Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
A family of neurotransmitter transporter proteins that facilitate NEUROTRANSMITTER reuptake into PRESYNAPTIC TERMINALS. They may play a role in regulating the intensity and duration of neurotransmission.
Nonmotile unicellular green algae potentially valuable as a source of high-grade protein and B-complex vitamins.
Proteins that cotransport hydrogen ions and phosphate ions across cellular membranes.
A family of symporters that facilitate sodium-dependent membrane transport of phosphate.
The founding member of the sodium glucose transport proteins. It is predominately expressed in the INTESTINAL MUCOSA of the SMALL INTESTINE.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.
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.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.
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.
An essential branched-chain amino acid important for hemoglobin formation.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
A subclass of symporters found in KIDNEY TUBULES, DISTAL that are the major pathway for salt resorption. Inhibition of these symporters by BENZOTHIADIAZINES is the basis of action of some DIURETICS.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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).
Proteins found in any species of bacterium.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Proteins that cotransport sodium ions and bicarbonate ions across cellular membranes.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The rate dynamics in chemical or physical systems.
A subclass of symporters that specifically transport SODIUM CHLORIDE and/or POTASSIUM CHLORIDE across cellular membranes in a tightly coupled process.

The paired-domain transcription factor Pax8 binds to the upstream enhancer of the rat sodium/iodide symporter gene and participates in both thyroid-specific and cyclic-AMP-dependent transcription. (1/2800)

The gene encoding the Na/I symporter (NIS) is expressed at high levels only in thyroid follicular cells, where its expression is regulated by the thyroid-stimulating hormone via the second messenger, cyclic AMP (cAMP). In this study, we demonstrate the presence of an enhancer that is located between nucleotides -2264 and -2495 in the 5'-flanking region of the NIS gene and that recapitulates the most relevant aspects of NIS regulation. When fused to either its own or a heterologous promoter, the NIS upstream enhancer, which we call NUE, stimulates transcription in a thyroid-specific and cAMP-dependent manner. The activity of NUE depends on the four most relevant sites, identified by mutational analysis. The thyroid-specific transcription factor Pax8 binds at two of these sites. Mutations that interfere with Pax8 binding also decrease transcriptional activity of the NUE. Furthermore, expression of Pax8 in nonthyroid cells results in transcriptional activation of NUE, strongly suggesting that the paired-domain protein Pax8 plays an important role in NUE activity. The NUE responds to cAMP in both protein kinase A-dependent and -independent manners, indicating that this enhancer could represent a novel type of cAMP responsive element. Such a cAMP response requires Pax8 but also depends on the integrity of a cAMP responsive element (CRE)-like sequence, thus suggesting a functional interaction between Pax8 and factors binding at the CRE-like site.  (+info)

Tyrosine kinase inhibitors and immunosuppressants perturb the myo-inositol but not the betaine cotransporter in isotonic and hypertonic MDCK cells. (2/2800)

BACKGROUND: The sodium/myo-inositol cotransporter (SMIT) and the betaine cotransporter (BGT1) are essential for the accumulation of myo-inositol and betaine, and hence cell survival in a hypertonic environment. The underlying molecular mechanism involves an increase in transcription of the SMIT and BGT1 genes through binding of a trans-acting factor to enhancer elements in the 5' flanking region of both genes, resulting in increased mRNA abundance and increased activity of the cotransporters. Current evidence regarding transcriptional and post-transcriptional regulation indicates that both cotransporters are regulated in parallel. METHODS: To investigate the signal transduction of hypertonic stress, we examined the effect of tyrosine kinase inhibitors and immunosuppressants on the hypertonicity-induced activity of the two cotransporters in Madin-Darby canine kidney (MDCK) cells. RESULTS: None of the agents studied affected BGT1 activity in isotonic or hypertonic conditions. Treatment of MDCK cells with genistein, a tyrosine kinase inhibitor, increased SMIT activity in hypertonic but not isotonic conditions. The stimulation of SMIT by genistein was accompanied by a parallel increase in mRNA abundance. In contrast, treating cells with tyrphostin A23, another tyrosine kinase inhibitor, or cyclosporine A, an immunosuppressant, inhibited SMIT activity in hypertonic cells. FK506, another immunosuppressant, increased SMIT activity, but only in isotonic conditions. CONCLUSIONS: These results provide the first evidence of divergent regulatory pathways modulating SMIT and BGT activity.  (+info)

Effects of phosphate intake on distribution of type II Na/Pi cotransporter mRNA in rat kidney. (3/2800)

BACKGROUND: Renal phosphate (Pi) reabsorption is regulated by dietary Pi intake, as well as in other ways. Changes in Pi reabsorption are associated with the modulation of sodium/Pi cotransporter type II (NaPi-2) protein abundance in the brush border membrane (BBM) of proximal tubules (PTs) and of renal NaPi-2 mRNA levels. In this study, we address whether the NaPi-2 protein and NaPi-2 mRNA distribution patterns in the renal cortex vary in parallel with changes of dietary Pi intake. METHODS: We investigated in cryosections of perfusion-fixed rat kidneys by in situ hybridization (ISH) and immunohistochemistry (IHC) the distribution patterns of NaPi-2 mRNA and of NaPi-2 protein one week, two hours, and four hours after changes in dietary Pi intake. RESULTS: NaPi-2 mRNA and NaPi-2 protein were present in PTs exclusively. In rats adapted to one week of high Pi intake, signals for NaPi-2 mRNA and NaPi-2 protein in cortical PTs were weak, except in the convoluted parts of PTs of juxtamedullary nephrons. After one week of low Pi intake, the ISH and IHC signals for NaPi-2 were high in PT segments in all cortical levels. The switch from a chronic high to a low Pi intake within two and four hours induced no increase and a slight increase, respectively, in the NaPi-2 mRNA signal in PTs of midcortical and of superficial nephrons, whereas in the BBM of these nephrons, NaPi-2 protein was markedly up-regulated. Two and four hours after switching from low to high Pi intake, the overall high ISH signal for NaPi-2 mRNA was unchanged, whereas NaPi-2 protein staining was drastically down-regulated in the BBM of PTs from superficial and midcortical nephrons. CONCLUSIONS: The marked changes in NaPi-2 protein abundance in the BBM, following altered dietary Pi intake, precede corresponding changes at the RNA level by several hours. Thus, the early adaptation to altered Pi intake involves mRNA-independent mechanisms. The up- or down-regulation of NaPi-2 protein abundance in the BBM and NaPi-2 mRNA in PT affects mainly midcortical and superficial nephrons.  (+info)

A previously undescribed intron and extensive 5' upstream sequence, but not Phox2a-mediated transactivation, are necessary for high level cell type-specific expression of the human norepinephrine transporter gene. (4/2800)

The synaptic action of norepinephrine is terminated by NaCl-dependent uptake into presynaptic noradrenergic nerve endings, mediated by the norepinephrine transporter (NET). NET is expressed only in neuronal tissues that synthesize and secrete norepinephrine and in most cases is co-expressed with the norepinephrine-synthetic enzyme dopamine beta-hydroxylase (DBH). To understand the molecular mechanisms regulating human NET (hNET) gene expression, we isolated and characterized an hNET genomic clone encompassing approximately 9. 5 kilobase pairs of the 5' upstream promoter region. Here we demonstrate that the hNET gene contains an as-yet-unidentified intron of 476 base pairs within the 5'-untranslated region. Furthermore, both primer extension and 5'-rapid amplification of cDNA ends analyses identified multiple transcription start sites from mRNAs expressed only in NET-expressing cell lines. The start sites clustered in two subdomains, each preceded by a TATA-like sequence motif. As expected for mature mRNAs, transcripts from most of these sites each contained an additional G residue at the 5' position. Together, the data strongly support the authenticity of these sites as the transcriptional start sites of hNET. We assembled hNET-chloramphenicol acetyltransferase reporter constructs containing different lengths of hNET 5' sequence in the presence or the absence of the first intron. Transient transfection assays indicated that the combination of the 5' upstream sequence and the first intron supported the highest level of noradrenergic cell-specific transcription. Forced expression of the paired-like homeodomain transcription factor Phox2a did not affect hNET promoter activity in NET-negative cell lines, in marked contrast to its effect on a DBH-chloramphenicol acetyltransferase reporter construct. Together with our previous studies suggesting a critical role of Phox2a for noradrenergic-specific expression of the DBH gene, these data support a model in which distinct, or partially distinct, molecular mechanisms regulate cell-specific expression of the NET and DBH genes.  (+info)

Regulation of PiT-1, a sodium-dependent phosphate co-transporter in rat parathyroid glands. (5/2800)

A cDNA encoding an Na+-Pi co-transporter, termed rat PiT-1, has now been isolated from rat parathyroid. Expression of rat PiT-1 in Xenopus oocytes revealed that it possesses Na+-dependent Pi co-transport activity. The amount of PiT-1 mRNA in the parathyroid of vitamin D-deficient rats was reduced compared with that in normal animals, and increased markedly after administration of 1,25-dihydroxyvitamin D3. Furthermore, the abundance of PiT-1 mRNA in the parathyroid was much greater in rats fed a low-Pi diet than in those fed a high-Pi diet. Thus, rat PiT-1 may contribute to the effects of Pi and vitamin D on parathyroid function.  (+info)

Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12. (6/2800)

ProP is an osmoregulatory compatible solute transporter in Escherichia coli K-12. Mutation proQ220::Tn5 decreased the rate constant for and the extent of ProP activation by an osmotic upshift but did not alter proP transcription or the ProP protein level. Allele proQ220::Tn5 was isolated, and the proQ sequence was determined. Locus proQ is upstream from prc (tsp) at 41.2 centisomes on the genetic map. The proQ220::Tn5 and prc phenotypes were different, however. Gene proQ is predicted to encode a 232-amino-acid, basic, hydrophilic protein (molecular mass, 25,876 Da; calculated isoelectric point, 9.66; 32% D, E, R, or K; 54.5% polar amino acids). The insertion of PCR-amplified proQ into vector pBAD24 produced a plasmid containing the wild-type proQ open reading frame, the expression of which yielded a soluble protein with an apparent molecular mass of 30 kDa. Antibodies raised against the overexpressed ProQ protein detected cross-reactive material in proQ+ bacteria but not in proQ220::Tn5 bacteria. ProQ may be a structural element that influences the osmotic activation of ProP at a posttranslational level.  (+info)

Genetic selection of mutations in the high affinity K+ transporter HKT1 that define functions of a loop site for reduced Na+ permeability and increased Na+ tolerance. (7/2800)

Potassium is an important macronutrient required for plant growth, whereas sodium (Na+) can be toxic at high concentrations. The wheat K+ uptake transporter HKT1 has been shown to function in yeast and oocytes as a high affinity K+-Na+ cotransporter, and as a low affinity Na+ transporter at high external Na+. A previous study showed that point mutations in HKT1, which confer enhancement of Na+ tolerance to yeast, can be isolated by genetic selection. Here we report on the isolation of mutations in new domains of HKT1 showing further large increases in Na+ tolerance. By selection in a Na+ ATPase deletion mutant of yeast that shows a high Na+ sensitivity, new HKT1 mutants at positions Gln-270 and Asn-365 were isolated. Several independent mutations were isolated at the Asn-365 site. N365S dramatically increased Na+ tolerance in yeast compared with all other HKT1 mutants. Cation uptake experiments in yeast and biophysical characterization in Xenopus oocytes showed that the mechanisms underlying the Na+ tolerance conferred by the N365S mutant were: reduced inhibition of high affinity Rb+ (K+) uptake at high Na+ concentrations, reduced low affinity Na+ uptake, and reduced Na+ to K+ content ratios in yeast. In addition, the N365S mutant could be clearly distinguished from less Na+-tolerant HKT1 mutants by a markedly decreased relative permeability for Na+ at high Na+ concentrations. The new mutations contribute to the identification of new functional domains and an amino acid in a loop domain that is involved in cation specificity of a plant high affinity K+ transporter and will be valuable for molecular analyses of Na+ transport mechanisms and stress in plants.  (+info)

Up-regulation of the Pit-2 phosphate transporter/retrovirus receptor by protein kinase C epsilon. (8/2800)

The membrane receptors for the gibbon ape leukemia retrovirus and the amphotropic murine retrovirus serve normal cellular functions as sodium-dependent phosphate transporters (Pit-1 and Pit-2, respectively). Our earlier studies established that activation of protein kinase C (PKC) by treatment of cells with phorbol 12-myristate 13-acetate (PMA) enhanced sodium-dependent phosphate (Na/Pi) uptake. Studies now have been carried out to determine which type of Na/Pi transporter (Pit-1 or Pit-2) is regulated by PKC and which PKC isotypes are involved in the up-regulation of Na/Pi uptake by the Na/Pi transporter/viral receptor. It was found that the activation of short term (2-min) Na/Pi uptake by PMA is abolished when cells are infected with amphotropic murine retrovirus (binds Pit-2 receptor) but not with gibbon ape leukemia retrovirus (binds Pit-1 receptor), indicating that Pit-2 is the form of Na/Pi transporter/viral receptor regulated by PKC. The PKC-mediated activation of Pit-2 was blocked by pretreating cells with the pan-PKC inhibitor bisindolylmaleimide but not with the conventional PKC isotype inhibitor Go 6976, suggesting that a novel PKC isotype is required to regulate Pit-2. Overexpression of PKCepsilon, but not of PKCalpha, -delta, or -zeta, was found to mimic the activation of Na/Pi uptake. To further establish that PKCepsilon is involved in the regulation of Pit-2, cells were treated with PKCepsilon-selective antisense oligonucleotides. Treatment with PKCepsilon antisense oligonucleotides decreased the PMA-induced activation of Na/Pi uptake. These results indicate that PMA-induced stimulation of Na/Pi uptake by Pit-2 is specifically mediated through activation of PKCepsilon.  (+info)

A symporter is a type of transmembrane protein that functions to transport two or more molecules or ions across a biological membrane in the same direction, simultaneously. This process is called co-transport and it is driven by the concentration gradient of one of the substrates, which is usually an ion such as sodium (Na+) or proton (H+).

Symporters are classified based on the type of energy that drives the transport process. Primary active transporters, such as symporters, use the energy from ATP hydrolysis or from the electrochemical gradient of ions to move substrates against their concentration gradient. In contrast, secondary active transporters use the energy stored in an existing electrochemical gradient of one substrate to drive the transport of another substrate against its own concentration gradient.

Symporters play important roles in various physiological processes, including nutrient uptake, neurotransmitter reuptake, and ion homeostasis. For example, the sodium-glucose transporter (SGLT) is a symporter that co-transports glucose and sodium ions across the intestinal epithelium and the renal proximal tubule, contributing to glucose absorption and regulation of blood glucose levels. Similarly, the dopamine transporter (DAT) is a symporter that co-transports dopamine and sodium ions back into presynaptic neurons, terminating the action of dopamine in the synapse.

Plasma membrane neurotransmitter transport proteins are a type of transmembrane protein found in the plasma membrane of neurons and other cells. They are responsible for the active transport of neurotransmitters, which are chemical messengers that transmit signals between neurons, from the extracellular space into the cell. This process helps to terminate the signal transmission and regulate the concentration of neurotransmitters in the synaptic cleft, which is the narrow gap between the presynaptic and postsynaptic neurons.

There are two main types of plasma membrane neurotransmitter transport proteins: sodium-dependent transporters and sodium-independent transporters. Sodium-dependent transporters use the energy generated by the movement of sodium ions across the membrane to move neurotransmitters against their concentration gradient, while sodium-independent transporters do not require sodium ions and use other sources of energy.

These transport proteins play a crucial role in maintaining the homeostasis of neurotransmitter levels in the brain and are targets for many drugs used to treat neurological and psychiatric disorders, such as antidepressants, antipsychotics, and stimulants.

Chlorella is a type of single-celled, green freshwater microalgae that is rich in nutrients, including proteins, vitamins, minerals, and chlorophyll. It is often marketed as a dietary supplement or health food because of its high nutritional content. Chlorella contains all the essential amino acids, making it a complete protein source, and is also rich in antioxidants, such as vitamin C, beta-carotene, and various phytochemicals.

Chlorella has been studied for its potential health benefits, including its ability to support immune function, detoxify heavy metals from the body, improve digestion, and reduce chronic inflammation. However, more research is needed to confirm these potential benefits and determine safe and effective dosages. It's important to note that chlorella supplements are not regulated by the FDA, so it's crucial to choose reputable brands and consult with a healthcare provider before taking any new supplements.

Proton-phosphate symporters are a type of transport protein that facilitate the movement of phosphate ions (PO4−3) into cells in exchange for protons (H+). This means that they co-transport both protons and phosphate ions in the same direction, usually into the cell. The energy needed for this transport is derived from the concentration gradient of the protons, which moves down its electrochemical gradient and drives the uptake of phosphate ions against their own concentration gradient. These transporters play important roles in various physiological processes, including nutrient uptake, pH regulation, and signal transduction.

Sodium-phosphate cotransporter proteins are membrane transport proteins that facilitate the active transport of sodium and inorganic phosphate ions across biological membranes. These proteins play a crucial role in maintaining phosphate homeostasis within the body by regulating the absorption and excretion of phosphate in the kidneys and intestines. They exist in two major types, type I (NaPi-I) and type II (NaPi-II), each having multiple subtypes with distinct tissue distributions and regulatory mechanisms.

Type I sodium-phosphate cotransporters are primarily expressed in the kidney's proximal tubules and play a significant role in reabsorbing phosphate from the primary urine back into the bloodstream. Type II sodium-phosphate cotransporters, on the other hand, are found in both the kidneys and intestines. In the kidneys, they contribute to phosphate reabsorption, while in the intestines, they facilitate phosphate absorption from food.

These proteins function by coupling the passive downhill movement of sodium ions (driven by the electrochemical gradient) with the active uphill transport of phosphate ions against their concentration gradient. This coupled transport process enables cells to maintain intracellular phosphate concentrations within a narrow range, despite fluctuations in dietary intake and renal function.

Dysregulation of sodium-phosphate cotransporter proteins has been implicated in various pathological conditions, such as chronic kidney disease (CKD), tumoral calcinosis, and certain genetic disorders affecting phosphate homeostasis.

Sodium-Glucose Transporter 1 (SGLT1) is a protein found in the membrane of intestinal and kidney cells. It is responsible for the active transport of glucose and sodium ions from the lumen into the epithelial cells. In the intestine, SGLT1 plays a crucial role in glucose absorption after meals, while in the kidneys, it helps reabsorb glucose back into the bloodstream to prevent wasting through urine. The transport process is driven by the sodium gradient created by Na+/K+ ATPase, which actively pumps sodium ions out of the cell. SGLT1 inhibitors are used in the treatment of type 2 diabetes to reduce glucose reabsorption and enhance urinary glucose excretion, leading to better glycemic control.

Amino acid transport systems refer to the various membrane transport proteins that are responsible for the active or passive translocation of amino acids across cell membranes in the body. These transport systems play a crucial role in maintaining amino acid homeostasis within cells and regulating their availability for protein synthesis, neurotransmission, and other physiological processes.

There are several distinct amino acid transport systems, each with its own specificity for particular types of amino acids or related molecules. These systems can be classified based on their energy requirements, substrate specificity, and membrane localization. Some of the major amino acid transport systems include:

1. System A - This is a sodium-dependent transport system that primarily transports small, neutral amino acids such as alanine, serine, and proline. It has several subtypes (ASC, A, and AN) with different substrate affinities and kinetic properties.
2. System L - This is a sodium-independent transport system that transports large, neutral amino acids such as leucine, isoleucine, valine, phenylalanine, and tryptophan. It has several subtypes (L1, L2, and y+L) with different substrate specificities and transport mechanisms.
3. System B0 - This is a sodium-dependent transport system that transports both neutral and basic amino acids such as arginine, lysine, and ornithine. It has several subtypes (B0,+, B0-, and b0,+) with different substrate affinities and kinetic properties.
4. System y+ - This is a sodium-independent transport system that transports primarily basic amino acids such as arginine, lysine, and ornithine. It has several subtypes (y+L, y+, b0,+) with different substrate specificities and transport mechanisms.
5. System X-AG - This is a sodium-independent antiporter system that exchanges glutamate and aspartate for neutral amino acids such as cystine, serine, and threonine. It plays an essential role in maintaining redox homeostasis by regulating the intracellular levels of cysteine, a precursor of glutathione.

These transport systems are critical for maintaining cellular homeostasis and regulating various physiological processes such as protein synthesis, neurotransmission, and immune function. Dysregulation of these transport systems has been implicated in several diseases, including cancer, neurological disorders, and cardiovascular disease. Therefore, understanding the molecular mechanisms underlying these transport systems is essential for developing novel therapeutic strategies to treat these conditions.

Sodium is an essential mineral and electrolyte that is necessary for human health. In a medical context, sodium is often discussed in terms of its concentration in the blood, as measured by serum sodium levels. The normal range for serum sodium is typically between 135 and 145 milliequivalents per liter (mEq/L).

Sodium plays a number of important roles in the body, including:

* Regulating fluid balance: Sodium helps to regulate the amount of water in and around your cells, which is important for maintaining normal blood pressure and preventing dehydration.
* Facilitating nerve impulse transmission: Sodium is involved in the generation and transmission of electrical signals in the nervous system, which is necessary for proper muscle function and coordination.
* Assisting with muscle contraction: Sodium helps to regulate muscle contractions by interacting with other minerals such as calcium and potassium.

Low sodium levels (hyponatremia) can cause symptoms such as confusion, seizures, and coma, while high sodium levels (hypernatremia) can lead to symptoms such as weakness, muscle cramps, and seizures. Both conditions require medical treatment to correct.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.

Monosaccharide transport proteins are a type of membrane transport protein that facilitate the passive or active transport of monosaccharides, such as glucose, fructose, and galactose, across cell membranes. These proteins play a crucial role in the absorption, distribution, and metabolism of carbohydrates in the body.

There are two main types of monosaccharide transport proteins: facilitated diffusion transporters and active transporters. Facilitated diffusion transporters, also known as glucose transporters (GLUTs), passively transport monosaccharides down their concentration gradient without the need for energy. In contrast, active transporters, such as the sodium-glucose cotransporter (SGLT), use energy in the form of ATP to actively transport monosaccharides against their concentration gradient.

Monosaccharide transport proteins are found in various tissues throughout the body, including the intestines, kidneys, liver, and brain. They play a critical role in maintaining glucose homeostasis by regulating the uptake and release of glucose into and out of cells. Dysfunction of these transporters has been implicated in several diseases, such as diabetes, cancer, and neurological disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.

Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Sodium chloride symporters are membrane transport proteins that actively co-transport sodium and chloride ions into a cell. They are also known as sodium-chloride cotransporters or NCCs. These transporters play a crucial role in regulating the electrolyte balance and water homeostasis in various tissues, particularly in the kidney's distal convoluted tubule.

The primary function of sodium chloride symporters is to reabsorb sodium and chloride ions from the filtrate in the nephron back into the bloodstream. By doing so, they help maintain the body's sodium concentration and control water balance through osmosis.

Mutations in the gene encoding for the NCC can lead to various kidney disorders, such as Gitelman syndrome or Bartter syndrome type III, which are characterized by electrolyte imbalances, low blood pressure, and metabolic alkalosis.

"Xenopus laevis" is not a medical term itself, but it refers to a specific species of African clawed frog that is often used in scientific research, including biomedical and developmental studies. Therefore, its relevance to medicine comes from its role as a model organism in laboratories.

In a broader sense, Xenopus laevis has contributed significantly to various medical discoveries, such as the understanding of embryonic development, cell cycle regulation, and genetic research. For instance, the Nobel Prize in Physiology or Medicine was awarded in 1963 to John R. B. Gurdon and Sir Michael J. Bishop for their discoveries concerning the genetic mechanisms of organism development using Xenopus laevis as a model system.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

An oocyte, also known as an egg cell or female gamete, is a large specialized cell found in the ovary of female organisms. It contains half the number of chromosomes as a normal diploid cell, as it is the product of meiotic division. Oocytes are surrounded by follicle cells and are responsible for the production of female offspring upon fertilization with sperm. The term "oocyte" specifically refers to the immature egg cell before it reaches full maturity and is ready for fertilization, at which point it is referred to as an ovum or egg.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Sodium-bicarbonate symporters, also known as sodium bicarbonate co-transporters, are membrane transport proteins that facilitate the movement of both sodium ions (Na+) and bicarbonate ions (HCO3-) across the cell membrane in the same direction. These transporters play a crucial role in maintaining acid-base balance in the body by regulating the concentration of bicarbonate ions, which is an important buffer in the blood and other bodily fluids.

The term "symporter" refers to the fact that these proteins transport two or more different molecules or ions in the same direction across a membrane. In this case, sodium-bicarbonate symporters co-transport one sodium ion and one bicarbonate ion together, usually using a concentration gradient of sodium to drive the uptake of bicarbonate.

These transporters are widely expressed in various tissues, including the kidneys, where they help reabsorb bicarbonate ions from the urine back into the bloodstream, and the gastrointestinal tract, where they contribute to the absorption of sodium and bicarbonate from food and drink. Dysfunction of sodium-bicarbonate symporters has been implicated in several diseases, including renal tubular acidosis and hypertension.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Sodium-Potassium-Chloride Symporters are membrane transport proteins that facilitate the active transport of sodium, potassium, and chloride ions across the cell membrane. These symporters use the energy derived from the concentration gradient of sodium ions to co-transport potassium and chloride ions into or out of the cell. This process helps maintain electrolyte balance, regulate cell volume, and facilitate various physiological functions such as nerve impulse transmission and kidney function. An example of a Sodium-Potassium-Chloride Symporter is the NKCC1 (Na-K-2Cl cotransporter).

In the roots of plants, the H+/K+ symporters are only one member of a group of several symporters/antiporters that specifically ... like H+/K+ symporters allow the specific ions to come into the cell and the out the plasmodesmata/symporters/antiporters of the ... Na+/K+/2Cl− symporter in the loop of Henle in the renal tubules of the kidney transports 4 molecules of 3 different types; a ... A symporter is an integral membrane protein that is involved in the transport of two (or more) different molecules across the ...
H+ symporter of Bacillus subtillus (GntP; TC# 2.A.8.1.1) and the D-fructuronate/D-gluconate:H+ symporter of E. coli (GntP; TC# ... The gluconate:H+ symporter (GntP) family (TC# 2.A.8) is a family of transport proteins belonging to the ion transporter (IT) ... The original text was at "The Gluconate:H+ Symporter (GntP) Family" v t e (Protein pages needing a picture, Articles with ... "2.A.8 The Gluconate:H+ Symporter (GntP) Family". Transporter Classification Database. Retrieved 2016-03-04. Porco A, Peekhaus N ...
One of these families is known as the sodium:dicarboxylate symporter family (SDF) (it is different from divalent anion-sodium ... Reizer J, Reizer A, Saier MH (June 1994). "A functional superfamily of sodium/solute symporters". Biochim. Biophys. Acta. 1197 ... sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. ... symporter). Such re-uptake of neurotransmitters from the synapses, is thought to be an important mechanism for terminating ...
A neurotransmitter sodium symporter (NSS) (TC# 2.A.22) is type of neurotransmitter transporter that catalyzes the uptake of a ... Neurotransmitter sodium symporters (NSS) are targets for anti-depressants, psychostimulants and other drugs. The generalized ... "2.A.22 The Neurotransmitter:Sodium Symporter (NSS) Family". Transporter Classification Database. Attwell D, Bouvier M (1992). " ... 2 Na+ symporter, LeuTAa: 2A65​, 2Q6H​, 2Q72​, 2QB4​, 2QJU​, 3F3A​, 3F3C​, (more) Several characterized proteins are classified ...
Sodium+Chloride+Symporters at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Sodium+Chloride+Symporter+ ... The sodium-chloride symporter accounts for the absorption of 5% of the salt filtered at the glomerulus. NCC activity is known ... The sodium-chloride symporter (also known as Na+-Cl− cotransporter, NCC or NCCT, or as the thiazide-sensitive Na+-Cl− ... The sodium-chloride symporter or NCC is a member of the SLC12 cotransporter family of electroneutral cation-coupled chloride ...
These sodium symporters can be grouped, on the basis of sequence and functional similarities into a number of distinct families ... Sodium sulfate symporters are integral membrane proteins that mediate the intake of a wide variety of molecules with the ... This family also includes a number of bacterial symporters. Markovich D, Forgo J, Stange G, Biber J, Murer H (September 1993 ...
The benzoate:H symporter (BenE) family (TC# 2.A.46) is a member of the APC Superfamily. The BenE family contains only two ... "2.A.46 The Benzoate:H Symporter (BenE) Family". Transporter Classification Database. Saier Lab Bioinformatics Group @ UCSD / ... H Symporter (AAHS) family (TC# 2.A.1.15) of the Major Facilitator Superfamily (MFS). The degree of similarity with the latter ...
The Malonate:Na+ Symporter (MSS) Family (TC# 2.A.70) is a group of transport proteins belonging to the CPA superfamily. These ... As of this edit, this article uses content from "2.A.70 The Malonate:Na+ Symporter (MSS) Family", which is licensed in a way ... "Malonate/sodium symporter MadM subunit, N-terminal (IPR018402) < InterPro < EMBL-EBI". www.ebi.ac.uk. Retrieved 2016-04-06. ... One constituent member of the MSS family, the monobasic malonate:Na+ symporter of Malonomonas rubra, has been functionally and ...
... are classified into: Chloride potassium symporter 4, predominating in the kidney. Chloride ... For example, chloride potassium symporter 5, or KCC2, is expressed through the SLC12A5 gene. Notably, symporters prior to 4 in ... The chloride potassium symporter is a membrane transport protein of the solute carrier family 12 that is present in the S3- ... Chloride potassium symporter can lower intracellular chloride concentrations below the electrochemical equilibrium potential. ...
Sodium/pantothenate symporter InterPro: IPR011849 Sodium/proline symporter InterPro: IPR011851 Cation/acetate symporter ActP ... of Escherichia coli is homologous to the Na+/proline symporter (PutP) of E. coli and the Na+/glucose symporters of mammals". ... Members of the Solute:Sodium Symporter (SSS) Family (TC# 2.A.21) catalyze solute:Na+ symport. The SSS family is within the APC ... The human placental multivitamin symporter co-transports an anionic vitamin with two Na+. In the rabbit Na+:D-glucose co- ...
Potassium-chloride transporter, member 4 is a chloride potassium symporter protein. It is encoded by the gene SLC12A4. Solute ...
This family of proteins are found both in prokaryotes and eukaryotes. In mammals, they are transmembrane proteins with functions in the liver and in the intestine. They are members of the solute carrier family of cotransporter genes which include SLC10A1 and SLC10A2. SLC10A1 encodes the sodium-taurocholate cotransporting polypeptide (NTCP) expressed in the liver and found on the basolateral membranes. It is involved in the uptake of all types of bile acids from portal blood plasma, a process mediated by the co-transport of Na+. It is also capable of transporting other solutes and is necessary for the entry of hepatitis B and hepatitis D viruses into the hepatocyte. SLC10A2 encodes the apical sodium bile acid transporter (ASBT) expressed in the small intestine with highest concentrations in the ileum. It is found on the brush border membrane and is also known as the ileal bile acid transporter (IBAT). It is responsible for the initial uptake of bile acids from the intestine as part of the ...
Both KCC2 isoforms can form homomultimers, or heteromultimers with other K-Cl symporters on the cell membrane to maintain ... Potassium-chloride transporter member 5 (aka: KCC2 and SLC12A5) is a neuron-specific chloride potassium symporter responsible ... symporter that maintains chloride homeostasis in neurons. The electrochemical chloride gradient established by KCC2 activity is ...
The Nucleobase:Cation Symporter-1 (NCS1) Family (TC# 2.A.39) consists of over 1000 currently sequenced proteins derived from ... NCS1 proteins are H+/Na+ symporters specific for the uptake of purines, pyrimidines and related metabolites. Krypotou et al. ... In these respects, and with respect to substrate specificity, these proteins resemble the symporters of the NCS2 family, ... "2.A.39 The Nucleobase:Cation Symporter-1 (NCS1) Family". Transporter Classification Database. Saier Lab Bioinformatics Group / ...
Divalent anion:Na+ symporters were found in bacteria, archaea, plant chloroplasts and animals. They vary in size from 432 amino ... They are all Na+-coupled symporters. The Na+:anion coupling ratio is 3:1, indicative of electrogenic properties. They have a ...
The Nucleobase cation symporter-2 (NCS2) family, also called the Nucleobase ascorbate transporter (NAT) family, consists of ... "2.A.40 The Nucleobase/Ascorbate Transporter (NAT) or Nucleobase:Cation Symporter-2 (NCS2) Family". Transporter Classification ...
H+ symporter of Schizosaccharomyces pombe. This yeast protein is about 24% identical to the plant sucrose:H+ symporters and is ... The generalized transport reaction catalyzed by the GPH:cation symporter family is: Sugar (out) + [H+ or Na+] (out) → Sugar (in ... As of this edit, this article uses content from "2.A.2 The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family", which ... Homologues are from bacteria, including the distantly related sucrose:H+ symporters of plants and a yeast maltose/sucrose: ...
The branched chain amino acid:cation symporter (LIVCS) family (TC# 2.A.26) is a member of the APC superfamily. Characterized ... "2.A.26 The Branched Chain Amino Acid:Cation Symporter (LIVCS) Family". Transporter Classification Database. Braun, Peter R.; Al ... June 29, 1994). "A functional superfamily of sodium/solute symporters.". 1197(2): (2): 133-66. PMID 8031825. Portal: Biology v ...
... or MV-NIS is an attenuated oncolytic Edmonston (Ed) strain ... guided radiovirotherapy for multiple myeloma using a recombinant measles virus expressing the thyroidal sodium iodide symporter ... Imaging and Radiovirotherapy of Prostate Cancer Using an Oncolytic Measles Virus Expressing the Sodium Iodide Symporter". ... Measles Virus Administered With or Without Cyclophosphamide Oncolytic measles virus encoding thyroidal sodium iodide symporter ...
Antiporter Symporter Cammack, Richard; Atwood, Teresa; Campbell, Peter; Parish, Howard; Smith, Anthony; Vella, Frank; Stirling ... Wolfersberger, MG (November 1994). "Uniporters, Symporters and Antiporters". J Exp Biol. 196: 5-6. doi:10.1242/jeb.196.1.5. ...
The SGLT1 protein is a symporter system because it passes both glucose and sodium in the same direction, from the lumen of the ... An example of a symporter mediated transport protein is SGLT1, a sodium/glucose co-transporter protein that is mainly found in ... WOLFERSBERGER, MICHAEL (1994). "Uniporters, symporters and antiporters" (PDF). Journal of Experimental Biology. 196: 5-6. doi: ...
Both Indy proteins are sodium sulfate symporters. Its name originates from a well-known comic line in Monty Python and the Holy ...
This symporter is located in the small intestines, heart, and brain. It is also located in the S3 segment of the proximal ... A symporter uses the downhill movement of one solute species from high to low concentration to move another molecule uphill ... In a symporter, two substrates are transported in the same direction across the membrane. Antiport and symport processes are ... An example is the glucose symporter SGLT1, which co-transports one glucose (or galactose) molecule into the cell for every two ...
2.A: Porters (uniporters, symporters, antiporters), SLCs. Excitatory amino acid transporters (EAATs) EAAT1 EAAT2 EAAT3 EAAT4 ...
Na+/I− symporter (NIS) - Sodium-Iodide is a type of symporter that is responsible for transferring iodide in the thyroid gland ... K+Cl− Symporter - The K+-Cl− cotransporter family consists of four specific symporters known as KCC1, KCC2, KCC3, and KCC4. The ... Antiporters and symporters both transport two or more different types of molecules at the same time in a coupled movement. An ... Na-K-2Cl symporter - This specific cotransporter regulates the cell volume by controlling the water and electrolyte content ...
Sodium Symporters (NSS). One of these proteins, LeuT, from Aquifex aeolicus, was crystallized by Yamashita et al. with very ... sodium symporters". Nature Structural & Molecular Biology. 17 (7): 822-9. doi:10.1038/nsmb.1854. PMC 3245867. PMID 20562855. ... sodium symporters". Nature. 449 (7163): 726-30. Bibcode:2007Natur.449..726Z. doi:10.1038/nature06133. PMID 17704762. S2CID ...
"Sodium-dependent lysophosphatidylcholine symporter 1". UniProt. Retrieved 2 April 2016. Ben-Zvi A, Lacoste B, Kur E, Andreone ... also known as sodium-dependent lysophosphatidylcholine symporter 1 -- is a protein that in humans is encoded by the MFSD2A gene ...
"Sodium-dependent lysophosphatidylcholine symporter 1". UniProt. Archived from the original on 22 April 2019. Retrieved 2 April ...
Both SLC25A22 and SLC25A18 are mitochondrial glutamate/H+ symporters. Mutations in the SLC25A22 gene cause early infantile ...
Na+ Symporter (PNaS) Family 2.A.82 - The Organic Solute Transporter (OST) Family 2.A.102 - The 4-Toluene Sulfonate Uptake ... Na+ symporters (PNaS); TC# 2.A.58) and (9) lysosomal cystine transporters (LCT); TC# 2.A.43). Currently recognized families ...

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