Amino Acid Transport Systems
Amino Acid Transport System L
Amino Acid Transport Systems, Basic
Amino Acid Transport System A
Amino Acid Transport Systems, Neutral
Biological Transport, Active
Amino Acid Transport System ASC
Membrane Transport Proteins
Fatty Acid Transport Proteins
Amino Acid Sequence
Amino Acid Transport Systems, Acidic
Molecular Sequence Data
Sequence Homology, Amino Acid
Rats, Inbred Strains
Large Neutral Amino Acid-Transporter 1
Antigens, CD98 Light Chains
Antigens, CD98 Heavy Chain
Amino Acid Substitution
Amino Acid Transport System X-AG
Monosaccharide Transport Proteins
Amino Acid Transport Disorders, Inborn
Amino Acids, Essential
Cationic Amino Acid Transporter 1
Amino Acid Motifs
ATP-Binding Cassette Transporters
Organic Anion Transporters
Anion Transport Proteins
Genetic Complementation Test
Radioisotope Dilution Technique
Protein Structure, Tertiary
Sequence Homology, Nucleic Acid
Recombinant Fusion Proteins
Organic Anion Transporters, Sodium-Dependent
Bile Acids and Salts
Glutamate Plasma Membrane Transport Proteins
Carcinoma, Ehrlich Tumor
Periplasmic Binding Proteins
Electrophoresis, Polyacrylamide Gel
Cell Membrane Permeability
Sequence Analysis, DNA
Gene Expression Regulation
Cation Transport Proteins
Dose-Response Relationship, Drug
Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons. (1/736)The characterization of the Caenorhabditis elegans unc-47 gene recently allowed the identification of a mammalian (gamma)-amino butyric acid (GABA) transporter, presumed to be located in the synaptic vesicle membrane. In situ hybridization data in rat brain suggested that it might also take up glycine and thus represent a general Vesicular Inhibitory Amino Acid Transporter (VIAAT). In the present study, we have investigated the localization of VIAAT in neurons by using a polyclonal antibody raised against the hydrophilic N-terminal domain of the protein. Light microscopy and immunocytochemistry in primary cultures or tissue sections of the rat spinal cord revealed that VIAAT was localized in a subset (63-65%) of synaptophysin-immunoreactive terminal boutons; among the VIAAT-positive terminals around motoneuronal somata, 32.9% of them were also immunoreactive for GAD65, a marker of GABAergic presynaptic endings. Labelling was also found apposed to clusters positive for the glycine receptor or for its associated protein gephyrin. At the ultrastructural level, VIAAT immunoreactivity was restricted to presynaptic boutons exhibiting classical inhibitory features and, within the boutons, concentrated over synaptic vesicle clusters. Pre-embedding detection of VIAAT followed by post-embedding detection of GABA or glycine on serial sections of the spinal cord or cerebellar cortex indicated that VIAAT was present in glycine-, GABA- or GABA- and glycine-containing boutons. Taken together, these data further support the view of a common vesicular transporter for these two inhibitory transmitters, which would be responsible for their costorage in the same synaptic vesicle and subsequent corelease at mixed GABA-and-glycine synapses. (+info)
Cutting edge: primary structure of the light chain of fusion regulatory protein-1/CD98/4F2 predicts a protein with multiple transmembrane domains that is almost identical to the amino acid transporter E16. (2/736)The CD98 light chain (CD98LC) was copurified from HeLa S3 cells by an affinity chromatography using a mAb specific for the fusion regulatory protein-1 (FRP-1) which is identical to the CD98 heavy chain. On the basis of the N-terminal sequence (63 amino acids) of purified CD98LC polypeptide, we have cloned a PCR fragment (155 bp) from a HeLa S3 cDNA library and finally obtained a full cDNA clone encoding the CD98LC. Fluorescence in situ hybridization analysis using the cDNA assigned the CD98LC gene to the long arm of human chromosome 16 (16q24). The predicted amino acid sequence suggested that CD98LC is a protein with multiple transmembrane domains and is almost identical to the amino acid transporter E16. Resting monocytes and lymphocytes expressed CD98LC as analyzed by a newly isolated anti-CD98LC mAb, which showed cross-reactivity with insect Sf9 cells as well as with various mammalian cell lines. (+info)
NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. (3/736)Addition of ammonium ions to yeast cells growing on proline as the sole nitrogen source induces internalization of the general amino acid permease Gap1p and its subsequent degradation in the vacuole. An essential step in this down-regulation is Gap1p ubiquitination through a process requiring the Npi1p/Rsp5p ubiquitin ligase. We show in this report that NPI2, a second gene required for NH4+-induced down-regulation of Gap1p, codes for the ubiquitin hydrolase Doa4p/Ubp4p/Ssv7p and that NH4+-induced Gap1p ubiquitination is strongly reduced in npi2 cells. The npi2 mutation results in substitution of an aromatic amino acid located in a 33-residue sequence shared by some ubiquitin hydrolases of the Ubp family. In this mutant, as in doa4(delta) cells, the amount of free monomeric ubiquitin is at least four times lower than in wild-type cells. Both ubiquitination and down-regulation of the permease can be restored in npi2 cells by over-expression of ubiquitin. In proline-grown wild-type and npi2/doa4 cells overproducing ubiquitin, Gap1p appears to be mono-ubiquitinated at two lysine acceptor sites. Addition of NH4+ triggers rapid poly-ubiquitination of Gap1p, the poly-ubiquitin chains being specifically formed by linkage through the lysine 63 residue of ubiquitin. Gap1p is thus ubiquitinated differently from the proteins targeted by ubiquitination for proteolysis by the proteasome, but in the same manner as the uracil permease, also subject to ubiquitin-dependent endocytosis. When poly-ubiquitination through Lys63 is blocked, the Gap1p permease still undergoes NH4+-induced down-regulation, but to a lesser extent. (+info)
The ArgR regulatory protein, a helper to the anaerobic regulator ANR during transcriptional activation of the arcD promoter in Pseudomonas aeruginosa. (4/736)Pseudomonas aeruginosa, when deprived of oxygen, generates ATP from arginine catabolism by enzymes of the arginine deiminase pathway, encoded by the arcDABC operon. Under conditions of low oxygen tension, the transcriptional activator ANR binds to a site centered 41.5 bp upstream of the arcD transcriptional start. ANR-mediated anaerobic induction was enhanced two- to threefold by extracellular arginine. This arginine effect depended, in trans, on the transcriptional regulator ArgR and, in cis, on an ArgR binding site centered at -73.5 bp in the arcD promoter. Binding of purified ArgR protein to this site was demonstrated by electrophoretic mobility shift assays and DNase I footprinting. This ArgR recognition site contained a sequence, 5'-TGACGC-3', which deviated in only 1 base from the common sequence motif 5'-TGTCGC-3' found in other ArgR binding sites of P. aeruginosa. Furthermore, an alignment of all known ArgR binding sites confirmed that they consist of two directly repeated half-sites. In the absence of ANR, arginine did not induce the arc operon, suggesting that ArgR alone does not activate the arcD promoter. According to a model proposed, ArgR makes physical contact with ANR and thereby facilitates initiation of arc transcription. (+info)
Yeast mutants affecting possible quality control of plasma membrane proteins. (5/736)Mutations gef1, stp22, STP26, and STP27 in Saccharomyces cerevisiae were identified as suppressors of the temperature-sensitive alpha-factor receptor (mutation ste2-3) and arginine permease (mutation can1(ts)). These suppressors inhibited the elimination of misfolded receptors (synthesized at 34 degrees C) as well as damaged surface receptors (shifted from 22 to 34 degrees C). The stp22 mutation (allelic to vps23 [M. Babst and S. Emr, personal communication] and the STP26 mutation also caused missorting of carboxypeptidase Y, and ste2-3 was suppressed by mutations vps1, vps8, vps10, and vps28 but not by mutation vps3. In the stp22 mutant, both the mutant and the wild-type receptors (tagged with green fluorescent protein [GFP]) accumulated within an endosome-like compartment and were excluded from the vacuole. GFP-tagged Stp22p also accumulated in this compartment. Upon reaching the vacuole, cytoplasmic domains of both mutant and wild-type receptors appeared within the vacuolar lumen. Stp22p and Gef1p are similar to tumor susceptibility protein TSG101 and voltage-gated chloride channel, respectively. These results identify potential elements of plasma membrane quality control and indicate that cytoplasmic domains of membrane proteins are translocated into the vacuolar lumen. (+info)
Stimulation of Na+-alanine cotransport activates a voltage-dependent conductance in single proximal tubule cells isolated from frog kidney. (6/736)1. The swelling induced by Na+-alanine cotransport in proximal tubule cells of the frog kidney is followed by regulatory volume decrease (RVD). This RVD is inhibited by gadolinium (Gd3+), an inhibitor of stretch-activated channels, but is independent of extracellular Ca2+. 2. In this study, the whole cell patch clamp technique was utilized to examine the effect of Na+-alanine cotransport on two previously identified volume- and Gd3+-sensitive conductances. One conductance is voltage dependent and anion selective (GVD) whilst the other is voltage independent and cation selective (GVI). 3. Addition of 5 mM L-alanine to the bathing solution increased the whole cell conductance and gave a positive (depolarizing) shift in the reversal potential (Vrev, equivalent to the membrane potential in current-clamped cells) consistent with activation of Na+-alanine cotransport. Vrev shifted from -36 +/- 4.9 to +12.9 +/- 4.2 mV (n = 15). 4. In the presence of alanine, the total whole cell conductance had several components including the cotransporter conductance and GVD and GVI. These conductances were separated using Gd3+, which inhibits both GVD and GVI, and the time dependency of GVD. Of these two volume-sensitive conductances, L-alanine elicited a specific increase in GVD, whereas GVI was unaffected. 5. The L-alanine-induced activation of GVD was significantly reduced when cells were incubated in a hypertonic bathing solution. 6. In summary, in single proximal tubule cells isolated from frog kidney, on stimulation of Na+-alanine cotransport GVD is activated, while GVI is unaffected. Taken with other evidence, this suggests that GVD is activated by cell swelling, consequent upon alanine entry, and may play a role as an anion efflux pathway during alanine-induced volume regulation. (+info)
Identification and characterization of GABA, proline and quaternary ammonium compound transporters from Arabidopsis thaliana. (7/736)Arabidopsis thaliana grows efficiently on GABA as the sole nitrogen source, thereby providing evidence for the existence of GABA transporters in plants. Heterologous complementation of a GABA uptake-deficient yeast mutant identified two previously known plant amino acid transporters, AAP3 and ProT2, as GABA transporters with Michaelis constants of 12.9 +/- 1.7 and 1.7 +/- 0.3 mM at pH 4, respectively. The simultaneous transport of [1-14C]GABA and [2,3-3H]proline by ProT2 as a function of pH, provided evidence that the zwitterionic state of GABA is an important parameter in substrate recognition. ProT2-mediated [1-14C]GABA transport was inhibited by proline and quaternary ammonium compounds. (+info)
Cloning and expression of cadD, a new cadmium resistance gene of Staphylococcus aureus. (8/736)A cadmium resistance gene, designated cadD, has been identified in and cloned from the Staphylococcus aureus plasmid pRW001. The gene is part of a two-component operon which contains the resistance gene cadD and an inactive regulatory gene, cadX*. A high degree of sequence similarity was observed between cadD and the cadB-like gene from S. lugdunensis, but no significant similarity was found with either cadA or cadB from the S. aureus plasmids pI258 and pII147. The positive regulatory gene cadX* is identical to cadX from pLUG10 over a stretch of 78 codons beginning at the N terminus, but it is truncated at this point and inactive. Sequence analysis showed that the cadmium resistance operon resides on a 3,972-bp element that is flanked by direct repeats of IS257. The expression of cadD in S. aureus and Bacillus subtilis resulted in low-level resistance to cadmium; in contrast, cadA and cadB from S. aureus induced higher level resistance. However, when the truncated version of cadX contained in pRW001 is complemented in trans with cadX from plasmid pLUG10, resistance increased approximately 10-fold suggesting that the cadmium resistance operons from pRW001 and pLUG10 are evolutionarily related. Moreover, the truncated version of cadX contained in pRW001 is nonfunctional and may have been generated by deletion during recombination to acquire the cadmium resistance element. (+info)
Cystinuria is caused by mutations in the SLC7A9 gene, which codes for a protein involved in the transport of cystine across the brush border membrane of renal tubular cells. The disorder is inherited in an autosomal recessive pattern, meaning that affected individuals must inherit two copies of the mutated gene (one from each parent) to develop symptoms.
There is no cure for cystinuria, but various treatments can help manage its symptoms. These may include medications to reduce the acidity of the urine and prevent infection, as well as surgical procedures to remove stones or repair damaged kidneys. In some cases, a kidney transplant may be necessary.
It's important for individuals with cystinuria to drink plenty of water and maintain good hydration to help flush out the urinary tract and prevent stone formation. They should also avoid certain foods that may increase the risk of stone formation, such as oxalate-rich foods like spinach and rhubarb.
Overall, while there is no cure for cystinuria, with proper management and care, individuals with this disorder can lead relatively normal lives and minimize the complications associated with it.
Hartnup disease is a rare genetic disorder that affects the body's ability to absorb vitamin B12 (cobalamin) and other nutrients. It is caused by a mutation in the HCN1 gene, which codes for a protein involved in the transport of cobalamin into the cells.
Symptoms of Hartnup Disease:
The symptoms of Hartnup disease can vary in severity and may include:
* Pale skin
* Shortness of breath
* Numbness or tingling in the hands and feet
* Poor appetite
Complications of Hartnup Disease:
If left untreated, Hartnup disease can lead to complications such as:
* Anemia (low red blood cell count)
* Nerve damage
* Skin problems
* Eye problems
* Hearing loss
* Increased risk of infections
Treatment of Hartnup Disease:
The treatment of Hartnup disease typically involves a combination of dietary changes and supplements. Patients with the condition may need to follow a strict diet that includes foods high in vitamin B12, such as meat, fish, and dairy products. They may also need to take supplements to ensure they are getting enough of this important nutrient. In some cases, medication may be prescribed to help manage symptoms.
Prognosis of Hartnup Disease:
The prognosis for Hartnup disease is generally good if the condition is diagnosed and treated early. With proper management, most patients with Hartnup disease can lead active and healthy lives. However, if left untreated, the condition can have serious complications that can be difficult to reverse.
Inheritance Pattern of Hartnup Disease:
Hartnup disease is an autosomal recessive disorder, which means that a person must inherit two copies of the mutated HCN1 gene (one from each parent) in order to develop the condition. If a person inherits only one copy of the mutated gene, they will be a carrier of the condition but are unlikely to develop symptoms themselves. Carriers of Hartnup disease can pass the mutated gene on to their children, who have a 25% chance of inheriting two copies of the gene and developing the condition.
Prevention of Hartnup Disease:
There is no known prevention for Hartnup disease. However, if a person knows they are a carrier of the condition, they can work with their healthcare provider to ensure they are getting enough vitamin B12 and monitoring their diet to prevent any complications.
In conclusion, Hartnup disease is a rare genetic disorder that affects the absorption of vitamin B12 in the small intestine. It can cause a range of symptoms, including diarrhea, abdominal pain, and fatigue. Treatment typically involves a combination of dietary changes and supplements, and early diagnosis and management can lead to a good prognosis. However, if left untreated, the condition can have serious complications. If you suspect you or someone you know may be experiencing symptoms of Hartnup disease, it is important to speak with a healthcare provider for proper diagnosis and treatment.
Also known as: aminoacyl-tRNA synthetase deficiency, aminoacyl-tRNA synthetase/tRNA synthetase deficiency, and amino acid transporter defects.
The signs and symptoms of CE can vary depending on the location of the tumor, but they may include:
* Lumps or swelling in the neck, underarm, or groin area
* Weight loss
* Night sweats
* Swollen lymph nodes
* Pain in the affected area
CE is caused by a genetic mutation that leads to uncontrolled cell growth and division. The exact cause of the mutation is not fully understood, but it is believed to be linked to exposure to certain viruses or chemicals.
Diagnosis of CE typically involves a combination of physical examination, imaging tests such as CT scans or PET scans, and biopsy to confirm the presence of cancer cells. Treatment options for CE depend on the stage and location of the tumor, but may include:
* Chemotherapy to kill cancer cells
* Radiation therapy to shrink the tumor
* Surgery to remove the tumor
* Immunotherapy to boost the immune system's ability to fight the cancer
Overall, CE is a rare and aggressive form of cancer that requires prompt diagnosis and treatment to improve outcomes.
There are several types of inborn errors of amino acid metabolism, including:
1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.
Examples of experimental liver neoplasms include:
1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and can be induced experimentally by injecting carcinogens such as diethylnitrosamine (DEN) or dimethylbenz(a)anthracene (DMBA) into the liver tissue of animals.
2. Cholangiocarcinoma: This type of cancer originates in the bile ducts within the liver and can be induced experimentally by injecting chemical carcinogens such as DEN or DMBA into the bile ducts of animals.
3. Hepatoblastoma: This is a rare type of liver cancer that primarily affects children and can be induced experimentally by administering chemotherapy drugs to newborn mice or rats.
4. Metastatic tumors: These are tumors that originate in other parts of the body and spread to the liver through the bloodstream or lymphatic system. Experimental models of metastatic tumors can be studied by injecting cancer cells into the liver tissue of animals.
The study of experimental liver neoplasms is important for understanding the underlying mechanisms of liver cancer development and progression, as well as identifying potential therapeutic targets for the treatment of this disease. Animal models can be used to test the efficacy of new drugs or therapies before they are tested in humans, which can help to accelerate the development of new treatments for liver cancer.
Sodium-coupled neutral amino acid transporter 2
Sodium-dependent neutral amino acid transporter B(0)AT1
Neutral amino acid transporter B(0)
Serotonin-norepinephrine reuptake inhibitor
Cationic amino acid transporter 3
4F2 cell-surface antigen heavy chain
List of MeSH codes (D12.776.157)
List of MeSH codes (D12.776.543)
Neutral and basic amino acid transport protein rBAT
Expanded genetic code
Membrane transport protein
B(0,+)-type amino acid transporter 1
Proton coupled amino acid transporter
Brain positron emission tomography
History of the Jews in Poland
Jebsen & Jessen (SEA)
Tetratricopeptide repeat protein 39B
Trimeric autotransporter adhesin
Coal in Turkey
Jin Kim Montclare
High-nutrient, low-chlorophyll regions
Physiological effects in space
ACE2 - from the renin-angiotensin system to gut microbiota and malnutrition
Tian Ge, Ph.D. | Harvard Catalyst Profiles | Harvard Catalyst
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- In addition, ACE2 has functions independent of the RAS: ACE2 is the receptor for the SARS coronavirus and ACE2 is essential for expression of neutral amino acid transporters in the gut. (nih.gov)
- Amino acid transporters found in yeasts, plants and lower organisms. (nih.gov)
- high confidence medium confidence low confidence transporter - transporters and PTS systems are shaded because predicting their specificity is particularly challenging. (lbl.gov)
- Comment: ABC transporters with 5 components: E. coli livFGHMJ and related systems (but the alternate substrate-binding protein livK does not transport valine). (lbl.gov)
- Analysis of IL-7 regulated gene expression revealed that neutral and cationic amino acid transporters were specific transcriptional targets of IL-7 signalling. (ox.ac.uk)
- This gene encodes a protein that belongs to a family of light subunits of amino acid transporters. (nih.gov)
- Torres-Salazar D, Jiang J, Divito CB, Garcia-Olivares J and Amara SG (2015) A Mutation in Transmembrane Domain 7 (TM7) of Excitatory Amino Acid Transporters Disrupts the Substrate-dependent Gating of the Intrinsic Anion Conductance and Drives the Channel into a Constitutively Open State. (nih.gov)
Neutral amino acids3
- One of the functions of the transporter system is to supply large neutral amino acids to the brain. (bvsalud.org)
- In the kidneys, B 0 AT1 reabsorbs neutral amino acids into the bloodstream so they are not released in urine. (medlineplus.gov)
- The reduced B 0 AT1 activity leads to large amounts of neutral amino acids being removed from the body as waste. (medlineplus.gov)
- Cellular proteins and protein complexes that transport amino acids across biological membranes. (nih.gov)
- Twenty alpha-amino acids are the subunits which are polymerized to form proteins. (lookformedical.com)
- Amino acids are the building blocks for proteins in the body. (nih.gov)
- Amino acids and proteins are the building blocks of life. (nih.gov)
- When proteins are digested or broken down, amino acids are the result. (nih.gov)
- To identify useful candidate antigens for such a vaccine, five B. bronchiseptica genes including amino acid ATP-binding cassette transporter substrate-binding protein (ABC), lipoprotein (PL), outer membrane porin protein (PPP), leu/ile/val-binding protein (BPP), and conserved hypothetical protein (CHP) were cloned and the recombinant proteins were expressed. (biomedcentral.com)
- Five proteins including amino acid ATP-binding cassette transporter substrate-binding protein (ABC), lipoprotein (PL), outer membrane porin protein (PPP), leu/ile/val-binding protein (BPP), and conserved hypothetical protein (CHP) were selected as targets on the basis of previous studies. (biomedcentral.com)
- The researchers suggested that MHC class I molecules, which function in the immune system to transport antigenic peptides to the cell surface, might also play a role in receptor recycling. (nih.gov)
- One group of these disorders is amino acid metabolism disorders. (nih.gov)
- Overview of Amino Acid Metabolism Disorders (Merck & Co., Inc. (nih.gov)
- Overview of Amino Acid Metabolism Disorders - Learn about the causes, symptoms, diagnosis & treatment from the Merck Manuals - Medical Consumer Version. (nih.gov)
- Phenylketonuria (PKU) is a type of amino acid metabolism disorder. (nih.gov)
- While glucose metabolism has previously been implicated in the mechanism of IL-7 induced survival and growth, the role of amino acids has not before been reported. (ox.ac.uk)
- Male Wistar rats were implanted with an i.t. catheter for drug injection and some were implanted with an additional microdialysis probe used for CSF dialysate collection and measurement of excitatory amino acids (EAAs). (tmu.edu.tw)
- Amphetamine also modulates extracellular glutamate concentrations and we discovered that the excitatory amino acid transporter EAAT3 is also internalized by amphetamine. (nih.gov)
- Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. (nih.gov)
- Extracellular glutamate concentrations are highly regulated by the members of the Excitatory Amino Acid Transporter (EAAT) family. (nih.gov)
- branched chain amino acid/phenylalanine ABC transporter ATP binding subunit LivF (EC 18.104.22.168). (lbl.gov)
- Since SNO pathway cannot utilize free-diffusion mechanism to get through the membrane as the molecular size is significantly larger than NO molecule, it utilizes amino acid transporter to convey signals as a form of S-nitrosylated cysteine (CysNO). (nih.gov)
- This gene encodes a member of a heteromeric, sodium-independent, anionic amino acid transport system that is highly specific for cysteine and glutamate. (origene.com)
- In this system, designated Xc(-), the anionic form of cysteine is transported in exchange for glutamate. (origene.com)
- It is the precursor to several amino acids including glycine and cysteine, and tryptophan in bacteria. (ecmdb.ca)
- To do that we combine molecular biology, radiolabeled glutamate uptake, cysteine modification experiments and electrophysiological recordings in heterologous expression systems expressing the different members of the EAAT family. (nih.gov)
PURINES and PYRIMIDINES1
- The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. (lookformedical.com)
- Extracellular l-glutamate poses a severe excitotoxic threat to neurons and glia when unregulated, therefore low synaptic levels of this neurotransmitter must be maintained via a rapid and robust transport system. (unthsc.edu)
- Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system b(0,+)-like activity). (nih.gov)
- This protein plays a role in the high-affinity and sodium-independent transport of cystine and neutral and dibasic amino acids, and appears to function in the reabsorption of cystine in the kidney tubule. (nih.gov)
- Mutations in this gene cause non-type I cystinuria, a disease that leads to cystine stones in the urinary system due to impaired transport of cystine and dibasic amino acids. (nih.gov)
- 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. (lookformedical.com)
- By mutational analysis, we found a unique amino acid sequence on EAAT3 that mediates this response. (nih.gov)
- Exogenous amino acids are essential for interleukin-7 induced CD8 T cell growth. (ox.ac.uk)
- 17. Neutral amino acid transport in human synovial cells: substrate specificity of adaptative regulation and transinhibition. (nih.gov)
- Researchers believe that many of these features are related to a deficiency of vitamin B3 (niacin) and one of its main components, the amino acid tryptophan. (medlineplus.gov)
- Diffusible NAD precursor molecules such as nicotinamide and nicotinic acid (vitamin B3) influence cellular NAD levels and NAD biosynthetic pathways are therapeutic targets for human diseases. (uni-marburg.de)
- The related liv system from Acidovorax, Ac3H11_1692:1695 and Ac3H11_2396, has not been shown to transport valine. (lbl.gov)
- high-affinity branched-chain amino acid ABC transporter, ATP-binding protein LivF. (lbl.gov)
- PMID- 669647 TI - System cuts red tape for patients from admission to discharge. (nih.gov)
- The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. (lookformedical.com)
- Our Dual RNA-Seq preliminary work with K. pneumoniae shows on the one hand that macrophages react differently after contact with the pathogen than with apathogenic bacterial stimuli, and on the other hand that the pathogen massively upregulates several transport systems for the absorption of diffusible substances such as heme, sulfates, amino acids, sugars, inositol and cobalamins. (uni-marburg.de)
- 1. Tumor cell invasion of basement membrane in vitro is regulated by amino acids. (nih.gov)
- Although numerous neurotoxicity studies have been conducted with L-BMAA in mice, rats, chickens, primates, and humans in vivo and several systems in vitro , studies to evaluate other toxicological endpoints, including reproductive, genotoxicity, and carcinogenicity effects are lacking. (nih.gov)
- Although numerous neurotoxicity studies have been conducted with L-BMAA in mice, rats, chickens, primates, and humans in vivo and in several systems in vitro , studies of other toxicological effects, including reproductive, developmental, and genotoxic, are lacking. (nih.gov)
- Plasma amino acids is a screening test, usually done on infants that looks at the amounts of amino acids in the blood. (nih.gov)
- 19. Electrophysiological investigation of the amino acid carrier selectivity in epithelial cells from Xenopus embryo. (nih.gov)
- Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. (lookformedical.com)
- Studies in rats showed that L-BMAA is rapidly taken up by central nervous system tissues and is eliminated at a much slower rate. (nih.gov)
- Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. (lookformedical.com)
- Dairy adaptations in CJ18 are reflected by a high percentage of pseudogenes (4.9%) representing genome decay which includes the inactivation of the lactose phosphotransferase system ( lacIIABC ) by multiple transposases integration. (biomedcentral.com)
- PTS system, Phosphotransferase system [Interproscan]. (ntu.edu.sg)
- PTS HPr component phosphorylation site, Phosphoenolpyruvate-dependent sugar phosphotransferase system [Interproscan]. (ntu.edu.sg)
- this protein complex absorbs particular protein building blocks ( amino acids ) back into the blood. (nih.gov)
- Their mechanism of action includes binding to the alpha-2/delta-1 subunit of the voltage-gated calcium channels in several areas of the central nervous system (CNS) and spinal cord in which these channels are expressed. (slideshare.net)
- infantarius ( Sii ) is a lactic acid bacterium (LAB) commonly associated with the gastrointestinal tract of animals and humans [ 1 ]. (biomedcentral.com)
- However, the molecular targets of hyaluronan to regulate synaptic transmission in the central nervous system have not been fully identified. (elsevier.com)
- 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. (lookformedical.com)
- Antidepressants may have additional mechanisms of action by modulating the immune system, which is heavily involved in neuropathic pain. (slideshare.net)
- 2. Amino acid transport systems modulate human tumor cell growth and invasion: a working hypothesis. (nih.gov)
- In our laboratory, we aim to elucidate the structural components controlling anion channel permeation trough EAATs, as well as the structural coupling between the two transport mechanisms. (nih.gov)
- Related systems include livJFGHM from Streptococcus pneumoniae, braCDEFG from Pseudomonas aeruginosa (braC is the SBP), and braCDEFG or braC3/braDEFG from R. leguminosarum. (lbl.gov)
- Thus, multiplexed combination of these steps and the regulatory factors involved in this system conform and modify the outcome from stimulus-response coupling via the SNO pathway. (nih.gov)
- L --Methylaminoalanine (L-BMAA) is a neurotoxic non-protein amino acid that is produced by cyanobacteria, a blue-green algae that is common to many lakes, oceans, and soils, and is found in Cycas circinalis seeds. (nih.gov)
- L --Methylaminoalanine (L-BMAA) is a neurotoxic non-protein amino acid produced naturally by cyanobacteria found in freshwater, marine and terrestrial ecosystems. (nih.gov)
- Serine and derivatives are compounds containing serine or a derivative thereof resulting from reaction of serine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. (ecmdb.ca)