medication to treat certain conditions. One of the primary functions of ornithine is to help the body produce the amino acid arginine, which is important for the production of nitric oxide, a molecule that helps to relax blood vessels and improve blood flow. Ornithine has also been studied for its potential to improve athletic performance, reduce muscle soreness, and enhance recovery after exercise. In addition, ornithine has been used to treat a variety of medical conditions, including liver disease, kidney disease, and metabolic disorders such as hyperammonemia, a condition in which there is an excess of ammonia in the blood. It has also been studied for its potential to treat certain types of cancer, although more research is needed to confirm its effectiveness. However, it is important to note that the use of ornithine as a supplement or medication should only be done under the guidance of a healthcare professional, as it can interact with other medications and may have side effects in some people.

Amino Acid Transport System X-AG refers to a specific type of amino acid transporter found in the plasma membrane of certain cells in the body. This transporter is responsible for the uptake of certain amino acids, such as alanine and glutamine, from the bloodstream into the cells. The X-AG transporter is a heterodimer composed of two subunits, SLC38A2 and SLC38A3, which work together to facilitate the transport of amino acids across the cell membrane. The X-AG transporter plays an important role in regulating the levels of these amino acids in the body and is involved in a number of physiological processes, including muscle metabolism and neurotransmitter synthesis. Disruptions in the function of the X-AG transporter have been linked to a number of diseases, including muscle wasting and certain neurological disorders.

Symporters are a type of membrane transport protein that move molecules across a cell membrane in the same direction, using the energy of a chemical gradient. In other words, symporters use the downhill flow of one molecule to drive the uphill transport of another molecule. Symporters are important for the transport of a variety of molecules across cell membranes, including ions, sugars, amino acids, and neurotransmitters. They play a crucial role in maintaining the proper balance of these molecules inside and outside of cells, and are involved in many physiological processes, such as nutrient uptake, nerve impulse transmission, and hormone secretion. In the medical field, symporters are often targeted for therapeutic purposes. For example, some drugs are designed to bind to symporters and block their function, which can be useful for treating conditions such as epilepsy, depression, and cancer. Other drugs are designed to activate symporters, which can be useful for delivering drugs across cell membranes and increasing their bioavailability.

Nitric oxide (NO) is a colorless, odorless gas that is produced naturally in the body by various cells, including endothelial cells in the lining of blood vessels. It plays a crucial role in the regulation of blood flow and blood pressure, as well as in the immune response and neurotransmission. In the medical field, NO is often studied in relation to cardiovascular disease, as it is involved in the regulation of blood vessel dilation and constriction. It has also been implicated in the pathogenesis of various conditions, including hypertension, atherosclerosis, and heart failure. NO is also used in medical treatments, such as in the treatment of erectile dysfunction, where it is used to enhance blood flow to the penis. It is also used in the treatment of pulmonary hypertension, where it helps to relax blood vessels in the lungs and improve blood flow. Overall, NO is a critical molecule in the body that plays a vital role in many physiological processes, and its study and manipulation have important implications for the treatment of various medical conditions.

Leucine is an essential amino acid that plays a crucial role in various biological processes in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. In the medical field, leucine is often used as a dietary supplement to promote muscle growth and recovery, particularly in athletes and bodybuilders. It is also used to treat certain medical conditions, such as phenylketonuria (PKU), a genetic disorder that affects the metabolism of amino acids. Leucine has been shown to have various physiological effects, including increasing protein synthesis, stimulating muscle growth, and improving insulin sensitivity. It is also involved in the regulation of gene expression and the production of neurotransmitters. However, excessive consumption of leucine can have negative effects on health, such as liver damage and increased risk of certain cancers. Therefore, it is important to consume leucine in moderation and as part of a balanced diet.

Membrane glycoproteins are proteins that are attached to the cell membrane through a glycosyl group, which is a complex carbohydrate. These proteins play important roles in cell signaling, cell adhesion, and cell recognition. They are involved in a wide range of biological processes, including immune response, cell growth and differentiation, and nerve transmission. Membrane glycoproteins can be classified into two main types: transmembrane glycoproteins, which span the entire cell membrane, and peripheral glycoproteins, which are located on one side of the membrane.

Membrane transport proteins are proteins that span the cell membrane and facilitate the movement of molecules across the membrane. These proteins play a crucial role in maintaining the proper balance of ions and molecules inside and outside of cells, and are involved in a wide range of cellular processes, including nutrient uptake, waste removal, and signal transduction. There are several types of membrane transport proteins, including channels, carriers, and pumps. Channels are pore-forming proteins that allow specific ions or molecules to pass through the membrane down their concentration gradient. Carriers are proteins that bind to specific molecules and change shape to transport them across the membrane against their concentration gradient. Pumps are proteins that use energy to actively transport molecules across the membrane against their concentration gradient. Membrane transport proteins are essential for the proper functioning of cells and are involved in many diseases, including cystic fibrosis, sickle cell anemia, and certain types of cancer. Understanding the structure and function of these proteins is important for developing new treatments for these diseases.

Organic Anion Transporters, Sodium-Dependent (OATs) are a group of membrane proteins that play a crucial role in the transport of organic anions across cell membranes. These transporters are found in various tissues throughout the body, including the liver, kidney, and brain. OATs are responsible for the uptake and elimination of a wide range of organic anions, including drugs, toxins, and metabolic waste products. They are also involved in the regulation of electrolyte balance and the maintenance of acid-base homeostasis. OATs function by coupling the transport of organic anions with the movement of sodium ions across the cell membrane. This process is known as secondary active transport and is an essential mechanism for maintaining the concentration gradients of organic anions and sodium ions across cell membranes. In the medical field, OATs are of particular interest because they play a critical role in the disposition of many drugs. Some drugs are substrates for OATs and are transported across cell membranes by these transporters, which can affect their absorption, distribution, metabolism, and elimination. Understanding the role of OATs in drug transport is important for the development of new drugs and for optimizing the use of existing drugs to minimize adverse effects and maximize therapeutic efficacy.

Organic anion transporters (OATs) are a group of membrane proteins that play a crucial role in the transport of organic anions across cell membranes. These transporters are found in various tissues and organs throughout the body, including the liver, kidney, and brain. OATs are responsible for the uptake and elimination of a wide range of organic anions, including drugs, toxins, and endogenous compounds such as bile acids and neurotransmitters. They are also involved in the regulation of electrolyte balance and the maintenance of acid-base homeostasis. There are several subtypes of OATs, including OAT1, OAT2, OAT3, and OAT4. Each subtype has a distinct tissue distribution and substrate specificity, and they can interact with a variety of drugs and other compounds. In the medical field, OATs are of particular interest because they play a critical role in the disposition of many drugs. Understanding the function and regulation of OATs can help to predict drug-drug interactions, optimize drug dosing, and develop new drugs with improved pharmacokinetic properties. Additionally, OATs have been implicated in the pathophysiology of several diseases, including liver and kidney disease, and may be potential targets for therapeutic intervention.

Cystine is a sulfur-containing amino acid that is an essential component of proteins. It is a dipeptide composed of two cysteine amino acids linked together by a disulfide bond. In the medical field, cystine is known to play a role in the formation of cystine stones in the urinary tract. These stones can cause significant pain and discomfort, and may require medical intervention to remove. Cystine is also involved in the structure and function of certain proteins, including enzymes and structural proteins. It is an important nutrient for the body, and is found in a variety of foods, including meat, poultry, fish, and dairy products.

Sodium is an essential mineral that plays a crucial role in various bodily functions. In the medical field, sodium is often measured in the blood and urine to assess its levels and monitor its balance in the body. Sodium is primarily responsible for regulating the body's fluid balance, which is essential for maintaining blood pressure and proper functioning of the heart, kidneys, and other organs. Sodium is also involved in nerve impulse transmission, muscle contraction, and the production of stomach acid. Abnormal levels of sodium in the body can lead to various medical conditions, including hyponatremia (low sodium levels), hypernatremia (high sodium levels), and dehydration. Sodium levels can be affected by various factors, including diet, medications, and underlying medical conditions. In the medical field, sodium levels are typically measured using a blood test called a serum sodium test or a urine test called a urine sodium test. These tests can help diagnose and monitor various medical conditions related to sodium levels, such as kidney disease, heart failure, and electrolyte imbalances.

ATP-binding cassette (ABC) transporters are a large family of membrane proteins that use the energy from ATP hydrolysis to transport a wide variety of molecules across cell membranes. These transporters are found in all kingdoms of life, from bacteria to humans, and play important roles in many physiological processes, including drug metabolism, detoxification, and the transport of nutrients and waste products across cell membranes. In the medical field, ABC transporters are of particular interest because they can also transport drugs and other xenobiotics (foreign substances) across cell membranes, which can affect the efficacy and toxicity of these compounds. For example, some ABC transporters can pump drugs out of cells, making them less effective, while others can transport toxins into cells, increasing their toxicity. As a result, ABC transporters are an important factor to consider in the development of new drugs and the optimization of drug therapy. ABC transporters are also involved in a number of diseases, including cancer, cystic fibrosis, and certain neurological disorders. In these conditions, the activity of ABC transporters is often altered, leading to the accumulation of toxins or the loss of important molecules, which can contribute to the development and progression of the disease. As a result, ABC transporters are an important target for the development of new therapies for these conditions.

GABA (gamma-aminobutyric acid) is a neurotransmitter that plays a crucial role in regulating the activity of neurons in the central nervous system. GABA plasma membrane transport proteins are proteins that are responsible for moving GABA across the plasma membrane of cells, including neurons. There are two main types of GABA plasma membrane transport proteins: GABA transporters (GATs) and GABA receptors. GATs are responsible for actively transporting GABA out of the cell, while GABA receptors are responsible for allowing GABA to enter the cell and bind to receptors, leading to changes in the activity of the neuron. GABA transporters are important for regulating the levels of GABA in the brain and maintaining the balance of neurotransmitters. Mutations in GABA transporter genes have been linked to a number of neurological disorders, including epilepsy and anxiety disorders.

In the medical field, "DNA, Complementary" refers to the property of DNA molecules to pair up with each other in a specific way. Each strand of DNA has a unique sequence of nucleotides (adenine, thymine, guanine, and cytosine), and the nucleotides on one strand can only pair up with specific nucleotides on the other strand in a complementary manner. For example, adenine (A) always pairs up with thymine (T), and guanine (G) always pairs up with cytosine (C). This complementary pairing is essential for DNA replication and transcription, as it ensures that the genetic information encoded in one strand of DNA can be accurately copied onto a new strand. The complementary nature of DNA also plays a crucial role in genetic engineering and biotechnology, as scientists can use complementary DNA strands to create specific genetic sequences or modify existing ones.

Cystinuria is a rare genetic disorder that affects the kidneys' ability to filter out certain amino acids, specifically cystine and ornithine, from the urine. This leads to the buildup of these amino acids in the urine, which can cause kidney stones and other complications. The condition is inherited in an autosomal recessive pattern, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the disorder. Cystinuria can affect both males and females of all ethnic backgrounds. Symptoms of cystinuria may include recurrent kidney stones, which can cause severe pain and may require surgery to remove. Other symptoms may include frequent urination, blood in the urine, and difficulty urinating. In some cases, the condition may also cause eye problems, such as cataracts or glaucoma. Treatment for cystinuria typically involves managing symptoms and preventing kidney stone formation. This may include drinking plenty of fluids, taking medications to prevent stone formation, and following a low-cystine diet. In severe cases, surgery may be necessary to remove kidney stones or to treat complications such as kidney damage or infection.

Ethylmaleimide is a chemical compound that is used in the medical field as a research tool to study the function of enzymes involved in the synthesis and breakdown of proteins. It works by inhibiting an enzyme called peptidyl-prolyl cis-trans isomerase (PPIase), which is involved in the folding and stability of proteins. By inhibiting PPIase, ethylmaleimide can be used to study the role of this enzyme in various cellular processes and diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. Ethylmaleimide is also used as a chemical probe to study the structure and function of proteins, particularly those involved in signal transduction pathways.

Cysteamine is a medication that is used to treat certain genetic disorders, such as cystinosis and homocystinuria. It works by reducing the amount of cystine in the body, which can help to prevent the buildup of cystine crystals in the kidneys and other organs. Cysteamine is usually taken by mouth in the form of tablets or capsules, and it may be taken in combination with other medications. It is important to follow the instructions of your healthcare provider when taking cysteamine, as the dosage and duration of treatment may vary depending on the specific condition being treated.

In the medical field, "Amino Acids, Cyclic" refers to a group of amino acids that have a ring structure in their side chain. These amino acids are also known as "cyclic amino acids" or "cyclic peptides." They are formed by the condensation of two or more amino acids through peptide bonds, resulting in a ring structure. Cyclic amino acids are found in various biological molecules, including peptides, proteins, and nucleic acids. They play important roles in various biological processes, such as enzyme catalysis, signal transduction, and gene regulation. Some examples of cyclic amino acids include proline, hydroxyproline, and ornithine. These amino acids have unique chemical and physical properties that make them useful in various medical applications, such as drug development, tissue engineering, and gene therapy.

In the medical field, "Amino Acids, Essential" refers to a group of nine amino acids that cannot be synthesized by the human body and must be obtained through the diet. These amino acids are essential for the growth and maintenance of tissues, as well as for the production of hormones and enzymes. They are considered "essential" because the body cannot produce them on its own and must obtain them from food sources. The nine essential amino acids are: isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine, and histidine.

Cystinosis is a rare genetic disorder that affects the body's ability to transport the amino acid cystine out of cells. This leads to the accumulation of cystine in various organs, particularly the kidneys, liver, and muscles. The accumulation of cystine in the kidneys can cause damage to the structure and function of the kidneys, leading to kidney failure. In the liver, cystine can cause damage to the bile ducts, leading to liver disease. In the muscles, cystine can cause weakness and wasting. Cystinosis is typically diagnosed in infancy or early childhood, and treatment involves managing the symptoms and preventing complications. This may include medications to help remove cystine from the body, dietary restrictions, and kidney transplantation in severe cases.

Renal aminoacidurias are a group of inherited metabolic disorders characterized by the accumulation of amino acids in the urine due to defects in the renal tubular reabsorption of these molecules. These disorders are caused by mutations in genes that encode for transport proteins in the renal tubules, leading to reduced or absent transport of specific amino acids across the tubular epithelium. As a result, the amino acids are excreted in the urine, leading to their accumulation in the blood and potentially causing symptoms such as kidney stones, neurological problems, and developmental delays. There are several types of renal aminoacidurias, including hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome, hyperargininemia, and hyperammonemia type I.

Glutamic acid is an amino acid that is naturally occurring in the human body and is essential for various bodily functions. It is a non-essential amino acid, meaning that the body can produce it from other compounds, but it is still important for maintaining good health. In the medical field, glutamic acid is sometimes used as a medication to treat certain conditions. For example, it is used to treat epilepsy, a neurological disorder characterized by recurrent seizures. Glutamic acid is also used to treat certain types of brain injuries, such as stroke, by promoting the growth of new brain cells. In addition to its medicinal uses, glutamic acid is also an important component of the diet. It is found in many foods, including meats, fish, poultry, dairy products, and grains. It is also available as a dietary supplement.

Glutamine is an amino acid that plays a crucial role in various physiological processes in the body. It is one of the most abundant amino acids in the human body and is involved in a wide range of functions, including: 1. Energy production: Glutamine is a major source of fuel for cells in the body, particularly in the muscles and immune system. 2. Protein synthesis: Glutamine is a key building block for proteins and is essential for the growth and repair of tissues. 3. Immune function: Glutamine plays a critical role in the function of the immune system, particularly in the production of white blood cells. 4. Gut health: Glutamine is important for maintaining the health of the gut lining and preventing damage to the gut. In the medical field, glutamine is often used as a supplement to support various health conditions, including: 1. Wound healing: Glutamine has been shown to promote wound healing and reduce the risk of infection. 2. Cancer treatment: Glutamine supplementation may help to reduce the side effects of cancer treatment, such as fatigue and muscle wasting. 3. Immune system support: Glutamine supplementation may help to boost the immune system and reduce the risk of infections. 4. Digestive disorders: Glutamine may be helpful in treating digestive disorders such as inflammatory bowel disease and irritable bowel syndrome. Overall, glutamine is an important nutrient that plays a crucial role in many physiological processes in the body and may be beneficial in supporting various health conditions.

Putrescine is a polyamine compound that is naturally produced in the body and is also found in many plants and animals. It is a colorless, odorless, and water-soluble compound that is synthesized from the amino acid ornithine and decarboxylation of arginine. In the medical field, putrescine has been studied for its potential therapeutic effects in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. It has been shown to have anti-inflammatory, anti-cancer, and anti-apoptotic effects, and may also have a role in regulating cell growth and differentiation. Putrescine has also been used as a food additive and preservative, and is found in some natural products such as mushrooms and fermented foods. However, excessive consumption of putrescine may have adverse effects on health, including nausea, vomiting, and diarrhea.

Monocarboxylic acid transporters (MCTs) are a family of membrane proteins that are responsible for the transport of monocarboxylic acids across cell membranes. These transporters play a crucial role in the metabolism of various compounds, including lactate, ketone bodies, and fatty acids. In the medical field, MCTs are of particular interest because they are involved in the transport of lactate, which is an important metabolic substrate in many tissues, including the brain, heart, and skeletal muscle. MCTs are also involved in the transport of ketone bodies, which are produced in the liver during periods of fasting or starvation and can be used as an alternative energy source by other tissues. MCTs are expressed in a variety of tissues, including the liver, kidney, and small intestine, and are involved in a number of physiological processes, including nutrient absorption, energy metabolism, and acid-base balance. In some cases, MCTs can also be involved in the transport of drugs and other xenobiotics, which can have important implications for drug metabolism and toxicity. Disruptions in MCT function can lead to a number of medical conditions, including lactate acidosis, which is a condition characterized by high levels of lactate in the blood, and ketosis, which is a metabolic state characterized by high levels of ketone bodies in the blood. MCTs are also being studied as potential targets for the treatment of a variety of diseases, including cancer, diabetes, and neurological disorders.

Hartnup disease is a rare genetic disorder that affects the body's ability to absorb certain amino acids from the diet. Specifically, it impairs the absorption of tryptophan, which is an essential amino acid that is necessary for the production of serotonin, a neurotransmitter that regulates mood, sleep, and other bodily functions. People with Hartnup disease may experience symptoms such as diarrhea, vomiting, abdominal pain, and skin rashes. They may also have difficulty absorbing other nutrients, such as vitamin B6 and niacin, which can lead to additional health problems. Hartnup disease is inherited in an autosomal recessive pattern, meaning that a person must inherit two copies of the mutated gene (one from each parent) in order to develop the condition. There is no cure for Hartnup disease, but symptoms can be managed with dietary changes and supplements to ensure adequate intake of essential nutrients.

In the medical field, "Amino Acids, Aromatic" refers to a group of amino acids that contain an aromatic ring in their side chain. These amino acids are important building blocks of proteins and play various roles in the body, including as neurotransmitters, hormones, and enzymes. The nine amino acids that are classified as aromatic are phenylalanine, tyrosine, tryptophan, histidine, methionine, and cysteine. These amino acids are essential for human health and must be obtained through the diet, as the body cannot produce them on its own. A deficiency in any of these amino acids can lead to various health problems, such as intellectual disabilities, skin disorders, and metabolic disorders. Therefore, it is important to ensure that the diet includes adequate amounts of these amino acids.

Vesicular inhibitory amino acid transport proteins (VIAATs) are a family of proteins that play a role in the transport of inhibitory neurotransmitters, such as gamma-aminobutyric acid (GABA) and glycine, into synaptic vesicles in neurons. These vesicles are small sacs that store neurotransmitters and release them into the synaptic cleft when a neuron is activated. VIAATs are responsible for the uptake of inhibitory neurotransmitters from the cytoplasm into the synaptic vesicles, where they can be stored and later released to inhibit the activity of neighboring neurons. Dysregulation of VIAATs has been implicated in a number of neurological disorders, including epilepsy, anxiety disorders, and schizophrenia.

Amino acid metabolism, inborn errors refer to a group of genetic disorders that affect the metabolism of amino acids, which are the building blocks of proteins. These disorders are caused by mutations in genes that encode enzymes involved in the metabolism of amino acids, leading to a deficiency or dysfunction of the corresponding enzyme. As a result, the normal metabolic pathways are disrupted, leading to the accumulation of toxic intermediates and the deficiency of essential amino acids. Inborn errors of amino acid metabolism can cause a wide range of symptoms, including developmental delays, intellectual disability, seizures, and neurological problems. Early diagnosis and treatment are crucial to prevent irreversible damage and improve the quality of life of affected individuals.

Nucleotide transport proteins are a group of proteins that are responsible for the transport of nucleotides across cell membranes. These proteins play a crucial role in the metabolism of nucleotides, which are the building blocks of DNA and RNA. There are several types of nucleotide transport proteins, including concentrative nucleoside transporters (CNTs), equilibrative nucleoside transporters (ENTs), and nucleotide-specific transporters (NSTs). These proteins are found in various tissues and cells throughout the body, and they are involved in a wide range of physiological processes, including energy metabolism, immune function, and neurotransmission. Mutations in nucleotide transport proteins can lead to a variety of diseases, including inherited disorders of metabolism and cancer.

Polyamines are organic compounds that contain multiple amine groups (-NH2) and are typically derived from the amino acids ornithine and lysine. They are found in all living organisms and play important roles in various biological processes, including cell growth and division, DNA synthesis, and regulation of gene expression. In the medical field, polyamines have been studied for their potential therapeutic applications. For example, polyamines have been shown to have anti-inflammatory and anti-cancer properties, and may be useful in the treatment of various diseases, including cancer, inflammatory bowel disease, and neurodegenerative disorders. Additionally, polyamines have been used as markers for certain types of cancer, and may be useful in the diagnosis and monitoring of these diseases.

Biogenic polyamines are a group of naturally occurring organic compounds that are synthesized in living organisms. They are primarily composed of three amino acids: ornithine, lysine, and arginine. Biogenic polyamines play important roles in various biological processes, including cell growth and division, DNA synthesis and repair, and regulation of gene expression. In the medical field, biogenic polyamines have been studied for their potential therapeutic applications. For example, some studies have suggested that biogenic polyamines may have anti-cancer properties, as they can inhibit the growth and proliferation of cancer cells. Additionally, biogenic polyamines have been shown to have anti-inflammatory effects, which may be useful in the treatment of various inflammatory diseases. Overall, biogenic polyamines are an important class of compounds that have a wide range of potential applications in the medical field.

Amino Acid Transport Disorders, Inborn are a group of genetic disorders that affect the ability of the body to transport amino acids across cell membranes. Amino acids are the building blocks of proteins and are essential for many bodily functions. Inborn errors of amino acid transport can lead to a variety of symptoms, including intellectual disability, developmental delays, seizures, and other neurological problems. These disorders are typically diagnosed through genetic testing and can be managed with dietary restrictions and supplementation with specific amino acids.

Beta-alanine is an amino acid that is naturally produced in the body and is also available as a dietary supplement. It is a building block of proteins and is involved in the production of carnosine, a dipeptide that is found in muscle tissue. Carnosine has been shown to have a number of potential health benefits, including improved exercise performance, enhanced muscle endurance, and increased mental alertness. In the medical field, beta-alanine is sometimes used to treat conditions such as muscle fatigue and weakness, as well as to improve athletic performance. It is also sometimes used to treat certain types of nerve pain and to reduce the symptoms of certain neurological disorders. However, more research is needed to fully understand the potential benefits and risks of beta-alanine supplementation.

Excitatory amino acids are a group of amino acids that are involved in the transmission of signals in the nervous system. They are called "excitatory" because they cause the release of neurotransmitters that stimulate the activity of neurons. The most well-known excitatory amino acids are glutamate and aspartate. These amino acids are found in high concentrations in the brain and are involved in many important functions, including learning, memory, and the regulation of mood. In excessive amounts, however, excitatory amino acids can be toxic to neurons and have been implicated in the development of neurological disorders such as epilepsy and stroke.

Aspartic acid is an amino acid that is naturally occurring in the human body. It is a non-essential amino acid, meaning that it can be synthesized by the body from other compounds and does not need to be obtained through the diet. Aspartic acid is found in high concentrations in the brain and spinal cord, and it plays a role in various physiological processes, including the production of neurotransmitters and the regulation of acid-base balance in the body. In the medical field, aspartic acid is sometimes used as a diagnostic tool to measure the function of the liver and kidneys, as well as to monitor the progression of certain diseases, such as cancer and HIV. It is also used as a dietary supplement in some cases.

Alanine is an amino acid that is a building block of proteins. It is an essential amino acid, meaning that it cannot be synthesized by the body and must be obtained through the diet. Alanine plays a number of important roles in the body, including: 1. Energy production: Alanine can be converted into glucose, which is a source of energy for the body. 2. Muscle function: Alanine is involved in the metabolism of muscle tissue and can help to prevent muscle damage. 3. Liver function: Alanine is an important component of the liver's detoxification process and can help to protect the liver from damage. 4. Acid-base balance: Alanine helps to regulate the body's acid-base balance by buffering excess acid in the blood. In the medical field, alanine is often used as a biomarker to assess liver function. Elevated levels of alanine in the blood can indicate liver damage or disease. Alanine is also used as a dietary supplement to support muscle growth and recovery.

Glycine is an amino acid that is essential for the proper functioning of the human body. It is a non-essential amino acid, meaning that the body can synthesize it from other compounds, but it is still important for various physiological processes. In the medical field, glycine is used as a dietary supplement to support muscle growth and recovery, as well as to improve sleep quality. It is also used in the treatment of certain medical conditions, such as liver disease, as it can help to reduce the buildup of toxins in the liver. Glycine is also used in the production of various medications, including antibiotics and tranquilizers. It has been shown to have a calming effect on the nervous system and may be used to treat anxiety and other mental health conditions. Overall, glycine is an important nutrient that plays a vital role in many physiological processes in the body.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

... is a protein that in humans is encoded by the SLC7A1 gene. Solute carrier ... Hammermann R, Brunn G, Racké K (2002). "Analysis of the genomic organization of the human cationic amino acid transporters CAT- ... Schnorr O, Suschek CV, Kolb-Bachofen V (June 2003). "The importance of cationic amino acid transporter expression in human skin ... "Entrez Gene: SLC7A1 solute carrier family 7 (cationic amino acid transporter, y+ system), member 1". Yoshimoto T, Yoshimoto E, ...
... is a protein that in humans is encoded by the SLC7A2 gene. SLC7A2+protein,+human at the U.S. ... 1997). "Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three related carriers with distinct transport ... Hammermann R, Brunn G, Racké K (2002). "Analysis of the genomic organization of the human cationic amino acid transporters CAT- ... Schnorr O, Suschek CV, Kolb-Bachofen V (2003). "The importance of cationic amino acid transporter expression in human skin". J ...
... is a protein that in humans is encoded by the SLC7A4 gene. SLC7A4+protein,+human at the U.S. ... Hammermann R, Brunn G, Racke K (Oct 2001). "Analysis of the genomic organization of the human cationic amino acid transporters ... "Entrez Gene: SLC7A4 solute carrier family 7 (cationic amino acid transporter, y+ system), member 4". Muñoz L, Lasa A, ... "The gene encoding a cationic amino acid transporter (SLC7A4) maps to the region deleted in the velocardiofacial syndrome". ...
... is a protein that in humans is encoded by the SLC7A3 gene. SLC7A3 is a member of the system ... Vekony N, Wolf S, Boissel JP, Gnauert K, Closs EI (Oct 2001). "Human cationic amino acid transporter hCAT-3 is preferentially ... Ito K, Groudine M (1997). "A new member of the cationic amino acid transporter family is preferentially expressed in adult ... 1999). "Neuron-specific expression of cationic amino acid transporter 3 in the adult rat brain". Brain Res. 838 (1-2): 158-65. ...
... , also known as cationic amino acid transporter, y+ system, is a protein that in humans is encoded ... cationic amino acid transporter". Pfeiffer R, Rossier G, Spindler B, Meier C, Kühn L, Verrey F (January 1999). "Amino acid ... Bröer A, Wagner CA, Lang F, Bröer S (August 2000). "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine ... Heterodimeric amino acid transporter GRCh38: Ensembl release 89: ENSG00000103064 - Ensembl, May 2017 GRCm38: Ensembl release 89 ...
"Entrez Gene: solute carrier family 7 (cationic amino acid transporter". "UniProt". www.uniprot.org. Kaira K, Oriuchi N, Imai H ... Large neutral amino acids transporter small subunit 1, also known as 4F2 light chain, or CD98 light chain is a protein that in ... 2009). "L-type amino acid transporter 1 (LAT1) is frequently expressed in thymic carcinomas but is absent in thymomas". J Surg ... 2009). "L-type amino-acid transporter 1 as a novel biomarker for high-grade malignancy in prostate cancer". Pathol. Int. 59 (1 ...
Currents of Opposite Polarity Evoked by Neutral and Cationic Amino Acids in Neutral and Basic Amino Acid Transporter cRNA- ... amino acid transport on substrate affinity of the heteromeric b(0,+) amino acid transporter". J. Biol. Chem. 275 (19): 14331- ... "Effects of truncation of the COOH-terminal region of a Na+-independent neutral and basic amino acid transporter on amino acid ... dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1". Pras E ...
"Entrez Gene: SLC7A8 solute carrier family 7 (cationic amino acid transporter, y+ system), member 8". Maruyama K, Sugano S (1994 ... an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids". J Biol Chem. 274 ... Large neutral amino acids transporter small subunit 2 is a protein that in humans is encoded by the SLC7A8 gene. Heterodimeric ... 2000). "LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine". J. Biol. Chem. 274 (49 ...
"Entrez Gene: SLC7A7 solute carrier family 7 (cationic amino acid transporter, y+ system), member 7". Pfeiffer, R; Rossier G; ... 1999). "Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid ... Y+L amino acid transporter 1 is a protein that in humans is encoded by the SLC7A7 gene. SLC7A7 has been shown to interact with ... "Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid ...
... is processed from hcr mRNA and may downregulate the high affinity cationic amino acid transporter CAT-1". RNA Biol. 1 (2): 106- ... Coiled-coil alpha-helical rod protein 1, also known as CCHCR1, is a protein which in humans is encoded by the CCHCR1 gene. The ... It is also known as Coiled-Coil Alphahelical Rod Protein 1, C6orf18, Putative Gene 8 Protein, SBP, HCR (A-Helix Coiled-Coil Rod ... "Entrez Gene: CCHCR1 coiled-coil alpha-helical rod protein 1". Asumalahti K, Laitinen T, Itkonen-Vatjus R, Lokki ML, Suomela S, ...
... is processed from hcr mRNA and may downregulate the high affinity cationic amino acid transporter CAT-1". RNA Biology. 1 (2): ... miR-122 is highly expressed in the liver, where it has been implicated as a regulator of fatty-acid metabolism in mouse studies ... This change is noted before increased amino-transferase activity, making it an early indicator of liver disease and ... Fabani MM, Gait MJ (February 2008). "miR-122 targeting with LNA/2'-O-methyl oligonucleotide mixmers, peptide nucleic acids (PNA ...
... heavy subunits of heteromeric amino acid transporters (6) Bacterial Leucine Transporter (LeuT) (7) cationic amino acid ... Solute carrier family Amino acid transport Amino acid transport, acidic Amino acid transport, basic Amino acid transport ... proton-coupled amino acid transporter (38) System A & N, sodium-coupled neutral amino acid transporter Vesicular inhibitory ... An amino acid transporter is a membrane transport protein that transports amino acids. They are mainly of the solute carrier ...
... dependent neutral and cationic amino acid transporter B(0+)". J Biol Chem. 274 (34): 23740-5. doi:10.1074/jbc.274.34.23740. ... dependent neurotransmitter transporter family and transports both neutral and cationic amino acids in an Na+- and Cl−-dependent ... "Polymorphisms in the amino acid transporter solute carrier family 6 (neurotransmitter transporter) member 14 gene contribute to ... Sloan JL, Grubb BR, Mager S (2003). "Expression of the amino acid transporter ATB 0+ in lung: possible role in luminal protein ...
This gene is predicted to encode a glycosylated, cationic amino acid transporter protein with 14 transmembrane domains. This ... hair cells and primary endothelial cells and its protein is predicted to mediate lysosomal uptake of cationic amino acids. In ... 8 (eabk0942): 1-17. doi:10.1126/sciadv.abk0942. PMC 8993119. PMID 35394837. This article incorporates text from the United ... "Docking motif-guided mapping of the interactome of protein phosphatase-1". Chemistry & Biology. 16 (4): 365-71. doi:10.1016/j. ...
... cationic amino acid transporter 2 MeSH D12.776.157.530.200.374.750 - amino acid transport system y+l MeSH D12.776.157.530. ... amino acid transport system y+ MeSH D12.776.157.530.200.374.600.200 - cationic amino acid transporter 1 MeSH D12.776.157.530. ... excitatory amino acid transporter 2 MeSH D12.776.157.530.200.249.500.500.875 - excitatory amino acid transporter 3 MeSH D12.776 ... excitatory amino acid transporter 4 MeSH D12.776.157.530.200.249.500.500.968 - excitatory amino acid transporter 5 MeSH D12.776 ...
... cationic amino acid transporter 2 MeSH D12.776.543.585.200.374.750 - amino acid transport system y+l MeSH D12.776.543.585. ... amino acid transport system y+ MeSH D12.776.543.585.200.374.600.200 - cationic amino acid transporter 1 MeSH D12.776.543.585. ... excitatory amino acid transporter 2 MeSH D12.776.543.585.200.249.500.500.875 - excitatory amino acid transporter 3 MeSH D12.776 ... excitatory amino acid transporter 4 MeSH D12.776.543.585.200.249.500.500.968 - excitatory amino acid transporter 5 MeSH D12.776 ...
Das P, Lahiri A, Lahiri A, Sen M, Iyer N, Kapoor N, Balaji KN, Chakravortty D, 2010, Cationic Amino Acid Transporters and ... Peptide transporter YjiY influences the expression of the virulence gene mgtC to regulate biofilm formation in Salmonella. FEMS ... Das P, Lahiri A, Chakravortty D, 2009, Novel role of the nitrite transporter NirC in Salmonella pathogenesis: SPI2-dependent ... Mayuri Gogoi, Akshay Datey, Chakravortty D, 2016, Arginine transporters and its role in pathogenesis, Current Opinion in ...
... cationic amino acid transporter/glycoprotein-associated cationic amino acid transporters (SLC7A1, SLC7A2, SLC7A3, SLC7A4) ... copper transporter (SLC31A1, SLC31A2) vesicular inhibitory amino acid transporter (SLC32A1) Acetyl-CoA transporter (SLC33A1) ... NPC-type cholesterol transporters (NPC1(SLC65A1), NPC1L1(SLC65A2)) Cationic amino acid exporters (SLC66A1, SLC66A2, SLC66A3, ... Ammonia transporter (RHAG(SLC42A1), RHBG(SLC42A2), RHCG(SLC42A3)) Na+-independent, system-L like amino acid transporter ( ...
The Cationic Amino Acid Transporter (CAT) Family 2.A.3.4: The Amino Acid/Choline Transporter (ACT) Family 2.A.3.5: The ... The Amino Acid Transporter (AAT) Family 2.A.3.2: The Basic Amino Acid/Polyamine Antiporter (APA) Family 2.A.3.3: ... "The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations ... are amino acid receptors rather than transporters and are truncated at their C-termini, relative to the transporters, having 10 ...
3.A.1.3 Polar Amino Acid Uptake Transporter (PAAT) 3.A.1.4 Hydrophobic Amino Acid Uptake Transporter (HAAT) 3.A.1.5 Peptide/ ... Pgp is known to transport organic cationic or neutral compounds. A few ABCC family members, also known as MRP, have also been ... Opine/Nickel Uptake Transporter (PepT) 3.A.1.6 Sulfate/Tungstate Uptake Transporter (SulT) 3.A.1.7 Phosphate Uptake Transporter ... Plant ABCB transporters have shown to transport the phytohormone indole-3-acetic acid ( IAA), also known as auxin, the ...
... of cationic amino acids such as L-arginine in various cell types HCP1 is identical to the proton-coupled folate transporter ( ... HCP1 is also known as proton-coupled folate transporter (PCFT), as it was initially identified as a transporter for folate, a ... HCP1 is a proton-coupled transporter meaning that HCP1 relies on a proton gradient across the cell membrane to transport heme ... HCP1 is the only known heme transporter expressed in the small intestine and is therefore unique in its function and expression ...
The attachment of the amino acid lysine slows down the relative amount of dextroamphetamine available to the blood stream. ... VMAT2 is the CNS vesicular transporter for not only the biogenic amines DA, NE, EPI, 5-HT, and HIS, but likely also for the ... Conversely, an acidic pH means the drug is predominantly in a water-soluble cationic (salt) form, and less is absorbed. ... Chemically, lisdexamfetamine is composed of the amino acid L-lysine, attached to dextroamphetamine. Lisdexamfetamine was ...
... charged amino acids and non-polar, hydrophobic amino acids. These two types of structures are referred to as polycationic or ... This feature requires the orientation of cationic -hydrophilic on one side, and hydrophobic residues on the other side of the ... CPPs found applications as transporters of contrast agents across plasma membranes. These contrast agents are able to label the ... CPPs typically have an amino acid composition that either contains a high relative abundance of positively charged amino acids ...
M3). A cationic amino acid at position 2 is largely responsible for the inhibiting effect of S107. The ratio of S105 to S107 ... Portal: Biology As of 10 March 2016, this article is derived in whole or in part from Transporter Classification Database (TCDB ... The latter protein, S107, is a 2-amino acid extension of the former protein, S105, due to a different translational initiation ... Like the N-terminal 2 amino acid extension in S107, they influence the timing of lysis by a charge dependent mechanism. ...
SLC1A1 is excitatory amino acid transporter 3 (EAAT3), a glutamate transporter located in neurons, SLC22A3 is an extraneuronal ... Conversely, an acidic pH means the drug is predominantly in a water-soluble cationic (salt) form, and less is absorbed. ... Malenka RC, Nestler EJ, Hyman SE (2009). "Chapter 5: Excitatory and Inhibitory Amino Acids". In Sydor A, Brown RY (eds.). ... The human serotonin transporter and norepinephrine transporter do not contain zinc binding sites. 4-Hydroxyamphetamine has been ...
Hong W, Wu Z, Fang Z, Huang J, Huang H, Hong M (December 2015). "Amino Acid Residues in the Putative Transmembrane Domain 11 of ... as well as neutral and even cationic compounds. They also transport an extremely diverse range of drug compounds, ranging from ... Along with the organic cation transporters and the ATP-binding cassette transporters, the OATPs play an important role in the ... As of this edit, this article uses content from "2.A.60 The Organo Anion Transporter (OAT) Family", which is licensed in a way ...
It is a synthetic cyclic beta hairpin peptidomimetic based on the cationic antimicrobial peptide protegrin I (PG-1) and the ... highly active and selective against the protein transporter LptD of Pseudomonas aeruginosa. In preclinical studies the compound ... "Macrocyclic hairpin mimetics of the cationic antimicrobial peptide protegrin I: a new family of broad‐spectrum antibiotics". ... "Properties and structure-activity studies of cyclic β-hairpin peptidomimetics based on the cationic antimicrobial peptide ...
It is a chemical substance which is naturally created from the amino acid arginine. Agmatine has been shown to exert modulatory ... Including: ATP-sensitive K+ channels, voltage-gated Ca2+ channels, and acid-sensing ion channels (ASICs). Membrane transporters ... Due to its ability to pass through open cationic channels, agmatine has also been used as a surrogate metric of integrated ... Amino Acids. 26 (4): 321-9. doi:10.1007/s00726-004-0078-4. PMID 15290337. S2CID 23116711. Pinthong, D.; Wright, I. K.; Hanmer, ...
Zhang L, Lee HK, Pruess TH, White HS, Bulaj G (March 2009). "Synthesis and applications of polyamine amino acid residues: ... In their cationic ammonium form, they bind to DNA, and, in structure, they represent compounds with cations that are found at ... molecular requirements for the selective delivery of polyamine conjugates into cells containing active polyamine transporters ... A polyamine is an organic compound having more than two amino groups. Alkyl polyamines occur naturally, but some are synthetic ...
... of amino acid residues belong to niches bound to a δ+ group, while another 7% have the conformation but no single cationic ... A Sodium ion bound in similar ways at the domain interface is seen in several other Na+-coupled transporters. The Hsp70 ... In the area of protein structural motifs, niches are three or four amino acid residue features in which main-chain CO groups ... Torrance, GM; Leader DP (2009). "A Novel Main Chain Motif in Proteins Bridged by Cationic Groups: The Niche". Journal of ...
... amino acids), namely lysine, arginine, and ornithine. Learn about this gene and related health conditions. ... L amino acid transporter 1 (y+LAT-1), which is involved in transporting certain building blocks of protein ( ... of a complex called the heterodimeric cationic amino acid transporter. This subunit is responsible for binding to the amino ... SOLUTE CARRIER FAMILY 7 (CATIONIC AMINO ACID TRANSPORTER, y+ SYSTEM), MEMBER 7; SLC7A7 ...
69:713-719). Moloney MLV envelopes confer an ecotropic host range because they bind to a murine cationic amino acid transporter ... confer an ecotropic host range because they attach selectively to a peptide loop in d e murine cationic amino acid transporter ... confer an ecotropic host range because they attach selectively to a peptide loop in the murine cationic amino acid transporter ... A method of screening nucleic acid sequences for those which encode an amino acid sequence which may or may not be cleaved by a ...
Cationic amino acid transporter mRNA expression in rat kidney and liver.. Kidney Int Suppl. 67, 54:136 (1998) ... Distinct effects of single amino-acid changes to tuberin on the function of the tuberin-hamartin complex.. Eur J Hum Genet. 13 ... Nuc Acids Res. 26:229 (1998). U. Grau, H.-G. Klein, C. Detter, H. Mair, A. Welz, D. Seidel, B Reichart.. A novel mutation in ... The role of cell-free nucleic acid diagnostics in clinical chemistry and pathology. J Lab Med 40(5):291 (2016) ...
Cationic amino acid transporter, CAAT (462 aas; 12 TMSs) Accession Number:. Q9HJ13. ... References (1). [1] "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A.et.al. 11029001 ... 1: MHGIFQSMGQ VAPAADIAIL LVATFSIAGS RTILSVIFGW LVYAIFMVTP YQFSKYKSNA 61: GSYYAFAAGS TESGKLGPVT ALSFMYYDIT GAAFGILGLS SFIFLISPRI ...
... cationic amino acid transporter 1 (CAT-1) gene is a target of miR-122. In this study, we found that CAT-1 protein levels were ... Expression of fatty acid synthase (FASN), acetyl-CoA carboxylase (ACC), and GRIA3 was detected by qRT-PCR and western blot. RNA ... METHODS: NAFLD cell and mouse models were established by treating with free fatty acid (FFA) and feeding a high fat diet (HFD ... LncRNA NEAT1, miR-212-5p, and GRIA3 expression were detected both in high fatty acid-treated hepatocytes cells and NAFLD ...
... organic cationic substrate). The deduced amino acid sequence of our hOAT3 showed 85% identity with that of hOAT3*. The major ... The deduced amino acid sequence of hOAT3 showed 36 to 51% identity to those of other members of the OAT family. Northern blot ... The amino acid sequence of hOAT3 showed 85, 51, 36, and 44% identity with those of hOAT3*, hOAT1, rOAT2, and hOAT4, ... The amino acid sequence of hOAT3 aligned with those of hOAT3, hOAT1, rOAT2, and hOAT4. Boxed residues indicate conserved ...
... a member of a cationic amino acid transporter subfamily in the Trypanosoma cruzi genome. Parasites and Vectors, 8 (1). ... Identification and functional characterization of a novel arginine/ornithine transporter, ... Kirkwood, Caitlin (2015) THE ROLE OF NEURONAL CALCIUM SENSOR PROTEIN VILIP-1 IN Aβ-INDUCED NEURONAL DEATH IN ALZHEIMER DISEASE. ...
Cationic Amino Acid Transporter 2 D12.776.157.530.937.375.300 D12.776.543.585.937.375.300 CD4 Lymphocyte Count G4.170.107.595. ... Excitatory Amino Acid Transporter 2 D12.776.157.530.937.250.500.750 D12.776.543.585.937.250.500.750 Excitatory Amino Acid ... Excitatory Amino Acid Transporter 4 D12.776.157.530.937.250.500.937 D12.776.543.585.937.250.500.937 Excitatory Amino Acid ... Cationic Amino Acid Transporter 1 D12.776.157.530.937.375.200 D12.776.543.585.937.375.200 ...
Cationic Amino Acid Transporter 2 D12.776.157.530.937.375.300 D12.776.543.585.937.375.300 CD4 Lymphocyte Count G4.170.107.595. ... Excitatory Amino Acid Transporter 2 D12.776.157.530.937.250.500.750 D12.776.543.585.937.250.500.750 Excitatory Amino Acid ... Excitatory Amino Acid Transporter 4 D12.776.157.530.937.250.500.937 D12.776.543.585.937.250.500.937 Excitatory Amino Acid ... Cationic Amino Acid Transporter 1 D12.776.157.530.937.375.200 D12.776.543.585.937.375.200 ...
Cationic Amino Acid Transporter 2 D12.776.157.530.937.375.300 D12.776.543.585.937.375.300 CD4 Lymphocyte Count G4.170.107.595. ... Excitatory Amino Acid Transporter 2 D12.776.157.530.937.250.500.750 D12.776.543.585.937.250.500.750 Excitatory Amino Acid ... Excitatory Amino Acid Transporter 4 D12.776.157.530.937.250.500.937 D12.776.543.585.937.250.500.937 Excitatory Amino Acid ... Cationic Amino Acid Transporter 1 D12.776.157.530.937.375.200 D12.776.543.585.937.375.200 ...
Cationic Amino Acid Transporter 2 D12.776.157.530.937.375.300 D12.776.543.585.937.375.300 CD4 Lymphocyte Count G4.170.107.595. ... Excitatory Amino Acid Transporter 2 D12.776.157.530.937.250.500.750 D12.776.543.585.937.250.500.750 Excitatory Amino Acid ... Excitatory Amino Acid Transporter 4 D12.776.157.530.937.250.500.937 D12.776.543.585.937.250.500.937 Excitatory Amino Acid ... Cationic Amino Acid Transporter 1 D12.776.157.530.937.375.200 D12.776.543.585.937.375.200 ...
Cationic Amino Acid Transporter 2 D12.776.157.530.937.375.300 D12.776.543.585.937.375.300 CD4 Lymphocyte Count G4.170.107.595. ... Excitatory Amino Acid Transporter 2 D12.776.157.530.937.250.500.750 D12.776.543.585.937.250.500.750 Excitatory Amino Acid ... Excitatory Amino Acid Transporter 4 D12.776.157.530.937.250.500.937 D12.776.543.585.937.250.500.937 Excitatory Amino Acid ... Cationic Amino Acid Transporter 1 D12.776.157.530.937.375.200 D12.776.543.585.937.375.200 ...
Glycine transporter subfamily in the IUPHAR/BPS Guide to PHARMACOLOGY. ... neutral cationic amino acid transporter B0,+ , sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) , ... 2004) Transport of amino acid esters and the amino-acid-based prodrug valganciclovir by the amino acid transporter ATB(0,+). ... solute carrier family 6 (neurotransmitter transporter), member 14 , Atb0+ , colonic system B0+ amino acid transporter , ...
High affinity cationic amino acid transporter 1. SLC7A1. 13q12-q14. P30825 details. ... High affinity cationic amino acid transporter 1. SLC7A1. 13q12-q14. P30825 details. ... 3. High affinity cationic amino acid transporter 1. General function:. Involved in transport. Specific function:. High-affinity ... Belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L- ...
Hypomorphic variants of cationic amino acid transporter 3 in males with autism spectrum disorders. Nava Caroline, et al. Amino ... Nature genetics 2018 0 (1) 106-116. * Phenotypic shift in copy number variants: Evidence in 16p11.2 duplication syndrome. ... The American journal of psychiatry 2021 0 (1) 77-86. * [Adolescent with a schizophreniform disorder and recurrent 16p11.2 ... Genetics in medicine : official journal of the American College of Medical Genetics 2023 25(1) 151-154 ...
Low affinity cationic amino acid transporter 2 is a protein that in humans is encoded by the SLC7A2 gene.[1][2]. உங்கள் ... low affinity cationic amino acid transporter 2; CAT-2; CAT2; solute carrier family 7 member 2 (SLC7A2, ATRC2) produces ... http://www.anvita.info/wiki/Cationic_Amino_Acid_Transporter_2. அது ப்ரோட்டின் தயாரிக்கும் ஒரு ஜீன்.அதில் ஏற்படும் மாற்றம் ... 1.இந்தSLC7A2 ஜீன் குப்பை ஜீனா?. ஆம்/இல்லை. 2.இன்ட்ரான்+லைன்+சைன் குப்பை ஜீன்களா?. ஆம்/இல்லை. 3.இன்ட்ரான்+லைன்+சைன் ஆகிய குப்பை ...
Mouse CAT1(Cationic Amino Acid Transporter 1) ELISA Kit. *Mouse CRLF1(Cytokine Receptor Like Factor 1) ELISA Kit ... Mouse FFAR2(Free Fatty Acid Receptor 2) ELISA Kit. *Human COPRS(Coordinator Of PRMT5 And Differentiation Stimulator) ELISA Kit ... Hyaluronic Acid Modified Curcumin-Loaded Chitosan Nanoparticles Inhibit Chondrocyte Apoptosis to Attenuate Osteoarthritis via ... Rat ELOVL1(Elongation Of Very Long Chain Fatty Acids Like Protein 1) ELISA Kit ...
... the ornithine carrier is composed of 300 amino acids that constitute 3 repeated motifs of approximately 100 amino acids each. ... The specifics of the liver transporter have recently been identified.. Cationic L-ornithine is electroneutrally transported ... Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. It is then cleaved ... The transporter was identified by probing a mammalian-expressed sequence tag database with 2 fungal mitochondrial ornithine ...
During her M.S., she focused on the development of fluorescent amino acids and peptide synthesis. Currently, Sarah is a PhD ... Remaining within the context of this specific paper, we are going to work on supramolecular transporters/vectors able to ... We planned thus to improve the liposomes performance by decorating their outer surface with our cationic calixarene-based ... They distinguish two proton-transfer steps and find that a hydrated Mg2+ ion acts as a general acid to protonate the leaving ...
... the ornithine carrier is composed of 300 amino acids that constitute 3 repeated motifs of approximately 100 amino acids each. ... The specifics of the liver transporter have recently been identified. Cationic L-ornithine is electroneutrally transported into ... Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. It is then cleaved ... The transporter was identified by probing a mammalian-expressed sequence tag database with 2 fungal mitochondrial ornithine ...
Mouse CAT1(Cationic Amino Acid Transporter 1) ELISA Kit. *Mouse CCR6(Chemokine C-C-Motif Receptor 6) ELISA Kit ... Mouse EAAT1(Excitatory Amino Acid Transporter 1) ELISA Kit. *Mouse EIF2aK3(Eukaryotic Translation Initiation Factor 2 Alpha ... Human ABCC10(ATP Binding Cassette Transporter C10) ELISA Kit. *Human AMIGO1(Adhesion Molecule With Ig Like Domain Protein 1) ... Mouse LIPA(Lipase A, Lysosomal Acid) ELISA Kit. *Mouse LTBP1(Latent Transforming Growth Factor Beta Binding Protein 1) ELISA ...
cationic amino acid transporter 6. ARABIDOPSIS THALIANA CATIONIC. AMINO ACID TRANSPORTER 6, cationic. amino acid transporter 6 ... Transmembrane amino acid transporter family protein. 0.66. 0.31. -0.32. 32. AT3G45960. expansin-like A3. expansin-like A3, ... sulfate transporter 3;2. sulfate transporter 3;2. -0.63. 0.32. -0.33. 43. AT3G56630. cytochrome P450, family 94, subfamily D, ... Sodium Bile acid symporter family. -0.61. 0.3. -0.3. 60. AT3G14100. RNA-binding (RRM/RBD/RNP motifs) family protein. -0.61. 0.3 ...
Substitutions of amino acids Ser645 and Phe641 cause 75% resistance in C. albicans. [10, 13]. Pharmacodynamic studies conducted ... ABC proteins are primary transporters that use ATP hydrolysis. MFS pumps are secondary transporters that use the motive force ... Production of cationic antimicrobial peptide lactoferricin. [73]. Human b-defensins (HBD). Cell membrane. Increases membrane ... Resistance-associated amino acid substitutions occur in two highly conserved hot-spot (HS) regions of the FKS genes. The ...
... cationic amino acid transporter/glycoprotein-associated cationic amino acid transporters (SLC7A1, SLC7A2, SLC7A3, SLC7A4) ... ... Common food acids include vinegar, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. Acidity ... The fruit contains citric acid, tartaric acid, malic acid and ascorbic acid, hydroxycitric acid, and flavonoids. Ripe asam ... amino acids, ω-3 fatty acids, ω-6 fatty acids, medium-chain triglycerides, dietary fiber, short and long chain fatty acids ...
2D IR spectroscopy studies of amyloid beta aggregation - using computational modeling to optimize unnatural amino acids that ... "GABA Transporter Assay Development". David Weaver. Carol He. "Comparing Different Machine Learning Methods for. Predicting NMR ... "Activation of C-H and C-O Bonds by Cationic Bis(Phosphine) Iridium Complexes". Nathan Schley. ... "Potential Implications of Dopamine Transporter Nanoclustering". Sandra Rosenthal. Alex Stoneman. Study of t-cells in immune ...
Repetitive Sequences, Amino Acid. *Peptides. *Amyloid beta-Peptides. *Antimicrobial Cationic Peptides. *Aptamers, Peptide ... The Dopamine Transporter Recycles via a Retromer-Dependent Postendocytic Mechanism: Tracking Studies Using a Novel Fluorophore- ... Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular ...
Our findings suggest that plasma glycogenic amino acids are sensitive indicators of brain glycogen levels with endurance ... Brain glycogen levels correlated negatively with plasma glycogenic amino acids (serine, proline, threonine, glutamate, ... and tyrosine share the same transporter, L-type amino acid transporter 1 (LAT1), on the blood-brain barrier (BBB) (Pardridge ... Cationic metabolites were analyzed using a fused-silica capillary (50 mm i.d., 680 cm total length) with cation buffer solution ...
Summary: membrane-permeable cationic dye used as substrate for the efflux pump P-glycoprotein ... Amino Acids & Building Blocks. *Natural Products. *Others. *SERVICES. *Analytical Services. *Custom Organic Synthesis ...
  • The hOAT3 cDNA consisted of 2179 base pairs that encoded a 543-amino-acid residue protein with 12 putative transmembrane domains. (aspetjournals.org)
  • Currently, Sarah is a PhD candidate in the Busschaert group at Tulane University, working on various medical and non-medical applications of synthetic transmembrane anion transporters. (rsc.org)
  • She then moved to the University to Southampton (UK) in 2010 to undertake a PhD under the supervision of Professor Philip A. Gale, working on the development of synthetic transmembrane anion transporters. (rsc.org)
  • The SLC7A7 gene provides instructions for producing a protein called y+L amino acid transporter 1 (y+LAT-1), which is involved in transporting certain protein building blocks (amino acids), namely lysine, arginine, and ornithine. (medlineplus.gov)
  • Variants in the y+LAT-1 protein disrupt the transportation of amino acids, reducing the amount of lysine, arginine, and ornithine in the body and increasing the amount of these amino acids in urine. (medlineplus.gov)
  • An inner mitochondrial membrane transporter directs ornithine to the transcarbamoylase enzyme to keep intramatrix ornithine levels low. (medscape.com)
  • Cationic L-ornithine is electroneutrally transported into the matrix in exchange for a proton and citrulline. (medscape.com)
  • As with other mitochondrial carrier family proteins, the ornithine carrier is composed of 300 amino acids that constitute 3 repeated motifs of approximately 100 amino acids each. (medscape.com)
  • The transporter was identified by probing a mammalian-expressed sequence tag database with 2 fungal mitochondrial ornithine carrier protein sequences. (medscape.com)
  • Ornithine incorporation was restored in fibroblasts derived from patients with hyperornithinemia-hyperammonemia-homocitrullinuria syndrome by transforming the fibroblasts with transporter complementary DNA (cDNA). (medscape.com)
  • In hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, the mitochondrial ornithine transporter ORNT1 is defective. (medscape.com)
  • In hyperornithinemia-hyperammonemia-homocitrullinemia syndrome, the mitochondrial ornithine transporter ORNT1 is defective. (medscape.com)
  • The y+LAT-1 protein forms one part (the light subunit) of a complex called the heterodimeric cationic amino acid transporter. (medlineplus.gov)
  • This variant disrupts the way the gene's instructions are used to make the y+LAT-1 protein, causing the protein to be misplaced in the cell. (medlineplus.gov)
  • The abnormal transportation and reduced amount of these amino acids in various tissues of the body leads to the signs and symptoms of lysinuric protein intolerance. (medlineplus.gov)
  • Most antimicrobial peptides are cationic amphiphilic compounds that function by binding to the negatively charged lipids of bacterial membranes, followed by membrane disruption. (rsc.org)
  • A cDNA encoding a multispecific organic anion transporter 3 (hOAT3) was isolated from a human kidney cDNA library. (aspetjournals.org)
  • first, organic anions are transported from the peritubular plasma by basolateral organic anion transporter(s) and subsequently effluxed into the tubular lumen by luminal transporter(s). (aspetjournals.org)
  • A particle according to claim 1, further comprising the nucleic acid sequence encoding die protease cleavage signal. (sumobrain.com)
  • 1] "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum. (tcdb.org)
  • The deduced amino acid sequence of hOAT3 showed 36 to 51% identity to those of other members of the OAT family. (aspetjournals.org)
  • ATB 0+ (SLC6A14) is a transporter for numerous dipolar and cationic amino acids and thus has a much broader substrate specificity than the glycine transporters alongside which it is grouped on the basis of structural similarity [ 10 ]. (guidetopharmacology.org)
  • The transportation of amino acids from the small intestine and kidneys to the rest of the body is necessary for the body to be able to make and use proteins. (medlineplus.gov)
  • Membrane transport proteins that actively co-transport ASCORBIC ACID and sodium ions across the CELL MEMBRANE. (lookformedical.com)
  • Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments. (umassmed.edu)
  • A well-established mechanism for MDSC suppressive activity is the metabolism of L-Arginine (L-Arg) by Arginase 1 (ARG1) and nitric oxide synthase 2 (NOS2). (purdue.edu)
  • Arginine or l-arginine, abbreviated Arg or R, is an essential amino acid that is physiologically active in the L-form. (cannabisdatabase.ca)
  • In mammals, arginine is formally classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. (cannabisdatabase.ca)
  • Arginine is a basic amino acid as its side chain contains a positively charged guanidinium group, which is highly polar, at the end of a hydrophobic¬†aliphatic¬†hydrocarbon chain. (cannabisdatabase.ca)
  • L-Arginine is an amino acid that has numerous functions in the body. (cannabisdatabase.ca)
  • 1,2 Lipopolysaccharide, a gram-negative bacterial outer membrane component, has been implicated as a critical factor contributing to the pathogenesis of sepsis. (asahq.org)
  • Two gene products, GlyT1 and GlyT2, are known that give rise to transporters that are predominantly located on glia and neurones, respectively. (guidetopharmacology.org)
  • Belongs to the class of organic compounds known as l-alpha-amino acids. (cannabisdatabase.ca)
  • Note that organic derivatives of phosphonic acids are listed under are ORGANOPHOSPHONATES. (lookformedical.com)
  • An acquired blood vessel disorder caused by severe deficiency of vitamin C (ASCORBIC ACID) in the diet leading to defective collagen formation in small blood vessels. (lookformedical.com)
  • Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. (medscape.com)
  • With the help of a combined mix of typical chromatographic methods, one sesquiterpenoid viglutin (1), one alkaloid viglutoside (2), one -pyranone viglutanone (3), along with two salts sodium phaseate (4) and sodium p-coumarate (5), had been characterized and their buildings were made of the nuclear magnetic resonance (NMR) spectral elucidation and mass (MS) spectrometric evaluation. (engineering-gdfsuez.com)
  • Dietary absorption of VITAMIN C is highly dependent upon this class of transporters and a subset of SODIUM GLUCOSE TRANSPORTERS which transport the oxidized form of vitamin C, DEHYDROASCORBIC ACID. (lookformedical.com)
  • The infrared (IR) absorption rings at 3416 and 1647 cm?1 were in contract using the presences of hydroxy and carbonCcarbon increase connection functionalities, respectively. (engineering-gdfsuez.com)
  • The life of hydroxyl and carbonCcarbon dual bond functionalities could possibly be determined in the IR absorption rings at 3430 and 1637 cm?1. (engineering-gdfsuez.com)
  • A particle according to claim 1 or 2, wherein the heterologous polypeptide has specific binding affinity for a cognate receptor on die surface of an eukaryotic cell, binding to which does not allow infection of the cell by the viral particle. (sumobrain.com)
  • A particle according to claim 1 or 2, wherein the heterologous polypeptide has no specific binding affinity for a eukaryotic cell surface component. (sumobrain.com)
  • All of these variants impair the y+LAT-1 protein's ability to transport amino acids. (medlineplus.gov)
  • The transport properties of rOAT1 are nearly identical to those of the classic PAH transporter. (aspetjournals.org)
  • Our findings suggest that plasma glycogenic amino acids are sensitive indicators of brain glycogen levels in endurance exercise. (frontiersin.org)
  • It is the lactone of 2,3-DIKETOGULONIC ACID and has antiscorbutic activity in man on oral ingestion. (lookformedical.com)
  • By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS. (lookformedical.com)
  • It exhibits antioxidant activity by virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus. (lookformedical.com)
  • The purpose of this study was to confirm whether cationic N,N-dimethyl amino acid esters of Cur could act as prodrugs and improve its water solubility and oral bioavailability. (researchgate.net)
  • Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. (lookformedical.com)
  • The relationship spectroscopy (COSY) indicated the linkage of H-2/H-3/H-4/H-5/H-13 and H-7/H-8/H-9/H-10 (Amount 1). (engineering-gdfsuez.com)
  • Antiretroviral therapy should be prescribed by a health care provider experienced in the management of HIV-1 infection. (who.int)
  • 1 Food spoilage remains a worldwide issue, despite the food science and technological advancement that has been made in recent years. (microbiologyjournal.org)
  • Ascorbic acid deficiency frequently develops into SCURVY in young children fed unsupplemented cow's milk exclusively during their first year. (lookformedical.com)
  • A particle according to any one of claims 1 to 9, wherein the protease cleavage site becomes accessible to die relevant protease only after the viral particle has become bound to an eukaryotic cell. (sumobrain.com)
  • These are alpha amino acids which have the L-configuration of the alpha-carbon atom. (cannabisdatabase.ca)