Amino Acid Transport System ASC: A ubiquitous sodium-dependent neutral amino acid transporter. The preferred substrates for this transporter system include ALANINE; SERINE; and CYSTEINE.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Amino Acid Transport System L: 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.Amino Acids: 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.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).Aminoisobutyric Acids: A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.Biological Transport: 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.Amino Acid Transport System A: 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.Amino Acid Transport Systems, Neutral: Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Amino Acid Transport System y+Harmaline: A beta-carboline alkaloid isolated from seeds of PEGANUM.Alanine: 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.beta-Alanine: 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.Sodium: A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.Antigens, CD98: 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.Amino Acids, Neutral: Amino acids with uncharged R groups or side chains.Amino Acids, Cyclic: A class of amino acids characterized by a closed ring structure.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Kinetics: The rate dynamics in chemical or physical systems.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Amino Acid Transport System y+LMembrane Transport Proteins: 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.4-Chloromercuribenzenesulfonate: A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.Glutamine: 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.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Cystine: 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.Isoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Fatty Acid Transport Proteins: A broad category of membrane transport proteins that specifically transport FREE FATTY ACIDS across cellular membranes. They play an important role in LIPID METABOLISM in CELLS that utilize free fatty acids as an energy source.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Amino Acid Sequence: 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.Arginine: An essential amino acid that is physiologically active in the L-form.Lysine: An essential amino acid. It is often added to animal feed.Leucine-tRNA Ligase: An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.Cloning, Molecular: 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.Mutation: 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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Amino Acid Transport Systems, Acidic: Amino acid transporter systems capable of transporting acidic amino acids (AMINO ACIDS, ACIDIC).Molecular Sequence Data: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Hydrogen-Ion Concentration: 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)Tryptophan: An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Glutamates: Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.Xenopus laevis: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Oocytes: 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).Histidine: An essential amino acid that is required for the production of HISTAMINE.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Taurocholic Acid: The product of conjugation of cholic acid with taurine. Its sodium salt is the chief ingredient of the bile of carnivorous animals. It acts as a detergent to solubilize fats for absorption and is itself absorbed. It is used as a cholagogue and cholerectic.Dicarboxylic AcidsRats, Inbred Strains: Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.RNA, Messenger: 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.Bacterial Proteins: Proteins found in any species of bacterium.Ethylmaleimide: A sulfhydryl reagent that is widely used in experimental biochemical studies.Large Neutral Amino Acid-Transporter 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.Cells, Cultured: 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.

The RD114/simian type D retrovirus receptor is a neutral amino acid transporter. (1/71)

The RD114/simian type D retroviruses, which include the feline endogenous retrovirus RD114, all strains of simian immunosuppressive type D retroviruses, the avian reticuloendotheliosis group including spleen necrosis virus, and baboon endogenous virus, use a common cell-surface receptor for cell entry. We have used a retroviral cDNA library approach, involving transfer and expression of cDNAs from highly infectable HeLa cells to nonpermissive NIH 3T3 mouse cells, to clone and identify this receptor. The cloned cDNA, denoted RDR, is an allele of the previously cloned neutral amino acid transporter ATB0 (SLC1A5). Both RDR and ATB0 serve as retrovirus receptors and both show specific transport of neutral amino acids. We have localized the receptor by radiation hybrid mapping to a region of about 500-kb pairs on the long arm of human chromosome 19 at q13.3. Infection of cells with RD114/type D retroviruses results in impaired amino acid transport, suggesting a mechanism for virus toxicity and immunosuppression. The identification and functional characterization of this retrovirus receptor provide insight into the retrovirus life cycle and pathogenesis and will be an important tool for optimization of gene therapy using vectors derived from RD114/type D retroviruses.  (+info)

A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses. (2/71)

The type D simian retroviruses cause immunosuppression in macaques and have been reported as a presumptive opportunistic infection in a patient with AIDS. Previous evidence based on viral interference has strongly suggested that the type D simian viruses share a common but unknown cell surface receptor with three type C viruses: feline endogenous virus (RD114), baboon endogenous virus, and avian reticuloendotheliosis virus. Furthermore, the receptor gene for these viruses has been mapped to human chromosome 19q13.1-13.2. We now report the isolation and characterization of a cell surface receptor for this group of retroviruses by using a human T-lymphocyte cDNA library in a retroviral vector. Swiss mouse fibroblasts (NIH 3T3), which are naturally resistant to RD114, were transduced with the retroviral library and then challenged with an RD114-pseudotyped virus containing a dominant selectable gene for puromycin resistance. Puromycin selection yielded 12 cellular clones that were highly susceptible to a beta-galactosidase-encoding lacZ(RD114) pseudotype virus. Using PCR primers specific for vector sequences, we amplified a common 2.9-kb product from 10 positive clones. Expression of the 2.9-kb cDNA in Chinese hamster ovary cells conferred susceptibility to RD114, baboon endogenous virus, and the type D simian retroviruses. The 2.9-kb cDNA predicted a protein of 541 amino acids that had 98% identity with the previously cloned human Na+-dependent neutral-amino-acid transporter Bo. Accordingly, expression of the RD114 receptor in NIH 3T3 cells resulted in enhanced cellular uptake of L-[3H]alanine and L-[3H]glutamine. RNA blot (Northern) analysis suggested that the RD114 receptor is widely expressed in human tissues and cell lines, including hematopoietic cells. The human Bo transporter gene has been previously mapped to 19q13.3, which is closely linked to the gene locus of the RD114 receptor.  (+info)

Na+ - and Cl- -coupled active transport of nitric oxide synthase inhibitors via amino acid transport system B(0,+). (3/71)

Nitric oxide synthase (NOS) inhibitors have therapeutic potential in the management of numerous conditions in which NO overproduction plays a critical role. Identification of transport systems in the intestine that can mediate the uptake of NOS inhibitors is important to assess the oral bioavailability and therapeutic efficacy of these potential drugs. Here, we have cloned the Na+ - and Cl- -coupled amino acid transport system B(0,+) (ATB(0,+)) from the mouse colon and investigated its ability to transport NOS inhibitors. When expressed in mammalian cells, ATB(0,+) can transport a variety of zwitterionic and cationic amino acids in a Na+ - and Cl- -coupled manner. Each of the NOS inhibitors tested compete with glycine for uptake through this transport system. Furthermore, using a tritiated analog of the NOS inhibitor N(G)-nitro-L-arginine, we showed that Na+ - and Cl- -coupled transport occurs via ATB(0,+). We then studied transport of a wide variety of NOS inhibitors in Xenopus laevis oocytes expressing the cloned ATB(0,+) and found that ATB(0,+) can transport a broad range of zwitterionic or cationic NOS inhibitors. These data represent the first identification of an ion gradient-driven transport system for NOS inhibitors in the intestinal tract.  (+info)

Na+- and Cl--coupled active transport of carnitine by the amino acid transporter ATB(0,+) from mouse colon expressed in HRPE cells and Xenopus oocytes. (4/71)

1. ATB(0,+) is an amino acid transporter energized by transmembrane gradients of Na+ and Cl(-) and membrane potential. We cloned this transporter from mouse colon and expressed the clone functionally in mammalian (human retinal pigment epithelial, HRPE) cells and Xenopus laevis oocytes to investigate the interaction of carnitine and its acyl esters with the transporter. 2. When expressed in mammalian cells, the cloned ATB(0,+) was able to transport carnitine, propionylcarnitine and acetylcarnitine. The transport process was Na(+) and Cl(-) dependent and inhibitable by the amino acid substrates of the transporter. The Michaelis constant for carnitine was 0.83 +/- 0.08 mM and the Hill coefficient for Na(+) activation was 1.6 +/- 0.1. 3. When expressed in Xenopus laevis oocytes, the cloned ATB(0,+) was able to induce inward currents in the presence of carnitine and propionylcarnitine under voltage-clamped conditions. There was no detectable current in the presence of acetylcarnitine. Carnitine-induced currents were obligatorily dependent on the presence of Na(+) and Cl(-). The currents were saturable with carnitine and the Michaelis constant was 1.8 +/- 0.4 mM. The analysis of Na(+)- and Cl(-)-activation kinetics revealed that 2 Na(+) and 1 Cl(-) were involved in the transport of carnitine via the transporter. 4. These studies describe the identification of a novel function for the amino acid transporter ATB(0,+). Since this transporter is expressed in the intestinal tract, lung and mammary gland, it is likely to play a significant role in the handling of carnitine in these tissues. 5. A Na(+)-dependent transport system for carnitine has already been described. This transporter, known as OCTN2 (novel organic cation transporter 2), is expressed in most tissues and transports carnitine with high affinity. It is energized, however, only by a Na(+) gradient and membrane potential. In contrast, ATB(0,+) is a low-affinity transporter for carnitine, but exhibits much higher concentrative capacity than OCTN2 because of its energization by transmembrane gradients of Na(+) and Cl(-) as well as by membrane potential.  (+info)

Na(+)-dependent neutral amino acid transporter ATB(0) is a rabbit epithelial cell brush-border protein. (5/71)

System B(0) activity accounts for the majority of intestinal and kidney luminal neutral amino acid absorption. An amino acid transport system, called ATB(0) (also known as ASCT2), with functional characteristics similar to those of system B(0), has been recently cloned. We generated polyclonal antibodies to human and rabbit ATB(0) COOH-terminal peptides and used Western blot analysis to detect ATB(0) protein in rabbit tissues, rabbit ileal brush-border membrane vesicles (BBMV), and HeLa cells transfected with plasmids containing ATB(0) cDNAs. Immunohistochemistry was used to localize ATB(0) in rabbit kidney and intestine. In Western blots of rabbit tissues, ATB(0) was a broad smear of 78- to 85-kDa proteins. In transfected HeLa cells, ATB(0) appeared as a smear consisting of 57- to 65-kDa proteins. The highest expression was found in the kidney. ATB(0) was enriched in rabbit ileal BBMV and in HeLa cells transfected with ATB(0) cDNAs. In the kidney and in the intestine, ATB(0) was confined to the brush-border membrane (BBM) of the proximal tubular cell and of the enterocyte, respectively. Tissue and intracellular distribution of ATB(0) protein parallels that of system B(0) activity. ATB(0) protein could be the transporter responsible for system B(0) in the BBM of epithelial cells.  (+info)

Sustained multilineage gene persistence and expression in dogs transplanted with CD34(+) marrow cells transduced by RD114-pseudotype oncoretrovirus vectors. (6/71)

Previous studies have shown that the choice of envelope protein (pseudotype) can have a significant effect on the efficiency of retroviral gene transfer into hematopoietic stem cells. This study used a competitive repopulation assay in the dog model to evaluate oncoretroviral vectors carrying the envelope protein of the endogenous feline virus, RD114. CD34-enriched marrow cells were divided into equal aliquots and transduced with vectors produced by the RD114-pseudotype packaging cells FLYRD (LgGLSN and LNX) or by the gibbon ape leukemia virus (GALV)-pseudotype packaging cells PG13 (LNY). A total of 5 dogs were studied. One dog died because of infection before sustained engraftment could be achieved, and monitoring was discontinued after 9 months in another animal that had very low overall gene-marking levels. The 3 remaining animals are alive with follow-ups at 11, 22, and 23 months. Analyses of gene marking frequencies in peripheral blood and marrow by polymerase chain reaction revealed no significant differences between the RD114 and GALV-pseudotype vectors. The LgGLSN vector also contained the enhanced green fluorescent protein (GFP), enabling us to monitor proviral expression by flow cytometry. Up to 10% of peripheral blood cells expressed GFP shortly after transplantation and approximately 6% after the longest follow-up of 23 months. Flow cytometric analysis of hematopoietic subpopulations showed that most of the GFP-expressing cells were granulocytes, although GFP-positive lymphocytes and monocytes were also detected. In summary, these results show that RD114-pseudotype oncoretroviral vectors are able to transduce hematopoietic long-term repopulating cells and, thus, may be useful for human stem cell gene therapy.  (+info)

ATB(0)/SLC1A5 gene. Fine localisation and exclusion of association with the intestinal phenotype of cystic fibrosis. (7/71)

The Na+-dependent amino acid transporter named ATB(0) was previously found to be located in 19q13.3 by fluorescence in situ hybridisation. Genetic heterogeneity in the 19q13.2-13.4 region, syntenic to the Cystic Fibrosis Modulator Locus 1 (CFM1) in mouse, seemed to be associated to the intestinal phenotypic variation of cystic fibrosis (CF). We performed fine chromosomal mapping of ATB(0) on radiation hybrid (RH) panels G3 and TNG. Based on the most accurate location results from TNG-RH panel, mapping analysis evidenced that ATB(0) is localised between STS SHGC-13875 (D19S995) and STS SHGC-6138 in 19q13.3, that corresponds with the immediately telomeric/distal segment of the strongest linkage region within the human CFM1 (hCFM1) syntenic region. Regarding to the genomic structure and exon organisation, our results show that the ATB(0) gene is organised into eight exons. The knowledge of the genomic structure allowed us to perform an exhaustive mutational analysis of the gene. Evaluation of the possible implication of ATB(0) in the intestinal phenotype of CF was performed on the basis of the functional characteristics of the encoded protein, its apparent relevance to meconium ileus (MI) and position in relation to the hCFM1 syntenic region. We have analysed this gene in samples from CF patients with and without MI. Several sequence variations in the ATB(0) gene were identified, although none of them seemed to be related to the intestinal phenotype of CF. Even though no particular allele or haplotype in ATB(0) appears to be associated to CF-MI disease, new SNPs identified should be useful in segregation and linkage disequilibrium analyses in families affected by other disorders caused by the impairment of neutral amino acid transport.  (+info)

Characterisation and cloning of a Na(+)-dependent broad-specificity neutral amino acid transporter from NBL-1 cells: a novel member of the ASC/B(0) transporter family. (8/71)

Na(+)-dependent neutral amino acid transport into the bovine renal epithelial cell line NBL-1 is catalysed by a broad-specificity transporter originally termed System B(0). This transporter is shown to differ in specificity from the B(0) transporter cloned from JAR cells [J. Biol. Chem. 271 (1996) 18657] in that it interacts much more strongly with phenylalanine. Using probes designed to conserved transmembrane regions of the ASC/B(0) transporter family we have isolated a cDNA encoding the NBL-1 cell System B(0) transporter. When expressed in Xenopus oocytes the clone catalysed Na(+)-dependent alanine uptake which was inhibited by glutamine, leucine and phenylalanine. However, the clone did not catalyse Na(+)-dependent phenylalanine transport, again as in NBL-1 cells. The clone encoded a protein of 539 amino acids; the predicted transmembrane domains were almost identical in sequence to those of the other members of the B(0)/ASC transporter family. Comparison of the sequences of NBL-1 and JAR cell transporters showed some differences near the N-terminus, C-terminus and in the loop between helices 3 and 4. The NBL-1 B(0) transporter is not the same as the renal brush border membrane transporter since it does not transport phenylalanine. Differences in specificity in this protein family arise from relatively small differences in amino acid sequence.  (+info)

*List of MeSH codes (D12.776.157)

... amino acid transport system a MeSH D12.776.157.530.200.500.200 -- amino acid transport system asc MeSH D12.776.157.530.200.500. ... amino acid transport systems, acidic MeSH D12.776.157.530.200.249.500 -- amino acid transport system x-ag MeSH D12.776.157.530. ... amino acid transport systems, basic MeSH D12.776.157.530.200.374.600 -- amino acid transport system y+ MeSH D12.776.157.530. ... cationic amino acid transporter 2 MeSH D12.776.157.530.200.374.750 -- amino acid transport system y+l MeSH D12.776.157.530. ...

*Transporter Classification Database

Family 3.B.1 The Na+-transporting Carboxylic Acid Decarboxylase (NaT-DC) Family 3.C.1 The Na+ Transporting ... L-Asc) Family 4.B.1 The Nicotinamide Ribonucleoside (NR) Uptake Permease (PnuC) Family 4.C.1 The Proposed Fatty Acid ... Family 2.A.78 The Branched Chain Amino Acid Exporter (LIV-E) Family 2.A.79 The Threonine/Serine Exporter (ThrE) Family 2.A.80 ... approved classification system for membrane transport proteins, including ion channels. The upper level of classification and a ...
The Alanine-Serine-Cysteine transporter ASCT2 (SLC1A5) is a membrane protein that transports neutral amino acids into cells in exchange for outward movement of intracellular amino acids. ASCT2 is highly expressed in peripheral tissues such as the lung and intestines where it contributes to the homeostasis of intracellular concentrations of neutral amino acids. ASCT2 also plays an important role in the development of a variety of cancers such as melanoma by transporting amino acid nutrients such as glutamine into the proliferating tumors. Therefore, ASCT2 is a key drug target with potentially great pharmacological importance. Here, we identify seven ASCT2 ligands by computational modeling and experimental testing. In particular, we construct homology models based on crystallographic structures of the aspartate transporter Glt(Ph) in two different conformations. Optimization of the models binding sites for protein-ligand complementarity reveals new putative pockets that can be targeted via structure
The NMDA receptor co-agonist D-serine is a substrate for the neutral amino acid transporters ASCT1 and ASCT2 which may regulate its extracellular levels in the CNS. We tested inhibitors of ASCT1 and ASCT2 for their effects in rodent models of schizophrenia and visual dysfunction which had previously been shown to be responsive to D-serine. L-4-fluorophenylglycine (L-4FPG), L-4-hydroxyPG (L-4OHPG) and L-4-chloroPG (L-4ClPG) all showed high plasma bioavailability when administered systemically to rats and mice. L-4FPG showed good brain penetration with brain:plasma ratios of 0.7-1.4, however values for L-4OHPG and L-4ClPG were lower. Systemically administered L-4FPG potently reduced amphetamine-induced hyperlocomotion in mice, whereas L-4OHPG was 100-fold less effective and L-4ClPG inactive at the doses tested. L-4FPG and L-4OHPG did not impair visual acuity in naive rats, and acute systemic administration of L-4FPG significantly improved the deficit in contrast sensitivity in blue-light treated ...
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NAC exerts survival-promoting effects in several cellular systems (Mayer and Noble 1994). Cysteine is transported mainly by the alanine-serine-cysteine (ASC) system, a ubiquitous system of Na+-dependent neutral amino acid transport in a variety of cells (Bannai and Tateishi 1986; Ishige et al. 2005). NAC, however, is a membrane-permeable cysteine precursor that does not require active transport and delivers cysteine to the cell in a unique way (Fig. 1) (Sen 1997). After free NAC enters a cell, it is rapidly hydrolyzed to release cysteine, a precursor of GSH. GSH is synthesized by the coactions of c-glutamylcysteine synthetase and GSH synthetase. The synthesis of GSH is limited by the availability of substrates; cysteine is usually the limiting precursor (Meister 1995). C-glutamylcysteine synthetase is inhibited by feedback from GSH (Richman and Meister 1975). In addition, intracellular GSH is maintained in its thiol form by GSH reductase, which requires NADPH (Sen 1997). GSH participates ...
As discussed earlier, cells can acquire serine by either synthesizing it internally or importing serine from the environment. Serine is a small, neutral amino acid and, as such, can be transported by one of three systems. Two of the systems are sodium dependent: the alanine/serine/cysteine/threonine transporters ASCT1 and ASCT2 (encoded by SLC1A4 and SLC1A5, respectively) and the system A transporters SAT1 and SAT2 (encoded by SLC38A1 and SLC38A2, respectively). The third is a family of neutral amino acid antiporters, the alanine/serine/cysteine transporter (ASC) system (El-Hattab, 2016). These antiporters are of particular interest because they are active even at steady state, so that for instance, one molecule of intracellular serine can be exchanged for one molecule of extracellular serine. Normally this process goes unnoticed, but a recent study (DeNicola et al., 2015) points out that it can complicate interpretation of heavy isotope-labeling experiments by setting up an exchange flux ...
Supply of amino acids to the body provides repair treatment means nourish human skin, nails and hair result in delay aging process naturally. Supply of amino acids strengthens connective tissue to keep our skin smooth, shine, glowing and elastic. Creatine play very important role to keep skin healthy and this creatine is made up of amino acids like Arginine and Methionine. Glutamine amino acid is responsible to regulate acid-base balance as a result it supports healthy skin. Carnitine is a di-peptide containing two essential amino acids lysine and Methionine. Carnitine helps in burning fat to produce energy so also known as fat burner so also added in fitness and wellness program ...
Dr. Mandanas responded: Glutamine amino acid. Glutamine is an Amino Acid (basic building block of proteins). People take it for various reasons as a dietary supplement. It purportedly helps maintain |a href="/topics/muscle-mass" track_data="{
Giacopo, Andrea Di; Rubio-Aliaga, Isabel; Cantone, Alessandra; Artunc, Ferruh; Rexhepaj, Rexhep; Frey-Wagner, Isabelle; Font-Llitjós, Mariona; Gehring, Nicole; Stange, Gerti; Jaenecke, Isabel; Mohebbi, Nilufar; Closs, Ellen I; Palacín, Manuel; Nunes, Virginia; Daniel, Hannelore; Lang, Florian; Capasso, Giovambattista; Wagner, Carsten A (2013). Differential cystine and dibasic amino acid handling after loss of function of the amino acid transporter b0,+AT (Slc7a9) in mice. American Journal of Physiology. Renal, Fluid and Electrolyte Physiology, 305(12):F1645-F1655.. Mariotta, Luca; Ramadan, Tamara; Singer, Dustin; Guetg, Adriano; Herzog, Brigitte; Stoeger, Claudia; Palacín, Manuel; Lahoutte, Tony; Camargo, Simone M R; Verrey, François (2012). T-type amino acid transporter TAT1 (Slc16a10) is essential for extracellular aromatic amino acid homeostasis control. Journal of Physiology, 590(Pt 24):6413-6424.. ...
RESULTS: In a genomic survey where we manually annotated and analyzing sequences from more than 300 SLC1 genes (from more than 40 vertebrate species), we found evidence for an interesting evolutionary history of this gene family. While human and mouse genomes contain 7 SLC1 genes, in prototheria, sauropsida, and amphibia genomes up to 9 and in actinopterygii up to 13 SLC1 genes are present. While some of the additional slc1 genes in ray-finned fishes originated from R3, the increased number of SLC1 genes in prototheria, sauropsida, and amphibia genomes originates from specific genes retained in these lineages.Phylogenetic comparison and microsynteny analyses of the SLC1 genes indicate, that theria genomes evidently lost several SLC1 genes still present in the other lineage. The genes lost in theria group into two new subfamilies of the slc1 gene family which we named slc1a8/eaat6 and slc1a9/eaat7 ...
Rasko JE, Battini JL, Gottschalk RJ, Mazo I, Miller AD. The RD114/simian type D retrovirus receptor is a neutral amino acidtransporter.Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2129-34. PMID: 10051606 [PubMed - indexed for MEDLINE]. The RD114/simian type D retroviruses, which include the feline endogenous retrovirus RD114, all strains of simian immunosuppressive type D retroviruses, the avian reticuloendotheliosis group including spleen necrosis virus, and baboon endogenous virus, use a common cell-surface receptor for cell entry. We have used a retroviral cDNA library approach, involving transfer and expression of cDNAs from highly infectable HeLa cells to nonpermissive NIH 3T3 mouse cells, to clone and identify this receptor. The cloned cDNA, denoted RDR, is an allele of the previously cloned neutral amino acid transporter ATB0 (SLC1A5). Both RDR and ATB0 serve as retrovirus receptors and both show specific transport of neutral amino acids. We have localized the receptor by radiation hybrid ...
Plasma membrane System A-like neutral amino acid transporter, SA1, SAT2 or SNAT2 (transports small, neutral aliphatic amino acids including α-(methylamino)isobutyrate, mAIB with Na+ (1:1 stoichiometry; Km = 200-500 μM)). Asparagine 82 controls the interaction of Na+ with the transporter (Zhang and Grewer, 2007). The C-terminal domain regulates transport activity through a voltage-dependent process (Zhang et al., 2011). An 11 TMS topology has been experimentally demonstrated (Ge et al. 2018 ...
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The Hartnup disorder page provides a brief description of the genetics and clinical features of this disease that results from defects in the neutral amino acid transporter encoded by the SLC16A19 gene.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Reverse transcription-PCR was performed based on the method of Sugawara et al., 59 with slight modifications, using 1 μg of total RNA isolated from human cornea (kindly provided by Alcon Laboratories, Fort Worth, TX). The forward and reverse primers were 5′-TCT CAC TGC TTA ACG GCG TGT G-3′, and 5′-TCC CTG GCC AAG TCT AAC AAT G-3′, respectively. These primers correspond to the nucleotide positions 110-132 and 606-628 in hLAT1 cDNA, respectively. RT-PCR was performed with a commercial kit (GeneAmp; Applied Biosystems, Foster City, CA). The conditions for reverse transcription were as follows: denaturation of the template RNA for 10 minutes at 70°C and reverse transcription for 60 minutes at 42°C. The conditions for PCR amplification were as follows: denaturation for 1 minute at 94°C; annealing for 1 minute at 58°C, and extension for 1 minute at 72°C, 37 cycles; final extension for 10 minutes at 72°C. The resultant product (∼520 bp) was subcloned in pGEM-T vector and sequenced from ...
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OBJECTIVES: To examine whether syncytin-1 has immune regulatory functions and is carried by human placental exosomes. Further, to examine whether corticotropin-releasing hormone (CRH) can induce the production of syncytin-1. STUDY DESIGN: Human placental exosomes were isolated from placental explant, primary trophoblast and BeWo cell cultures. The presence of exosomes was confirmed by transmission electron microscopy and western blotting. Exosomal protein was probed with 3 separate antibodies targeting syncytin-1. Syncytin-1 immunosuppression was tested, using either a syncytin-1 recombinant ectodomain protein or a synthetic peptide with the human syncytin-1 immunosuppressive domain sequence, in an in vitro human blood culture system immune challenged with LPS or PHA. The inhibition of cytokine production by syncytin-1 was determined by ELISA of TNF-α, IFN-γ and CXCL10. BeWo cells were stimulated with CRH or vehicle for 24 h. mRNA and Protein was extracted from the cells for real-time PCR and ...
Sodium-dependent neutral amino acid transporter-2 (SNAT2), the ubiquitous member of SLC38 family, accounts for the activity of transport system A for neutral amino acids in most mammalian tissues. As the transport process performed by SNAT2 is highly
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The neutral amino acid transport activity, System A, is enhanced by amino acid limitation of mammalian cells. Of the three gene products that encode System A activity, the one that exhibits this regulation is SNAT2 (sodium-coupled neutral amino acid
Disease: (OMIM: 138500 242600 608331) Defects in SLC36A2 are a cause of hyperglycinuria (HG) [MIM:138500]. It is a condition characterized by excess of glycine in the urine. In some cases it is associated with renal colic and renal oxalate stones; Defects in SLC36A2 are a cause of iminoglycinuria (IG) [MIM:242600]. It is a disorder of renal tubular reabsorption of glycine and imino acids (proline and hydroxyproline), marked by excessive levels of all three substances in the urine. Note=Mutations in SLC36A2 that retain residual transport activity result in the IG phenotype only when combined with haploinsufficiency of the imino acid transporter SLC6A20 or deficiency of the neutral amino acid transporter SLC6A19. Additional polymorphisms and mutations in SLC6A18 can contribute to iminoglycinuria in some families ...
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Download the 2020 Educational Webinar Registration Form and mail or email to ASCT with payment. You will receive your webinar access information via email from ASCT after payment is received. Using your email address, the ASCT will send you the link to access the webinar. Participants can choose to hear the audio via the phone or over their computer speakers. Each webinar will offer one CE credit as defined by the ASCP CMP.. All Members and Non-Members may purchase ASCT educational webinars online by clicking here.. Individual Webinar Registration ...
EAS L-Glutamine One of the most readily available amino acids in your body is glutamine. Glutamine is very important. In fact, it is considered essential when it comes to the repair and recovery of your body after training sessions. This is why EAS laboratories have developed L-Glutamine.
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L-glutamine is an amino acid. It is one of the building blocks of protein and in the grand scheme of the body one of the building blocks of life.
While L-Glutamine continues to become more popular for its use with digestive issues, particularly the growing complaint of leaky gut, it has some risks
I need some help. I have a ASC case where the MD did a cystourethroscopy w/ bilaterial retrograde ureterograms. He also did Litholapaxy with the extra
TECHNICALLY, Tryptophan doesnt directly make you drowsy. A more-likely hypothesis is that the ingestion of large quantities of food, such as at a Thanksgiving feast, means that large quantities of both carbohydrates and branched-chain amino acids are consumed. Like carbohydrates, branched-chain amino acids require insulin to be transduced through the myocyte membranes, which, after a large meal, creates a competition among the amino acids and glucose for insulin, while simultaneously creating tryptophans reduced competition with other amino acids for the Large Neutral Amino Acid Transporter protein for transduction across the blood-brain barrier. The result is a greater availability of tryptophan, via the Large Neutral Amino Acid Transporter, for conversion into serotonin by the raphe nuclei, which is then available for conversion into melatonin by the pineal gland. Drowsiness is the result ...
Lysine Exporters are a superfamily of transmembrane proteins which export amino acids, lipids and heavy metal ions. They provide ionic homeostasis, play a role in cell envelope assembly, and protect from excessive concentrations of heavy metals in cytoplasm. The superfamily was named based on the early discovery of the LysE carrier protein of Corynebacterium glutamicum. 2.A.75 - The L-Lysine Exporter (LysE) Family 2.A.76 - The Resistance to Homoserine/Threonine (RhtB) Family 2.A.77 - The Cadmium Resistance (CadD) Family 2.A.95 - The 6TMS Neutral Amino Acid Transporter (NAAT) Family 2.A.106 - The Ca2+:H+ Antiporter-2 (CaCA2) Family 2.A.107 - The Mn2+ exporter (MntP) Family 2.A.108 - The Iron/Lead Transporter (ILT) Family 2.A.109 - The Tellurium Ion Resistance (TerC) Family 2.A.113 - The Nickel/Cobalt Transporter (NicO) Family 2.A.116 - The Peptidoglycolipid Addressing Protein (GAP) Family 5.A.1 - The Disulfide Bond Oxidoreductase D (DsbD) Family Two members of the LysE family (LysE of ...
The Alanine, Serine, Cysteine Transporters (ASCTs) mediate the Na+-dependent transport of neutral amino acids. ASCT2 is the predominant glutamine transport system for human cancer cells, and is upregulated across various types of cancer. ASCT1 and ASCT2 share 57% amino acid sequence identity, however they display varying substrate selectivity profiles. ASCT1 transports small neutral amino acids including alanine, serine and cysteine. ASCT2 transports a broader range of substrates, including glutamine, asparagine and methionine. In this study, we investigate the molecular basis for differences in substrate selectivity between the ASCTs. Mutating the key substrate binding residue in ASCT1 to the ASCT2 equivalent (T459C) introduced glutamine sensitivity. The additional mutation T458S to create T458S/T459C increased the glutamine affinity to reflect that of ASCT2. Similarly, glutamyl-p-nitroanilide (GPNA) is an inhibitor of ASCT2 but not ASCT1. T459C did not display an increased sensitivity to GPNA, ...
Rai, K. M. Lokanatha and Umesha, K. B. and Yathirajan, H. S. (1999) Determination of molecular weight of neutral amino acids with chloramine-T. JOURNAL OF THE INDIAN CHEMICAL SOCIETY, 76 (3). pp. 170-171. Full text not available from this repository. (Request a copy ...
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Praktické cvičenie č. 2 Stafylokokové infekcie. Diagnostika stafylokokových infekcií Diagnostický model: absces - hnis, enterotoxikóza - zvyšky potravín, osteomyelitída - punktát, Mikroskopia, kultivácia, biochemické testy, dôkaz patogenity, citlivosť na ATB. 1 normálna...
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p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
12. Nov. 2019: ATB-Wissenschaftler Niels Landwehr wurde gestern im Rahmen des Großen Professoriums an der Universität Potsdam als neu berufener Professor für "Data Science in Agriculture" an der Mathematisch-Naturwissenschaftlichen Fakultät der Universität Potsdam begrüßt. Die Ernennung erfolgte.... ». ...
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Amino acids represent a strong signal that positively regulates mTORC1 (reviewed by Guertin and Sabatini, 2007). It was recently shown that leucine, an essential amino acid required for mTORC1 activation, is transported into cells in a glutamine-dependent fashion (Nicklin et al., 2009). Glutamine, which is imported into cells through SLC1A5 [solute carrier family 1 (neutral amino acid transporter) member 5], is exchanged to import leucine via a heterodimeric system composed of SLC7A5 [antiport solute carrier family 7 (cationic amino acid transporter, y+ system, member 5] and SLC3A2 [solute carrier family 3 (activators of dibasic and neutral amino acid transport) member 2]. The mechanism by which intracellular amino acids then signal to mTORC1 remained obscure for many years. The activation of mTORC1 by amino acids is known to be independent of TSC1/2, because the mTORC1 pathway remains sensitive to amino acid deprivation in cells that lack TSC1 or TSC2 (Nobukuni et al., 2005). Some studies have ...
Find SLC3: Heavy Subunits of the Heteromeric Amino Acid Transporter Family research area related information and SLC3: Heavy Subunits of the Heteromeric Amino Acid Transporter Family research products from R&D Systems. Learn more.
MetabolismTransport and binding proteinsAmino acids, peptides and aminesbranched-chain amino acid transport system II carrier protein (TIGR00796; HMM-score: 412.2) ...
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Using some chicory or other bitter lettuce complements the creamy sweetness of the blue cheese.. Serve with crustless cucumber sandwiches.. Adapted from "Skinny Soups: 80 Flavor-Packed Recipes of Less Than 300 Calories," by Kathryn Bruton (Kyle Books, 2017).. Ingredients. (3 or 4 servings (makes about 5 cups), Healthy). 3 cups no-salt-added vegetable or chicken broth. 1 leek. 1 rib celery. 1 clove garlic. 1 1/2 teaspoons olive oil. 1 pound mixed lettuces, such as baby gem, chicory and romaine. 2 1/2 ounces Gorgonzola dolce, plus a bit more for optional garnish. 3/4 to 1 1/4 cups packed basil leaves. 1 lemon. Kosher salt. Freshly ground black pepper. Method. Pour the broth into a medium saucepan over medium-high heat, letting it come to a boil.. While thats heating up, trim the leeks root end and tough green leaves. Split the rest in half lengthwise and rinse thoroughly, then cut crosswise into thin slices. Coarsely chop the celery and garlic.. Heat the oil in a deep saute pan over medium heat. ...

Identification and Functional Characterization of a Na+-Independent Large Neutral Amino Acid Transporter, LAT1, in Human and...Identification and Functional Characterization of a Na+-Independent Large Neutral Amino Acid Transporter, LAT1, in Human and...

ASC, asc, b0,+, B0,+ and x−, Gly, n, and T. 25 26 27 28 29 30 31 32 System L is a major amino acid transporter that transports ... Among the amino acid transport systems, the A system is sodium-dependent and inhibited by NMAIB, the L system is sodium ... Su, TZ, Lunney, E, Campbell, G, et al (1995) Transport of gabapentin, a gamma-amino acid drug, by system L alpha-amino acid ... 34 System L has been known to transport not only naturally occurring amino acids but also amino acid-related compounds such as ...
more infohttp://iovs.arvojournals.org/article.aspx?articleid=2181705

Amino acid transport System A resembles System N in sequence but differs in mechanism | PNASAmino acid transport System A resembles System N in sequence but differs in mechanism | PNAS

... unlike System ASC, System L does not depend on Na+. Thus, two of the three general amino acid transport systems mediate ... Three principal transport systems account for much of the amino acid uptake by mammalian cells (1, 2). System ASC ... Classical amino acid transport System A accounts for most of the Na+-dependent neutral amino acid uptake by mammalian cells. ... System L recognizes branched chain and aromatic amino acids (6). Like System ASC, System L catalyzes exchange rather than net ...
more infohttps://www.pnas.org/content/97/14/7715

Glucagon: acute actions on hepatic metabolism | SpringerLinkGlucagon: acute actions on hepatic metabolism | SpringerLink

Lim SK, Cynober L, De Bandt JP, Aussel C (1999) A Na+-dependent system A and ASC-independent amino acid transport system ... Glucagon has been shown to stimulate amino acid transporters, both the system A and system N transport pathways, which account ... Gebhardt R, Kleemann E (1987) Hormonal regulation of amino acid transport system N in primary cultures of rat hepatocytes. Eur ... Given the known role of amino acids in triggering the secretion of glucagon from the alpha cell, the elevated amino acids ...
more infohttps://link.springer.com/article/10.1007/s00125-016-3955-y

Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid...Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid...

... resulted in ATF4-dependent upregulation of several amino acid transporters, including SLC1A5 and its truncated isoforms, which ... Activating Transcription Factor 4, Amino Acid Transport System ASC, Amino Acid Transport Systems, Cell Line, Tumor, Cellular ... Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid ... Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid ...
more infohttps://www.rdm.ox.ac.uk/publications/645765

PDF] Heteromeric amino acid transporters: biochemistry, genetics, and physiology. | Semantic ScholarPDF] Heteromeric amino acid transporters: biochemistry, genetics, and physiology. | Semantic Scholar

HATs represent several of the classic mammalian amino acid transport systems (e.g., L isoforms, y(+)L isoforms, asc, x(c)(-), ... In addition to the role in amino acid transport, one HSHAT [the heavy subunit of the cell-surface antigen 4F2 (also named CD98 ... The heteromeric amino acid transporters (HATs) are composed of two polypeptides: a heavy subunit (HSHAT) and a light subunit ( ... HATs represent several of the classic mammalian amino acid transport systems (e.g., L isoforms, y(+)L isoforms, asc… CONTINUE ...
more infohttps://www.semanticscholar.org/paper/Heteromeric-amino-acid-transporters%3A-biochemistry%2C-Chillar%C3%B3n-Roca/9d7fb82ef12d96940f9f0250932186321cae1e95

Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid...Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid...

... resulted in ATF4-dependent upregulation of several amino acid transporters, including SLC1A5 and its truncated isoforms, which ... Activating Transcription Factor 4, Amino Acid Transport System ASC, Amino Acid Transport Systems, Cell Line, Tumor, Cellular ... Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid ... Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid ...
more infohttps://pharm.ox.ac.uk/publications/645765

Bidirectional transport of amino acids regulates mTOR and autophagy.  - PubMed - NCBIBidirectional transport of amino acids regulates mTOR and autophagy. - PubMed - NCBI

Amino Acid Transport System ASC/metabolism. *Animals. *Autophagy*. *Cell Line, Tumor. *Drosophila melanogaster ... G) S2 or S2-R Drosophila cells starved of serum and amino acids were then treated with amino acids in the presence or absence ... Bidirectional transport of amino acids regulates mTOR and autophagy.. Nicklin P1, Bergman P, Zhang B, Triantafellow E, Wang H, ... RNAi-Mediated Downregulation of SLC1A5, SLC3A2, or SLC7A5 Inhibits Amino Acid Transport and mTOR Pathway Activity. (A) HeLa ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/19203585?dopt=Abstract

phosphatidylethanolamine binding proteinphosphatidylethanolamine binding protein

amino acid transport system asc*flowering tops*nematospiroides dubius*neoplasm genes. Genomes and Genes. *PEBP1 products*Pebp1 ... You are here: Research Topics , and proteins peptides amino acids , peptides , intracellular signaling peptides and proteins , ... Our results therefore suggest that the RKIP conserved pocket may constitute a novel phosphoamino-acid binding motif and is ... the central nervous system and reproduction. Cell Signal. 2008;20:1-9 pubmed ...
more infohttp://www.labome.org/topics/and/peptides/intracellular/phosphatidylethanolamine-binding-protein-13946.html

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The third and most recently discovered is the neutral amino acid transport system ASCT1 (ASC for Ala- Ser- and Cys-preferring ... 959) D-amino acid (p. The binding activities of the monovalent and bivalent ligands measured by com- petitive ELISA assay are ... Computer algebra systems have commands that plot sample gradient vectors. [38] Stop TB Partnership. In this formula, P is a ... There can also be problems in both systems.1997; Miyoshi et al. thyroid artery. I looked at the time and ttading was almost at ...
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Manganese disrupts astrocyte glutamine transporter expression and function.  - PubMed - NCBIManganese disrupts astrocyte glutamine transporter expression and function. - PubMed - NCBI

Amino Acid Transport System ASC/antagonists & inhibitors*. *Amino Acid Transport System ASC/biosynthesis ... Amino Acid Transport System ASC/metabolism*. *Amino Acid Transport System ASC/physiology ... p , 0.05 versus total control; # p , 0.05 versus system N control; Δ p , 0.05 versus system ASC control; @ p,0.05 versus system ... system A) and LAT2 (system L), and lowered the protein but not mRNA expression of ASCT2 (system ASC). Mn exposure did not ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/19457077?dopt=Abstract

N-ACETYL L-CYSTEINE CHELATES AND METHODS FOR MAKING AND USING THE SAME - XIE XUEJUN-ACETYL L-CYSTEINE CHELATES AND METHODS FOR MAKING AND USING THE SAME - XIE XUEJU

ASC) system, a ubiquitous system of Na+-dependent neutral amino acid transport, in a variety of cells. NAC is a membrane- ... Mineral amino acid chelates, including derivative amino acid chelates, are often absorbed intact by amino acid absorption ... Mineral amino acid chelates, including derivative amino acid chelates, usually do not dissociate into free mineral ions in the ... Natural amino acid chelates bind to metallic and inorganic minerals, including calcium, phosphate, and potassium. Amino acid ...
more infohttp://www.freepatentsonline.com/y2015/0038577.html

Development and Physiology of the Placenta and Membranes | GLOWMDevelopment and Physiology of the Placenta and Membranes | GLOWM

... and the ASC, or alanine-serine system. Each system preferentially transports certain neutral amino acids, but there is ... transporting the L-amino acids more rapidly than the D-amino acids. Recent evidence also indicates that placental amino acid ... the active transport of amino acids is mediated by several pathways that are specific for several groups of amino acids. Three ... The fetal uptake of amino acids may depend to some extent on this concentrating capacity of the placenta. Uptake of amino acids ...
more infohttp://www.glowm.com/section_view/heading/Development%20and%20Physiology%20of%20the%20Placenta%20and%20Membranes/item/101

The importance of serine metabolism in cancer | JCBThe importance of serine metabolism in cancer | JCB

Serine is a small, neutral amino acid and, as such, can be transported by one of three systems. Two of the systems are sodium ... The third is a family of neutral amino acid antiporters, the alanine/serine/cysteine transporter (ASC) system (El-Hattab, 2016 ... suggesting that active serine synthesis might be required to facilitate amino acid transport, nucleotide synthesis, folate ... In Amino Acid Metabolism. W.D. McElroy, and B. Glass, editors. Johns Hopkins, Baltimore. 782-796. ...
more infohttp://jcb.rupress.org/content/214/3/249?cct=1418

Search Articles | University of Toronto LibrariesSearch Articles | University of Toronto Libraries

Amino Acid Transport System ASC - physiology , Gene Products, env - physiology , Pregnancy Proteins - physiology , Adult , ... Amino Acid Transport System ASC - antagonists & inhibitors , Cell Communication , Pregnancy , Microscopy, Confocal , Tumor ... Amino Acid Transport System ASC - genetics , Trophoblasts - metabolism , Furin - physiology , RNA, Small Interfering - ... Amino acids , Biosynthesis , Kinases , Deletion mutant , Proteins , Renin , Clonal deletion , Deletion , Furin , Cleavage , ...
more infohttps://query.library.utoronto.ca/index.php/search/q?kw=SubjectTerms:Furin%20-%20antagonists%20&%20inhibitors

Search Articles | University of Toronto LibrariesSearch Articles | University of Toronto Libraries

Amino Acid Transport System ASC - metabolism , Male , NF-kappa B - metabolism , CARD Signaling Adaptor Proteins - genetics , ... LACTIC-ACID , ORIGIN , TRANSMISSION , LACHNOSPIRACEAE , MULTIDISCIPLINARY SCIENCES , RAW-MILK , MICROBIOTA , DIVERSITY , ... LEPTIN , SYSTEM , MULTIDISCIPLINARY SCIENCES , FETAL-GROWTH , BINDING PROTEIN-1 , RECEPTOR , TERM , INTERLEUKIN-6 , GROWTH- ... Infants (Newborn) , RNA sequencing , Polysaccharides , Microbiota (Symbiotic organisms) , Analysis , Gastrointestinal system , ...
more infohttps://query.library.utoronto.ca/index.php/search/q?kw=Author:Bernasconi,%20Sergio

Frontiers | Functional Polarity of Microvascular Brain Endothelial Cells Supported by Neurovascular Unit Computational Model of...Frontiers | Functional Polarity of Microvascular Brain Endothelial Cells Supported by Neurovascular Unit Computational Model of...

The LAT1-mediated trans-endothelial transport of LNAAs, however, could not be characterized precisely by available in vitro and ... The LAT1-mediated trans-endothelial transport of LNAAs, however, could not be characterized precisely by available in vitro and ... allowing us to evaluate hypotheses concerning LAT1-mediated trans-endothelial transport of LNAAs across the blood brain barrier ... allowing us to evaluate hypotheses concerning LAT1-mediated trans-endothelial transport of LNAAs across the blood brain barrier ...
more infohttps://www.frontiersin.org/articles/10.3389/fphys.2018.00171/full

Altered tryptophan and alanine transport in fibroblasts from boys with attention-deficit/hyperactivity disorder (ADHD): an in...Altered tryptophan and alanine transport in fibroblasts from boys with attention-deficit/hyperactivity disorder (ADHD): an in...

... system A, and system ASC [12].. In order to study amino acid transport properties, in various psychiatric disorders, fibroblast ... Transport assay of amino acids. Amino acid transport was measured using the cluster tray method for rapid measurement of amino ... by different amino acid transport systems [12-14]. A competition between amino acids using the same transporters exists [13, 15 ... transported through system A, by its isoform ATA2 [12]. System A is known to transport short-chain amino acids, such as alanine ...
more infohttps://behavioralandbrainfunctions.biomedcentral.com/articles/10.1186/1744-9081-7-40

Correlation between 18 F-1-amino-3-fluorocyclobutane-1-carboxylic acid ( 18 F-fluciclovine) uptake and expression of alanine...Correlation between 18 F-1-amino-3-fluorocyclobutane-1-carboxylic acid ( 18 F-fluciclovine) uptake and expression of alanine...

Our findings suggest that LAT1 is moderately associated with the transport of 18F-fluciclovine in local PCa not exposed to ... and their impact on uptake of 18F-1-amino-3-fluorocyclobutane-1-carboxylic acid (18F-fluciclovine) which is approved for the ... and L-type amino acid transporter1 (LAT1) in prostate cancer (PCa) ... for system ASC and sodium-independent L-type amino acid transporter 1 (LAT1) for system L. [4]. The expression of these amino ...
more infohttps://ejnmmires.springeropen.com/articles/10.1186/s13550-019-0518-5

The light subunit of system bo,+ is fully functional in the absence of the heavy subunit | The EMBO JournalThe light subunit of system bo,+ is fully functional in the absence of the heavy subunit | The EMBO Journal

Transport in exchange with the internal amino acid was calculated by subtracting transport in the absence of amino acid in the ... system asc (Fukasawa et al., 2000; Nakauchi et al., 2000), (iii) with y+LAT‐1 or y+LAT‐2, variants of system y+L (Torrents et ... System bo,+ is an exchanger for the influx of cystine and dibasic amino acids and the efflux of neutral amino acids (for a ... In order to characterize further the amino acid transport activity of the reconstituted bo,+AT, several amino acids were ...
more infohttp://emboj.embopress.org/content/21/18/4906?ijkey=087a1321e2730e5dfb76da604ca2c0288e551eab&keytype2=tf_ipsecsha

The gene expression of numerous SLC transporters is altered in the immortalized hypothalamic cell line N25/2 following amino...The gene expression of numerous SLC transporters is altered in the immortalized hypothalamic cell line N25/2 following amino...

ASC, L, N, T, xc-, and y+. UsingGO annotations, genes involved in amino acid transport and amino acidtransmembrane transporter ... pathwayand the amino acid responsive (AAR) pathway. It is vital for cells tohave a system to sense amino acid levels, in order ... Amino acids are known to play a key role in gene expression regulation,and in mammalian cells, amino acid signaling is mainly ... Amino acid transporters are crucialin these pathways, due to both their sensing and transport functions. Inthis large-scale ...
more infohttp://uu.diva-portal.org/smash/record.jsf?pid=diva2%3A1148778&c=26&searchType=SIMPLE&language=en&query=&af=%5B%5D&aq=%5B%5B%7B%22personId%22%3A%22authority-person%3A11492%22%7D%5D%5D&aq2=%5B%5B%5D%5D&aqe=%5B%5D&noOfRows=50&sortOrder=author_sort_asc&sortOrder2=title_sort_asc&onlyFullText=false&sf=all

Prolonged infusion of amino acids increases leucine oxidation in fetal sheep | Endocrinology and MetabolismProlonged infusion of amino acids increases leucine oxidation in fetal sheep | Endocrinology and Metabolism

Multiple amino acids share affinity for several transporter systems (32, 33). Specifically, the β°+ and ASC amino acid ... Thus a direct fetal amino acid infusion might have decreased placental transport of amino acids. The mechanism for this remains ... and long-term maternal amino acid infusions using mixtures of amino acids with a higher essential-nonessential amino acid ... Fetal supply of amino acids and amino nitrogen after maternal infusion of amino acids in pregnant sheep. Am J Obstet Gynecol ...
more infohttp://ajpendo.physiology.org/content/302/12/E1483

Global Library of Womens Medicine - Placental Physiology - DOI 10.3843/GLOWM.10195Global Library of Women's Medicine - Placental Physiology - DOI 10.3843/GLOWM.10195

... decrease amino acid transport. Limiting supplies of oxygen or glucose to the placenta decreases amino acid transport. ... Shennan DB, Boyd CAR: Ion transport by the placenta: A review of membrane transport systems. Biochim Bio Physica Acta 906: 437 ... "ASC," transferring alanine, serine, and cysteine; and XAG, selectively permeable to acidic amino acids (glutamate and aspartate ... Amino Acids. The placenta actively transports all amino acids, with fetal concentrations exceeding maternal levels. ...
more infohttp://editorial.glowm.com/?p=glowm.cml/section_view&articleid=195

Alkylator resistance in human B lymphoid cell lines: (1). Melphalan accumulation, cytotoxicity, interstrand-DNA-crosslinks,...Alkylator resistance in human B lymphoid cell lines: (1). Melphalan accumulation, cytotoxicity, interstrand-DNA-crosslinks,...

... heptane-2-carboxylic acid(BCH) in both cell lines, indicating that the amino acid transport (System L, which is sodium ... Only a minor degree of inhibition of melphalan transport was noted after sodium depletion (System ASC, which is sodium ... Melphalan transport studies demonstrated decreased initial melphalan accumulation in WSU-CLL cells as compared to WIL2 cells. ... Melphalan transport, glutathione levels, and glutathione-S-transferase activity in human medulloblastoma. ...
more infohttps://christie.openrepository.com/handle/10541/86144

Amino Acid Transport Across the Mammalian Intestine - Comprehensive PhysiologyAmino Acid Transport Across the Mammalian Intestine - Comprehensive Physiology

ABSTRACT The small intestine mediates the absorption of amino acids after ingestion of protein and sustains the supply of amino ... Transport of neutral, cationic and anionic amino acids by systems B, b(o,+), X(AG), and ASC in swine small intestine. Comp ... AA0, neutral amino acids, AA+, cationic amino acids, AA−, anionic amino acids. Tau, taurine; β, beta‐amino acids, P, proline; G ... AA0, neutral amino acids, AA+, cationic amino acids, AA−, anionic amino acids. Tau, taurine; β, beta‐amino acids, P, proline; G ...
more infohttp://www.comprehensivephysiology.com/WileyCDA/CompPhysArticle/refId-c170041.html

List of MeSH codes (D12.776.157) - WikipediaList of MeSH codes (D12.776.157) - Wikipedia

... amino acid transport system a MeSH D12.776.157.530.200.500.200 -- amino acid transport system asc MeSH D12.776.157.530.200.500. ... amino acid transport systems, acidic MeSH D12.776.157.530.200.249.500 -- amino acid transport system x-ag MeSH D12.776.157.530. ... amino acid transport systems, basic MeSH D12.776.157.530.200.374.600 -- amino acid transport system y+ MeSH D12.776.157.530. ... cationic amino acid transporter 2 MeSH D12.776.157.530.200.374.750 -- amino acid transport system y+l MeSH D12.776.157.530. ...
more infohttps://en.wikipedia.org/wiki/List_of_MeSH_codes_(D12.776.157)
  • Recent studies cast new light on the role of serine metabolism in cancer, suggesting that active serine synthesis might be required to facilitate amino acid transport, nucleotide synthesis, folate metabolism, and redox homeostasis in a manner that impacts cancer. (rupress.org)
  • The importance of serine metabolism in multiple cancers is increasingly apparent, and how the metabolism of this amino acid influences cancer phenotypes is an area of active investigation. (rupress.org)
  • Amino acids are required for activation of the mammalian target of rapamycin (mTOR) kinase which regulates protein translation, cell growth, and autophagy. (nih.gov)
  • Due to their ability to transport a large repertoire of substances across, not just the plasma membrane, but also the membrane of internal organelles, they hold a key position in maintaining homeostasis affecting metabolic pathways. (diva-portal.org)
  • Similarly, supplementation of pregnant sheep with intravenous amino acids for several days at the end of gestation demonstrated adverse fetal effects, including hypoxia and respiratory and metabolic acidosis ( 34 ). (physiology.org)
  • The molecular basis for L-glutamine sensitivity is due to SLC7A5/SLC3A2, a bidirectional transporter that regulates the simultaneous efflux of L-glutamine out of cells and transport of L-leucine/EAA into cells. (nih.gov)
  • Melphalan transport studies demonstrated decreased initial melphalan accumulation in WSU-CLL cells as compared to WIL2 cells. (openrepository.com)
  • Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid Transporter Profile in Tumor Cells. (ox.ac.uk)
  • G) S2 or S2-R Drosophila cells starved of serum and amino acids were then treated with amino acids in the presence or absence of L-glutamine. (nih.gov)
  • b o,+ AT‐reconstituted systems from HeLa or MDCK cells catalysed transport of arginine that was totally dependent on the presence of one of the b o,+ substrates inside the liposomes. (embopress.org)
  • No system b o,+ transport was detected in liposomes derived from cells expressing rBAT alone. (embopress.org)
  • SLC3A2 protein provides cells with the capacity of adjusting to their surroundings by mediating two fundamental molecular functions: amino acid transport and integrin signaling. (springer.com)
  • UsingGO annotations, genes involved in amino acid transport and amino acidtransmembrane transporter activity were found to be most upregulated at3 h and 5 h of starvation. (diva-portal.org)
  • Despite progress made in the model plant Arabidopsis, one of the main obstacles to a better understanding of the genes and pathways underlying nonhost resistance is the lack of genetically tractable systems segregating for this type of resistance, which often operates at the species level. (plantphysiol.org)
  • It is not known whether these observations are specific to the mode of delivery of supplemental amino acids to the fetus (via the mother and placenta vs. a direct fetal infusion) or to the excess amino acids themselves. (physiology.org)
  • Glutamine transport was relatively weakly inhibited by a 50-fold excess of leucine and was not inhibited by phenylalanine or N -methyl aminoisobutyrate. (biochemj.org)
  • Taken together, different classes of NVU-AATs constitute an integrated dynamic system controlling the homeostasis of AAs such as large neutral amino acids (LNAAs: L-tyrosine, L-leucine, L-isoleucine, L-phenylalanine, L-histidine, L-valine, L-tryptophan, and L-methionine) in the brain interstitial fluid (ISF). (frontiersin.org)
  • 17 18 19 20 A few reports about the presence of carrier-mediated nutrient transport systems on the cornea are available, but most of them are believed to be present on the corneal endothelium. (arvojournals.org)
  • Three inter-related areas, intestinal nutrient transport, intestinal drug transport and epithelial-bacterial pathogen interactions are the focus of current research. (ncl.ac.uk)
  • The BBB endothelium together with the astrocytes and neurons are the fundamental elements of the neurovascular unit (NVU) system. (frontiersin.org)
  • Moreover, stimulant agents, such as methylphenidate, amphetamine and atomoxetine, which currently are the most common drugs used for treatment of ADHD, act primarily on the catecholaminergic system. (biomedcentral.com)
  • Consistent with this sensitivity, we found that the System N transporter (SN1) mediates proton exchange as well as Na + cotransport ( 26 ). (pnas.org)
  • A disturbed transport of tyrosine, as well as other amino acids, has been found in a number of other psychiatric disorders, such as schizophrenia, bipolar disorder and autism, when using the fibroblast cell model. (biomedcentral.com)
  • To bypass placental transport, singleton fetal sheep were intravenously infused with an amino acid mixture (AA, n = 8) or saline [control (Con), n = for ∼12 days during late gestation. (physiology.org)