Vesicular Neurotransmitter Transport Proteins
Neurotransmitter Transport Proteins
Plasma Membrane Neurotransmitter Transport Proteins
Neurotransmitter Agents
Membrane Transport Proteins
Fatty Acid Transport Proteins
Biological Transport
Biological Transport, Active
Carrier Proteins
Monosaccharide Transport Proteins
Cation Transport Proteins
Ion Transport
Anion Transport Proteins
Protein Transport
Na+ - and Cl- -coupled active transport of nitric oxide synthase inhibitors via amino acid transport system B(0,+). (1/35)
Nitric oxide synthase (NOS) inhibitors have therapeutic potential in the management of numerous conditions in which NO overproduction plays a critical role. Identification of transport systems in the intestine that can mediate the uptake of NOS inhibitors is important to assess the oral bioavailability and therapeutic efficacy of these potential drugs. Here, we have cloned the Na+ - and Cl- -coupled amino acid transport system B(0,+) (ATB(0,+)) from the mouse colon and investigated its ability to transport NOS inhibitors. When expressed in mammalian cells, ATB(0,+) can transport a variety of zwitterionic and cationic amino acids in a Na+ - and Cl- -coupled manner. Each of the NOS inhibitors tested compete with glycine for uptake through this transport system. Furthermore, using a tritiated analog of the NOS inhibitor N(G)-nitro-L-arginine, we showed that Na+ - and Cl- -coupled transport occurs via ATB(0,+). We then studied transport of a wide variety of NOS inhibitors in Xenopus laevis oocytes expressing the cloned ATB(0,+) and found that ATB(0,+) can transport a broad range of zwitterionic or cationic NOS inhibitors. These data represent the first identification of an ion gradient-driven transport system for NOS inhibitors in the intestinal tract. (+info)Neurotransmitter transporters and their impact on the development of psychopharmacology. (2/35)
The synaptic actions of most neurotransmitters are inactivated by reuptake into the nerve terminals from which they are released, or by uptake into adjacent cells. A family of more than 20 transporter proteins is involved. In addition to the plasma membrane transporters, vesicular transporters in the membranes of neurotransmitter storage vesicles are responsible for maintaining vesicle stores and facilitating exocytotic neurotransmitter release. The cell membrane monoamine transporters are important targets for CNS drugs. The transporters for noradrenaline and serotonin are key targets for antidepressant drugs. Both noradrenaline-selective and serotonin-selective reuptake inhibitors are effective against major depression and a range of other psychiatric illnesses. As the newer drugs are safer in overdose than the first-generation tricyclic antidepressants, their use has greatly expanded. The dopamine transporter (DAT) is a key target for amphetamine and methylphenidate, used in the treatment of attention deficit hyperactivity disorder. Psychostimulant drugs of abuse (amphetamines and cocaine) also target DAT. The amino-acid neurotransmitters are inactivated by other families of neurotransmitter transporters, mainly located on astrocytes and other non-neural cells. Although there are many different transporters involved (four for GABA; two for glycine/D-serine; five for L-glutamate), pharmacology is less well developed in this area. So far, only one new amino-acid transporter-related drug has become available: the GABA uptake inhibitor tiagabine as a novel antiepileptic agent. (+info)Experimental colitis: decreased Octn2 and Atb0+ expression in rat colonocytes induces carnitine depletion that is reversible by carnitine-loaded liposomes. (3/35)
Carnitine transporters have recently been implicated in susceptibility to inflammatory bowel disease (IBD). Because carnitine is required for beta-oxidation, it was suggested that decreased carnitine transporters, and hence reduced carnitine uptake, could lead to impaired fatty acid oxidation in intestinal epithelial cells, and to cell injury. We investigated this issue by examining the expression of the carnitine transporters OCTN2 and ATB0+, and butyrate metabolism in colonocytes in a rat model of IBD induced by trinitrobenzene sulfonic acid (TNBS). We found that Octn2 and Atb0+ expression was decreased in inflammatory samples at translational and functional level. Butyrate oxidation, evaluated based on CO2 production and acetyl-coenzyme A synthesis, was deranged in colonocytes from TNBS-treated rats. Treatment with carnitine-loaded liposomes corrected the butyrate metabolic alterations in vitro and reduced the severity of colitis in vivo. These results suggest that carnitine depletion in colonocytes is associated with the inability of mitochondria to maintain normal butyrate beta-oxidation. Our data indicate that carnitine is a rate-limiting factor for the maintenance of physiological butyrate oxidation in colonic cells. This hypothesis could also explain the contradictory therapeutic efficacy of butyrate supplementation observed in clinical trials of IBD. (+info)Ancestry of neuronal monoamine transporters in the Metazoa. (4/35)
Selective Na(+)-dependent re-uptake of biogenic monoamines at mammalian nerve synapses is accomplished by three types of solute-linked carrier family 6 (SLC6) membrane transporter with high affinity for serotonin (SERTs), dopamine (DATs) and norepinephrine (NETs). An additional SLC6 monoamine transporter (OAT), is responsible for the selective uptake of the phenolamines octopamine and tyramine by insect neurons. We have characterized a similar high-affinity phenoloamine transporter expressed in the CNS of the earthworm Lumbricus terrestris. Phylogenetic analysis of its protein sequence clusters it with both arthropod phenolamine and chordate catecholamine transporters. To clarify the relationships among metazoan monoamine transporters we identified representatives in the major branches of metazoan evolution by polymerase chain reaction (PCR)-amplifying conserved cDNA fragments from isolated nervous tissue and by analyzing available genomic data. Analysis of conserved motifs in the sequence data suggest that the presumed common ancestor of modern-day Bilateria expressed at least three functionally distinct monoamine transporters in its nervous system: a SERT currently found throughout bilaterian phyla, a DAT now restricted in distribution to protostome invertebrates and echinoderms and a third monoamine transporter (MAT), widely represented in contemporary Bilateria, that is selective for catecholamines and/or phenolamines. Chordate DATs, NETs, epinephrine transporters (ETs) and arthropod and annelid OATs all belong to the MAT clade. Contemporary invertebrate and chordate DATs belong to different SLC6 clades. Furthermore, the genes for dopamine and norepinephrine transporters of vertebrates are paralogous, apparently having arisen through duplication of an invertebrate MAT gene after the loss of an invertebrate-type DAT gene in a basal protochordate. (+info)Molecular targets for antiepileptic drug development. (5/35)
This review considers how recent advances in the physiology of ion channels and other potential molecular targets, in conjunction with new information on the genetics of idiopathic epilepsies, can be applied to the search for improved antiepileptic drugs (AEDs). Marketed AEDs predominantly target voltage-gated cation channels (the alpha subunits of voltage-gated Na+ channels and also T-type voltage-gated Ca2+ channels) or influence GABA-mediated inhibition. Recently, alpha2-delta voltage-gated Ca2+ channel subunits and the SV2A synaptic vesicle protein have been recognized as likely targets. Genetic studies of familial idiopathic epilepsies have identified numerous genes associated with diverse epilepsy syndromes, including genes encoding Na+ channels and GABA(A) receptors, which are known AED targets. A strategy based on genes associated with epilepsy in animal models and humans suggests other potential AED targets, including various voltage-gated Ca2+ channel subunits and auxiliary proteins, A- or M-type voltage-gated K+ channels, and ionotropic glutamate receptors. Recent progress in ion channel research brought about by molecular cloning of the channel subunit proteins and studies in epilepsy models suggest additional targets, including G-protein-coupled receptors, such as GABA(B) and metabotropic glutamate receptors; hyperpolarization-activated cyclic nucleotide-gated cation (HCN) channel subunits, responsible for hyperpolarization-activated current Ih; connexins, which make up gap junctions; and neurotransmitter transporters, particularly plasma membrane and vesicular transporters for GABA and glutamate. New information from the structural characterization of ion channels, along with better understanding of ion channel function, may allow for more selective targeting. For example, Na+ channels underlying persistent Na+ currents or GABA(A) receptor isoforms responsible for tonic (extrasynaptic) currents represent attractive targets. The growing understanding of the pathophysiology of epilepsy and the structural and functional characterization of the molecular targets provide many opportunities to create improved epilepsy therapies. (+info)Characterization of the antinociceptive actions of bicifadine in models of acute, persistent, and chronic pain. (6/35)
Bicifadine (1-p-tolyl-3-azabicyclo[3.1.0]hexane) inhibits monoamine neurotransmitter uptake by recombinant human transporters in vitro with a relative potency of norepinephrine > serotonin > dopamine (approximately 1:2:17). This in vitro profile is supported by microdialysis studies in freely moving rats, where bicifadine (20 mg/kg i.p.) increased extrasynaptic norepinephrine and serotonin levels in the prefrontal cortex, norepinephrine levels in the locus coeruleus, and dopamine levels in the striatum. Orally administered bicifadine is an effective antinociceptive in several models of acute, persistent, and chronic pain. Bicifadine potently suppressed pain responses in both the Randall-Selitto and kaolin models of acute inflammatory pain and in the phenyl-p-quinone-induced and colonic distension models of persistent visceral pain. Unlike many transport inhibitors, bicifadine was potent and completely efficacious in both phases of the formalin test in both rats and mice. Bicifadine also normalized the nociceptive threshold in the complete Freund's adjuvant model of persistent inflammatory pain and suppressed mechanical and thermal hyperalgesia and mechanical allodynia in the spinal nerve ligation model of chronic neuropathic pain. Mechanical hyperalgesia was also reduced by bicifadine in the streptozotocin model of neuropathic pain. Administration of the D(2) receptor antagonist (-)-sulpiride reduced the effects of bicifadine in the mechanical hyperalgesia assessment in rats with spinal nerve ligations. These results indicate that bicifadine is a functional triple reuptake inhibitor with antinociceptive and antiallodynic activity in acute, persistent, and chronic pain models, with activation of dopaminergic pathways contributing to its antihyperalgesic actions. (+info)All aglow about presynaptic receptor regulation of neurotransmitter transporters. (7/35)
Mounting evidence supports the idea that neurotransmitter transporters are subject to many forms of post-translational regulation typically associated with receptors and ion channels, including receptor and kinase-mediated changes in transporter phosphorylation, cell surface trafficking, and/or catalytic activation. Although hints of this regulation can be achieved with traditional radiolabeled substrate flux techniques, higher resolution methods are needed that can localize transporter function in situ as well as permit real-time monitoring of transport function without confounds associated with coincident receptor activation. The elegant study by Bolan et al. (p. 1222) capitalizes on the fluorescent properties of a recently introduced substrate for the dopamine (DA) transporter (DAT), termed 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP+), to illuminate a pertussis toxin-sensitive, extracellular signal-regulated kinase (ERK1/2)-dependent pathway by which presynaptic DA D(2) receptors regulate DATs. (+info)The neurotransmitter cycle and quantal size. (8/35)
Changes in the response to release of a single synaptic vesicle have generally been attributed to postsynaptic modification of receptor sensitivity, but considerable evidence now demonstrates that alterations in vesicle filling also contribute to changes in quantal size. Receptors are not saturated at many synapses, and changes in the amount of transmitter per vesicle contribute to the physiological regulation of release. On the other hand, the presynaptic factors that determine quantal size remain poorly understood. Aside from regulation of the fusion pore, these mechanisms fall into two general categories: those that affect the accumulation of transmitter inside a vesicle and those that affect vesicle size. This review will summarize current understanding of the neurotransmitter cycle and indicate basic, unanswered questions about the presynaptic regulation of quantal size. (+info)Vesicular neurotransmitter transport proteins are a type of membrane protein that play a crucial role in the storage and release of neurotransmitters within neurons. They are responsible for transporting neurotransmitters from the cytoplasm into synaptic vesicles, which are small membrane-bound sacs that store neurotransmitters and are released during neurotransmission.
There are several different types of vesicular neurotransmitter transport proteins, each specific to a particular neurotransmitter or group of neurotransmitters. For example, the vesicular monoamine transporter (VMAT) family transports monoamines such as dopamine, norepinephrine, and serotonin, while the vesicular acetylcholine transporter (VAChT) transports acetylcholine.
These transport proteins are critical for maintaining appropriate levels of neurotransmitters in the synapse and regulating neuronal signaling. Dysfunction in these proteins has been implicated in a variety of neurological disorders, including Parkinson's disease, depression, and attention deficit hyperactivity disorder (ADHD).
Neurotransmitter transport proteins are a type of membrane transporter protein that are responsible for the reuptake of neurotransmitters from the synaptic cleft back into the presynaptic neuron or glial cells. These proteins play a crucial role in regulating the concentration and duration of action of neurotransmitters in the synapse, thereby terminating the neurotransmission process.
There are two main types of neurotransmitter transport proteins: sodium-dependent and sodium-independent transporters. Sodium-dependent transporters use the energy generated by the movement of sodium ions across the membrane to transport neurotransmitters against their concentration gradient, while sodium-independent transporters do not require sodium ions for transport.
Neurotransmitter transport proteins are specific to each type of neurotransmitter and play an essential role in maintaining the homeostasis of the nervous system. Dysfunction of these proteins has been implicated in various neurological and psychiatric disorders, such as depression, anxiety, and Parkinson's disease.
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.
Neurotransmitter agents are substances that affect the synthesis, storage, release, uptake, degradation, or reuptake of neurotransmitters, which are chemical messengers that transmit signals across a chemical synapse from one neuron to another. These agents can be either agonists, which mimic the action of a neurotransmitter and bind to its receptor, or antagonists, which block the action of a neurotransmitter by binding to its receptor without activating it. They are used in medicine to treat various neurological and psychiatric disorders, such as depression, anxiety, and Parkinson's disease.
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.
Fatty acid transport proteins (FATPs) are a group of membrane-bound proteins that play a crucial role in the uptake and transport of long-chain fatty acids across the plasma membrane of cells. They are widely expressed in various tissues, including the heart, muscle, adipose tissue, and liver.
FATPs have several domains that enable them to perform their functions, including a cytoplasmic domain that binds to fatty acids, a transmembrane domain that spans the plasma membrane, and an ATP-binding cassette (ABC) domain that hydrolyzes ATP to provide energy for fatty acid transport.
FATPs also play a role in the regulation of intracellular lipid metabolism by modulating the activity of enzymes involved in fatty acid activation, desaturation, and elongation. Mutations in FATP genes have been associated with various metabolic disorders, including congenital deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), a rare autosomal recessive disorder that affects fatty acid oxidation.
In summary, fatty acid transport proteins are essential for the uptake and metabolism of long-chain fatty acids in cells and have implications in various metabolic disorders.
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.
Biological transport, active is the process by which cells use energy to move materials across their membranes from an area of lower concentration to an area of higher concentration. This type of transport is facilitated by specialized proteins called transporters or pumps that are located in the cell membrane. These proteins undergo conformational changes to physically carry the molecules through the lipid bilayer of the membrane, often against their concentration gradient.
Active transport requires energy because it works against the natural tendency of molecules to move from an area of higher concentration to an area of lower concentration, a process known as diffusion. Cells obtain this energy in the form of ATP (adenosine triphosphate), which is produced through cellular respiration.
Examples of active transport include the uptake of glucose and amino acids into cells, as well as the secretion of hormones and neurotransmitters. The sodium-potassium pump, which helps maintain resting membrane potential in nerve and muscle cells, is a classic example of an active transporter.
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.
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.
Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.
There are several types of cation transport proteins, including:
1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.
2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).
3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.
4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.
Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.
Ion transport refers to the active or passive movement of ions, such as sodium (Na+), potassium (K+), chloride (Cl-), and calcium (Ca2+) ions, across cell membranes. This process is essential for various physiological functions, including nerve impulse transmission, muscle contraction, and maintenance of resting membrane potential.
Ion transport can occur through several mechanisms, including:
1. Diffusion: the passive movement of ions down their concentration gradient, from an area of high concentration to an area of low concentration.
2. Facilitated diffusion: the passive movement of ions through specialized channels or transporters in the cell membrane.
3. Active transport: the energy-dependent movement of ions against their concentration gradient, requiring the use of ATP. This process is often mediated by ion pumps, such as the sodium-potassium pump (Na+/K+-ATPase).
4. Co-transport or symport: the coupled transport of two or more different ions or molecules in the same direction, often driven by an electrochemical gradient.
5. Counter-transport or antiport: the coupled transport of two or more different ions or molecules in opposite directions, also often driven by an electrochemical gradient.
Abnormalities in ion transport can lead to various medical conditions, such as cystic fibrosis (which involves defective chloride channel function), hypertension (which may be related to altered sodium transport), and certain forms of heart disease (which can result from abnormal calcium handling).
Anion transport proteins are specialized membrane transport proteins that facilitate the movement of negatively charged ions, known as anions, across biological membranes. These proteins play a crucial role in maintaining ionic balance and regulating various physiological processes within the body.
There are several types of anion transport proteins, including:
1. Cl-/HCO3- exchangers (also known as anion exchangers or band 3 proteins): These transporters facilitate the exchange of chloride (Cl-) and bicarbonate (HCO3-) ions across the membrane. They are widely expressed in various tissues, including the red blood cells, gastrointestinal tract, and kidneys, where they help regulate pH, fluid balance, and electrolyte homeostasis.
2. Sulfate permeases: These transporters facilitate the movement of sulfate ions (SO42-) across membranes. They are primarily found in the epithelial cells of the kidneys, intestines, and choroid plexus, where they play a role in sulfur metabolism and absorption.
3. Cl- channels: These proteins form ion channels that allow chloride ions to pass through the membrane. They are involved in various physiological processes, such as neuronal excitability, transepithelial fluid transport, and cell volume regulation.
4. Cation-chloride cotransporters: These transporters move both cations (positively charged ions) and chloride anions together across the membrane. They are involved in regulating neuronal excitability, cell volume, and ionic balance in various tissues.
Dysfunction of anion transport proteins has been implicated in several diseases, such as cystic fibrosis (due to mutations in the CFTR Cl- channel), distal renal tubular acidosis (due to defects in Cl-/HCO3- exchangers), and some forms of epilepsy (due to abnormalities in cation-chloride cotransporters).
Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.
Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.
Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.
It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.
Axonal transport is the controlled movement of materials and organelles within axons, which are the nerve fibers of neurons (nerve cells). This intracellular transport system is essential for maintaining the structural and functional integrity of axons, particularly in neurons with long axonal processes. There are two types of axonal transport: anterograde transport, which moves materials from the cell body toward the synaptic terminals, and retrograde transport, which transports materials from the synaptic terminals back to the cell body. Anterograde transport is typically slower than retrograde transport and can be divided into fast and slow components based on velocity. Fast anterograde transport moves vesicles containing neurotransmitters and their receptors, as well as mitochondria and other organelles, at speeds of up to 400 mm/day. Slow anterograde transport moves cytoskeletal elements, proteins, and RNA at speeds of 1-10 mm/day. Retrograde transport is primarily responsible for recycling membrane components, removing damaged organelles, and transmitting signals from the axon terminal to the cell body. Dysfunctions in axonal transport have been implicated in various neurodegenerative disorders, such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS).
Neurotransmitter transporter
Viral neuronal tracing
Vesicular glutamate transporter 3
Neurotransmitter
Endocannabinoid transporter
S100A10
Exocytosis
Cell signaling
Synaptic vesicle
Synaptic scaling
Vesicular monoamine transporter 2
Serotonin transporter
Reuptake
Richard Scheller
Transporter
Bacterial Leucine Transporter
Membrane transport protein
Synaptic fatigue
Uptake
Transport protein
Plasma membrane monoamine transporter
Amino acid
God gene
Axonal transport
Monoamine neurotransmitter
Soluble NSF attachment protein
Neurotransmitter sodium symporter
Chemical messenger
Vesicular monoamine transporter
SLC6A18
Neurotransmitter Transport Proteins (medical concept explorer)
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Transporters17
- Neurotransmitter transporters are a class of membrane transport proteins that span the cellular membranes of neurons. (wikipedia.org)
- There are more than twenty types of neurotransmitter transporters. (wikipedia.org)
- Vesicular transporters move neurotransmitters into synaptic vesicles, regulating the concentrations of substances within them. (wikipedia.org)
- Neurotransmitter transporters frequently use electrochemical gradients that exist across cell membranes to carry out their work. (wikipedia.org)
- Normally, transporters in the synaptic membrane serve to remove neurotransmitters from the synaptic cleft and prevent their action or bring it to an end. (wikipedia.org)
- However, on occasion transporters can work in reverse, transporting neurotransmitters into the synapse, allowing these neurotransmitters to bind to their receptors and exert their effect. (wikipedia.org)
- A variety of neurotransmitter reuptake transporters are pharmacotherapeutic targets for modulating the synaptic neurotransmitter concentration, and therefore neurotransmission. (wikipedia.org)
- Antidepressants such as SSRIs, SNRIs and TCAs suppress the activity of serotonin and/or norepinephrine transporters, preventing the reuptake of targeted neurotransmitters from the synaptic cleft. (wikipedia.org)
- Vesicular transporters could provide an alternative therapeutic target for the modulation of chemical neurotransmission, as the activity of these transporters could affect the quantity of neurotransmitter released. (wikipedia.org)
- The neurotransmitter transporters belong to three known families of intrinsic membrane proteins (Figure 1). (caltech.edu)
- Drawing upon insights from model organisms and mammalian cells we show how eNHE affect surface expression and function of membrane receptors and neurotransmitter transporters. (johnshopkins.edu)
- Studies using electrophysiology and radioactive-labeled dopamine have confirmed that the dopamine transporter is similar to other monoamine transporters in that one molecule of neurotransmitter can be transported across the membrane with one or two sodium ions. (cloudfront.net)
- These transporters, many of which are sodium-coupled, have been shown to use an elevator mechanism of transport, but exactly how substrate binding is coupled to sodium ion binding and transport is not clear. (elifesciences.org)
- While the transporters that accumulate classical neurotransmitters in synaptic vesicles have been identified, little is known about how their expression regulates synaptic transmission. (bvsalud.org)
- One focus of Patrick's graduate work involved a structural and functional characterization of vesicular transport proteins such as the vesicular monoamine transporters. (fr.com)
- These projects contained simulations of neurotransmitter transporters, protein located in the cell membrane and are responsible for transporting amino acids and neurotransmitters in to cell. (boinc-af.org)
- With your help, we were able uncover how the addition of sugar molecules, also known as glycans, affects the structure and dynamics of four critical neurotransmitter transporters which may help develop more effective therapeutic molecules for neurodegenerative disorders. (boinc-af.org)
Transporter12
- A family of neurotransmitter transporter proteins that are INTEGRAL MEMBRANE PROTEINS of the LIPID BILAYER of SECRETORY VESICLES. (uams.edu)
- A family of vesicular neurotransmitter transporter proteins that were originally characterized as sodium dependent inorganic phosphate cotransporters. (uchicago.edu)
- The dopamine transporter ( DAT ) also ( sodium-dependent dopamine transporter ) is a membrane-spanning protein coded for in the human by the SLC6A3 gene , (also known as DAT1 ), that pumps the neurotransmitter dopamine out of the synaptic cleft back into cytosol . (cloudfront.net)
- [11] since DAT phosphorylation by CAMKII results in dopamine efflux in vivo , activation of transporter-coupled calcium channels is a potential mechanism by which certain drugs (e.g., amphetamine ) trigger neurotransmitter release. (cloudfront.net)
- The reuptake process occurs through specialized transporter proteins located on the membrane of the presynaptic neuron. (londonspring.org)
- These transporter proteins recognize specific neurotransmitters and transport them back into the neuron for recycling. (londonspring.org)
- In ADHD, for example, it is believed that the brain has difficulty regulating dopamine levels due to a dysfunction in dopamine transporter proteins. (londonspring.org)
- Monoamine transport inhibitors and neurotransmitters inhibited [3H]CFT binding in each fraction with a rank order of potency consistent with binding to the dopamine transporter. (aspetjournals.org)
- The SLC6A3 gene provides instructions for making a protein called the dopamine transporter or DAT. (medlineplus.gov)
- Some of the mutations change single protein building blocks (amino acids) in the dopamine transporter protein. (medlineplus.gov)
- Catecholamine plasma membrane transporter proteins regulate neural transmission as well as catecholamine metabolism and recycling. (nih.gov)
- serotonin transporter (SERT) is a protein in the cell membrane that facilitates the transport of the neurotransmitter serotonin (popularly known as the 'happiness hormone') into the cell. (facmedicine.com)
Receptors5
- For one thing, they have glutamate receptors, which they use to detect and clean up excess neurotransmitters in the spaces around neurons. (quantamagazine.org)
- For example, a class of neurotransmitters called endocannabinoids bind to proteins called cannabinoid receptors in the BBB, and the receptors help transport the molecules across the barrier and into the brain. (sciencedaily.com)
- During neurotransmitter release, often triggered by an action potential in the presynaptic neuron, the neurotransmitter is released from the presynaptic terminal and diffuses across the synaptic cleft to bind to receptors on the postsynaptic neuron. (londonspring.org)
- Some of the neurotransmitters that are not bound to receptors are taken up by the presynaptic neuron via reuptake. (londonspring.org)
- PM proteins include a variety of important proteins such as neurotransmitter receptors, G-proteins, carriers, voltage-gated ion channels, CD antigens and many drug targ. (biozol.de)
Storage and release of neurotransmitt1
- Synaptic vesicles are responsible for regulating the storage and release of neurotransmitters in the nerve terminal. (wn.com)
Neurons9
- Neurons are the chatterboxes of this conversational organ, and they speak with one another by exchanging pulses of electricity using chemical messengers called neurotransmitters. (quantamagazine.org)
- Reuptake is a crucial process by which the brain regulates the amount of neurotransmitters it uses to communicate between neurons. (londonspring.org)
- Reuptake is the process by which neurotransmitters that have been released into the synaptic cleft (the space between two neurons) are taken back up by the presynaptic neuron. (londonspring.org)
- This mechanism is essential for regulating the amount of neurotransmitters in the synaptic cleft, which affects the strength and duration of the signal between neurons. (londonspring.org)
- Reuptake is a fundamental process in the brain that regulates the amount of neurotransmitters used for communication between neurons. (londonspring.org)
- Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of serotonergic neurons. (musc.edu)
- This protein is embedded in the membrane of certain nerve cells (neurons) in the brain, where it transports a molecule called dopamine into the cell. (medlineplus.gov)
- The loss of dopaminergic neurons in the substantia nigra pars compacta (SNpc) and the accumulation of protein inclusions (Lewy bodies) are the pathological hallmarks of Parkinson's disease (PD). (northumbria.ac.uk)
- An action potential cannot cross the gap between two neighbouring neurons and instead the nerve impulse is 'carried' by neurotransmitters , a type of chemical messenger. (atarsurvivalguide.com)
Genes5
- Alcohol-responsive genes encoded proteins primarily involved in structural plasticity and neurotransmitter transport and release. (nih.gov)
- Schekman was awarded the Nobel Prize in Medicine for work he did in the 1970s, when he identified genes that control different aspects of the cell transport system. (livescience.com)
- Modular Organization of Cis-regulatory Control Information of Neurotransmitter Pathway Genes in Caenorhabditis elegans. (uchicago.edu)
- In a forward screen for genes affecting neurotransmission in Drosophila, we identified mutations in dynamin-related protein (drp1). (nih.gov)
- By figuring out which genes were defective in these yeasts, Schekman discovered dozens of components that built and controlled the cell's transport system. (nhpr.org)
Neurotransmission1
- They are ANTIPORTERS that exchange vesicular PROTONS for cytoplasmic NEUROTRANSMITTER and play an essential role in regulating neurotransmission. (uams.edu)
Cells18
- This "nonvesicular release" of neurotransmitters is used by some cells, such as amacrine cells in the retina, as a normal form of neurotransmitter release. (wikipedia.org)
- Over 30 years ago, we observed what we interpreted to be vesicular transport in crude extracts of tissue culture cells. (yale.edu)
- Our lab is working to elucidate the underlying mechanisms of vesicular transport within cells and the secretion of proteins and neurotransmitters. (yale.edu)
- Three scientists who helped uncover how the body's cells transport molecules to their correct locations have received this year's Nobel Prize in Physiology or Medicine. (livescience.com)
- Their discoveries revealed how cells control the delivery and release of molecules - such as hormones, proteins and neurotransmitters. (livescience.com)
- This protein helps transport various neurotransmitters out of cells to have an effect on the brain and body. (grass-routes.org)
- DAT is an integral membrane protein that removes dopamine from the synaptic cleft and deposits it into surrounding cells, thus terminating the signal of the neurotransmitter. (cloudfront.net)
- and RED BLOOD CELLS where they remove inhibitory neurotransmitter glycine from the EXTRACELLULAR SPACE. (childrensmercy.org)
- When signals are transmitted by synapses, messenger molecules (neurotransmitters) are released from storage chambers (synaptic vesicles) into the synaptic cleft, where they are "recognized" by neighboring nerve cells. (news-medical.net)
- They carried out measurements on PC12 cells that release the neurotransmitter dopamine when stimulated by a high potassium concentration, analogous to nerve cells. (news-medical.net)
- The cause lies in a mutation that changes a single amino acid in a protein that transports the neurotransmitter glutamate across the membrane of neural cells. (hexbyteinc.com)
- This protein transports glutamate across the membrane of neural cells," explains structural biologist Albert Guskov. (hexbyteinc.com)
- In human neural cells, this would lead to a reduced transport of the neurotransmitter glutamate , and increased anion imbalance. (hexbyteinc.com)
- In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues. (elitehealthonline.com)
- Others lead to the production of an abnormally short protein or prevent cells from producing any functional protein. (medlineplus.gov)
- Alterations in redox homeostasis and bioenergetics (energy failure) are thought to be central components of neurodegeneration that contribute to the impairment of important homeostatic processes in dopaminergic cells such as protein quality control mechanisms, neurotransmitter release/metabolism, axonal transport of vesicles and cell survival. (northumbria.ac.uk)
- In 1976, Schekman , a new professor at the University of California, Berkeley, had recently found mutant yeast cells that had faulty transport systems. (nhpr.org)
- The ambulatory little guys are believed to carry a number of necessary materials, including but not limited to vesicles - AKA, tiny lil' sacks that the body creates to transport things like enzymes, hormones, neurotransmitters and proteins - and organelles, which are in essence tiny organs that perform a number of necessary functions inside individual cells. (futurism.com)
Symporters1
- A family of sodium chloride-dependent neurotransmitter symporters that transport the amino acid GLYCINE. (childrensmercy.org)
Cell membrane2
- The protein is inserted in the cell membrane, and the mutation changes a proline amino acid in one of the helical transmembrane domains into an arginine. (hexbyteinc.com)
- This causes the neurotransmitter-containing vesicles to fuse with the cell membrane of the pre-synaptic knob. (atarsurvivalguide.com)
Optimization Elixir1
- Neurotransmitter Optimization Elixir works to improve overall health and wellbeing by providing energetic frequencies designed to improve the production and function of the important neurotransmitters GABA, Dopamine, Glutamate, Norepinephrine and Serotonin, as well as their associated transport proteins. (gethealthyagain.com)
Reuptake5
- If you are studying AP Psychology, you have likely encountered the term 'reuptake' in your lessons about how neurotransmitters work in the brain. (londonspring.org)
- Reuptake is a crucial mechanism for maintaining the balance of neurotransmitters in the brain. (londonspring.org)
- If reuptake is disrupted, it can result in an imbalanced amount of neurotransmitters in the synaptic cleft. (londonspring.org)
- In addiction, drugs of abuse can interfere with the normal reuptake process, leading to an overabundance of neurotransmitters like dopamine in the synaptic cleft. (londonspring.org)
- However, certain gene classes including neurotransmitter release and reuptake as well as synapse turnover, harbor significant variability in the same cell type across anatomical regions, suggesting differences in network activity may influence cell-type identity. (biorxiv.org)
Neuron6
- Once inside the neuron, the neurotransmitter can be either degraded by enzymes or repackaged into vesicles for later release. (londonspring.org)
- Dopamine is a chemical messenger (neurotransmitter) that relays signals from one neuron to another. (medlineplus.gov)
- One neuron communicates with another by secreting neurotransmitters , such as dopamine and serotonin. (nhpr.org)
- But a neuron must release the neurotransmitter at a particular place - and at the right time. (nhpr.org)
- The pre-synaptic neuron ends with an enlarged tip, called the synaptic knob , which houses vesicles containing neurotransmitters (often acetylcholine). (atarsurvivalguide.com)
- The neurotransmitters then bind to specific receptor proteins which are found on the dendrites of the post-synaptic neuron . (atarsurvivalguide.com)
Molecules4
- However, the BBB does permit some molecules to pass, such as glucose and certain amino acids and neurotransmitters. (sciencedaily.com)
- The bile acid sodium symporter (BASS) family transports a wide array of molecules across membranes, including bile acids in humans, and small metabolites in plants. (elifesciences.org)
- This salt bridge, a form of attraction between molecules, appears to slow down the movement of the elevator part of the protein. (hexbyteinc.com)
- Perhaps most excitingly, it's believed that because these molecules play an important role in cell division , figuring out how to selectively annihilate or otherwise manipulate cancerous motor proteins may one day be used as the mechanism behind promising future treatments. (futurism.com)
Vesicle4
- Then the efflux of protons from the vesicle provides the energy to bring the neurotransmitter into the vesicle. (wikipedia.org)
- He found that specific proteins on the vesicle bind to proteins on the cell's membrane, "like two sides of a zipper," the statement said. (livescience.com)
- Synaptic vesicle membrane protein VAT-1 homolog is a protein that in humans is encoded by the VAT1 gene . (wn.com)
- The process works a bit like a zipper: A protein on the vesicle zips up with another one on the cell's membrane to position the cargo in the correct location. (nhpr.org)
Bind1
- The fact that there are many such proteins and that they bind only in specific combinations ensures that cargo is delivered to a precise location," the statement said. (livescience.com)
Excitatory1
- Vesicular glutamate transport proteins sequester the excitatory neurotransmitter GLUTAMATE from the CYTOPLASM into SECRETORY VESICLES in exchange for lumenal PROTONS. (uchicago.edu)
Regulates1
- However, not much is known about how the cell's internal machinery regulates these proteins. (boinc-af.org)
Release4
- Our results finally provide a connection between zinc and the regulation of neurotransmitter release. (news-medical.net)
- To determine which drugs might specifically potentiate neurotransmitter release, we performed an additional secondary screen for drugs that require presynaptic amine storage to rescue larval locomotion. (bvsalud.org)
- Vesicular transport proteins package classical neurotransmitters for regulated exocytotic release, and localize to at least two distinct types of secretory vesicles. (bvsalud.org)
- If the activity of the protein-transporting neurotransmitters is really low, it might mean, for example, decreased release of dopamine, a compound related to feeling well", explained Vaht. (ut.ee)
Membranes2
- Their primary function is to carry neurotransmitters across these membranes and to direct their further transport to specific intracellular locations. (wikipedia.org)
- These proteins harness the sodium ion gradient to transport bile acids across the plasma membranes of enterocytes of the terminal ileum and hepatocytes, respectively. (elifesciences.org)
Drugs1
- There may be a breakthrough in curing this, as well as many other psychic disorders, after the potential discovery of drugs that would impact a certain transport protein in the brain - the one that a group of scientists from the University of Tartu have, figuratively speaking, put their finger on. (ut.ee)
Structural2
- The overall goal is to understand transport pathways from structural mechanism to cellular physiology. (yale.edu)
- Structural and biochemical analysis of a bacterial homolog, ASTBnm, in complex with its native substrate (not bile acids, but a vitamin A precursor, pantoate) show a new binding site that is consistent with classical proposals for elevator-type transport mechanisms. (elifesciences.org)
Conformational1
- Once dopamine binds, the protein undergoes a conformational change, which allows both sodium and dopamine to unbind on the intracellular side of the membrane. (cloudfront.net)
Nerve1
- It might seem simple: neurotransmitters related to feeling well and alert, such as serotonin, dopamine, adrenaline, noradrenaline, are sent from one nerve cell to another at the right time and in the right amount. (ut.ee)
Molecular7
- Molecular dynamics (MD) simulations highlight the improved stability for the substrate in the active site when ions are present, suggesting a binding order during the transport cycle. (elifesciences.org)
- The true molecular nature of the protein is unknown [3] . (chemeurope.com)
- Therefore, the researchers performed molecular dynamics simulations , which show all the interactions of the amino acids of the protein with their surroundings. (hexbyteinc.com)
- Size-exclusion chromatography indicated [3H]CFT bound to a single protein in each fraction (apparent molecular weight, 170 kDa). (aspetjournals.org)
- In particular, he regularly performed molecular cloning and protein purification techniques as well as analytical activity assays such as transport assays designed to measure neurotransmitter transport into vesicles. (fr.com)
- Structure of monomeric full-length ARC sheds light on molecular flexibility, protein interactions, and functional modalities. (nih.gov)
- Signal transduction, molecular transport and cell-cell interactions are all mediated by PM proteins. (biozol.de)
Myosins2
- In reality, there are many different proteins, three of which - kinesins, myosins, and dyneins- are considered 'motor' proteins. (futurism.com)
- Different motor proteins are understood to move differently - myosins carry out a type of scooting motion , while dyneins have been shown to swing from tiny cellular monkey bars with grappling hook-like arms . (futurism.com)
Profiles3
- This graph shows the total number of publications written about "Vesicular Neurotransmitter Transport Proteins" by people in UAMS Profiles by year, and whether "Vesicular Neurotransmitter Transport Proteins" was a major or minor topic of these publications. (uams.edu)
- Below are the most recent publications written about "Vesicular Neurotransmitter Transport Proteins" by people in Profiles over the past ten years. (uams.edu)
- Below are the most recent publications written about "Serotonin Plasma Membrane Transport Proteins" by people in Profiles. (musc.edu)
Vesicular transport1
- The protein encoded by this gene is an abundant integral membrane protein of cholinergic synaptic vesicles and is thought to be involved in vesicular transport. (wn.com)
Mitochondria1
- The other three ("non-standard" or "non-canonical") are selenocysteine (present in many noneukaryotes as well as most eukaryotes, but not coded directly by DNA), pyrrolysine (found only in some archea and one bacterium) and N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts). (elitehealthonline.com)
Cell's transport system1
- The cell's transport system must control the delivery of cargo to ensure it reaches the right place at the right time. (livescience.com)
Concentration2
- The energy for transport, which is often against the neurotransmitter concentration gradient, is derived from the cotransport (and in some cases the counter transport) of inorganic ions. (caltech.edu)
- Ion-transporting ATPases establish the concentration gradients for these ions. (caltech.edu)
Mechanism1
- Then a few years later, Suedhof , who is now 57, identified the trigger mechanism that dumps the neurotransmitter outside the cell at just the right time by unzipping the two proteins. (nhpr.org)
MeSH2
- Vesicular Neurotransmitter Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uams.edu)
- Serotonin Plasma Membrane Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (musc.edu)
Functional1
- Compartmental specificity is encoded to a remarkable degree in the functional partnering of SNARE proteins, a fact which is in no way inconsistent with the emerging contribution of upstream regulatory components (like rabGTPases and tethering complexes) to domain/compartment specificity. (yale.edu)
Lipid2
- Using cryo-electron microscopy on normal and mutated proteins placed in lipid nanodiscs, the team was able to compare the shape of the mutated protein to the normal version. (hexbyteinc.com)
- and the non-standard carnitine is used in lipid transport. (elitehealthonline.com)
