Relevant bibliographies by topics / Neurotransmitter Transport Proteins

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Academic literature on the topic 'Neurotransmitter Transport Proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Neurotransmitter Transport Proteins"

1

Reyes, Nicolas, and Sotiria Tavoulari. "To be, or not to be two sites: that is the question about LeuT substrate binding." Journal of General Physiology 138, no. 4 (September 12, 2011): 467–71. http://dx.doi.org/10.1085/jgp.201110652.

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Transport proteins of the neurotransmitter sodium symporter (NSS) family regulate the extracellular concentration of several neurotransmitters in the central nervous system. The only member of this family for which atomic-resolution structural data are available is the prokaryotic homologue LeuT. This protein has been used as a model system to study the molecular mechanism of transport of the NSS family. In this Journal Club, we discuss two strikingly different LeuT transport mechanisms: one involving a single high-affinity substrate binding site and one recently proposed alternative involving two high-affinity substrate binding sites that are allosterically coupled.
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Gouaux, Eric. "The molecular logic of sodium-coupled neurotransmitter transporters." Philosophical Transactions of the Royal Society B: Biological Sciences 364, no. 1514 (October 31, 2008): 149–54. http://dx.doi.org/10.1098/rstb.2008.0181.

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Synaptic transmission at chemical synapses requires the removal of neurotransmitter from extracellular spaces. At synapses in the central nervous system, this is accomplished by sodium-coupled transport proteins, integral membrane proteins that thermodynamically couple the uptake of neurotransmitter to the uptake of sodium and, in some cases, the uptake and export of additional ions. Recent X-ray crystallographic studies have revealed the architecture of the two major families of neurotransmitter transporters and, together with additional biochemical and biophysical studies, have provided insights into mechanisms of ion coupling, substrate uptake, and inhibition of transport.
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Nair, Ramya, Juliane Lauks, SangYong Jung, Nancy E. Cooke, Heidi de Wit, Nils Brose, Manfred W. Kilimann, Matthijs Verhage, and JeongSeop Rhee. "Neurobeachin regulates neurotransmitter receptor trafficking to synapses." Journal of Cell Biology 200, no. 1 (December 31, 2012): 61–80. http://dx.doi.org/10.1083/jcb.201207113.

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The surface density of neurotransmitter receptors at synapses is a key determinant of synaptic efficacy. Synaptic receptor accumulation is regulated by the transport, postsynaptic anchoring, and turnover of receptors, involving multiple trafficking, sorting, motor, and scaffold proteins. We found that neurons lacking the BEACH (beige-Chediak/Higashi) domain protein Neurobeachin (Nbea) had strongly reduced synaptic responses caused by a reduction in surface levels of glutamate and GABAA receptors. In the absence of Nbea, immature AMPA receptors accumulated early in the biosynthetic pathway, and mature N-methyl-d-aspartate, kainate, and GABAA receptors did not reach the synapse, whereas maturation and surface expression of other membrane proteins, synapse formation, and presynaptic function were unaffected. These data show that Nbea regulates synaptic transmission under basal conditions by targeting neurotransmitter receptors to synapses.
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Benner, Emily, Marco J. Acevedo, and Jeffry D. Madura. "Assessing the Transport Mechanism of Neurotransmitter Sodium Symporter Proteins with Molecular Dynamics." Biophysical Journal 106, no. 2 (January 2014): 255a—256a. http://dx.doi.org/10.1016/j.bpj.2013.11.1501.

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LoPresti, Patrizia. "HDAC6 in Diseases of Cognition and of Neurons." Cells 10, no. 1 (December 23, 2020): 12. http://dx.doi.org/10.3390/cells10010012.

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Central nervous system (CNS) neurodegenerative diseases are characterized by faulty intracellular transport, cognition, and aggregate regulation. Traditionally, neuroprotection exerted by histone deacetylase (HDAC) inhibitors (HDACi) has been attributed to the ability of this drug class to promote histone acetylation. However, HDAC6 in the healthy CNS functions via distinct mechanisms, due largely to its cytoplasmic localization. Indeed, in healthy neurons, cytoplasmic HDAC6 regulates the acetylation of a variety of non-histone proteins that are linked to separate functions, i.e., intracellular transport, neurotransmitter release, and aggregate formation. These three HDAC6 activities could work independently or in synergy. Of particular interest, HDAC6 targets the synaptic protein Bruchpilot and neurotransmitter release. In pathological conditions, HDAC6 becomes abundant in the nucleus, with deleterious consequences for transcription regulation and synapses. Thus, HDAC6 plays a leading role in neuronal health or dysfunction. Here, we review recent findings and novel conclusions on the role of HDAC6 in neurodegeneration. Selective studies with pan-HDACi are also included. We propose that an early alteration of HDAC6 undermines synaptic transmission, while altering transport and aggregation, eventually leading to neurodegeneration.
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Jones, Eugenia M. C. "Na+ - and Cl−-dependent neurotransmitter transporters in bovine retina: Identification and localization by in situ hybridization histochemistry." Visual Neuroscience 12, no. 6 (November 1995): 1135–42. http://dx.doi.org/10.1017/s0952523800006775.

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AbstractThe physiological actions of biogenic amine and amino-acid neurotransmitters are terminated by their removal from the synaptic cleft by specific high-affinity transport proteins. The members of the Na+- and Cl−-dependent neurotransmitter transporter family expressed in bovine retina and responsible for the uptake of biogenic amine and amino-acid neurotransmitters were identified using a reverse transcriptase-polymerase chain reaction-based approach. cDNA clones encoding bovine homologues of glycine (GLYT-1), γ-aminobutyric acid (GAT-1) creatine (CreaT), and orphan (NTT4) transporters were identified using this strategy. The expression pattern of mRNAs encoding these proteins in the retina was determined by in situ hybridization histochemistry GLYT-1 CreaT NTT4 and GAT-1 mRNAs were expressed in the retina by cells in the inner nuclear inner plex, iform and ganglion cell layers They were not expressed at detectable levels in the photoreceptor cells whose cell bodies are in the outer nuclear layer and are the most abundant cell type in the retina GLYT-1 mRNA was present exclusively in the proximal inner nuclear layer GAT-1 mRNA was localized to both the inner nuclear and ganglion cell layers CreaT mRNA was expressed in all cell types in the retina except photoreceptors and NTT4 mRNA was expressed by a sub subpoulation of cells in the ganglion cell laver. Elucidation of the expression pattern of these neurotransmitter transporter mRNAs in the retina provides a basis for studies of the role of glycine γ-aminobutyric acid and creatine transporters in retinal function.
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Vardy, Eyal, Sonia Steiner-Mordoch, and Shimon Schuldiner. "Characterization of Bacterial Drug Antiporters Homologous to Mammalian Neurotransmitter Transporters." Journal of Bacteriology 187, no. 21 (November 1, 2005): 7518–25. http://dx.doi.org/10.1128/jb.187.21.7518-7525.2005.

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ABSTRACT Multidrug transporters are ubiquitous proteins, and, based on amino acid sequence similarities, they have been classified into several families. Here we characterize a cluster of archaeal and bacterial proteins from the major facilitator superfamily (MFS). One member of this family, the vesicular monoamine transporter (VMAT) was previously shown to remove both neurotransmitters and toxic compounds from the cytoplasm, thereby conferring resistance to their effects. A BLAST search of the available microbial genomes against the VMAT sequence yielded sequences of novel putative multidrug transporters. The new sequences along with VMAT form a distinct cluster within the dendrogram of the MFS, drug-proton antiporters. A comparison with other proteins in the family suggests the existence of a potential ion pair in the membrane domain. Three of these genes, from Mycobacterium smegmatis, Corynebacterium glutamicum, and Halobacterium salinarum, were cloned and functionally expressed in Escherichia coli. The proteins conferred resistance to fluoroquinolones and chloramphenicol (at concentrations two to four times greater than that of the control). Measurement of antibiotic accumulation in cells revealed proton motive force-dependent transport of those compounds.
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Vandenberg, Robert J., and Renae M. Ryan. "Mechanisms of Glutamate Transport." Physiological Reviews 93, no. 4 (October 2013): 1621–57. http://dx.doi.org/10.1152/physrev.00007.2013.

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l-Glutamate is the predominant excitatory neurotransmitter in the mammalian central nervous system and plays important roles in a wide variety of brain functions, but it is also a key player in the pathogenesis of many neurological disorders. The control of glutamate concentrations is critical to the normal functioning of the central nervous system, and in this review we discuss how glutamate transporters regulate glutamate concentrations to maintain dynamic signaling mechanisms between neurons. In 2004, the crystal structure of a prokaryotic homolog of the mammalian glutamate transporter family of proteins was crystallized and its structure determined. This has paved the way for a better understanding of the structural basis for glutamate transporter function. In this review we provide a broad perspective of this field of research, but focus primarily on the more recent studies with a particular emphasis on how our understanding of the structure of glutamate transporters has generated new insights.
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Haase, J., A. M. Killian, F. Magnani, and C. Williams. "Regulation of the serotonin transporter by interacting proteins." Biochemical Society Transactions 29, no. 6 (November 1, 2001): 722–28. http://dx.doi.org/10.1042/bst0290722.

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The serotonin transporter (SERT) plays a critical role in the maintenance of normal neurotransmission by serotonin [5-hydroxytryptamine (5-HT)]. Recent evidence suggests that SERT and other neurotransmitter transporters are tightly regulated. Activation of protein kinase C results in a decrease in SERT-mediated 5-HT uptake, which is due to an internalization of the transporter. However, to date little is known about the mechanism and proteins involved in the down-regulation of the transporter. One candidate SERT-regulatory protein is the SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) protein, syntaxin 1A (Syn1A), which has recently been implicated in the regulation of ion channels as well as the SERT-related γ-aminobutyric acid- and glycine-transporters. Using 5-HT uptake assays, confocal microscopy and glutathione S-transferase (GST) pull-down assays we showed that Syn1A also interacts with SERT and alters the subcellular localization of the transporter, resulting in a reduction of 5-HT transport. In addition, we have used the yeast two-hybrid system to search for novel regulatory proteins that interact with the cytoplasmic N-terminal domain of SERT. By screening rat brain cDNA library we have identified six potential SERT-binding proteins. Here we also present progress towards the elucidation of the biological relevance of these proteins and their potential role for the regulation of the serotonin transporter.
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Matsuura, Kenji, Mieko Otani, Masaoki Takano, Keiichi Kadoyama, and Shogo Matsuyama. "Proteomic Analysis of Hippocampus and Cortex in Streptozotocin-Induced Diabetic Model Mice Showing Dementia." Journal of Diabetes Research 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/8953015.

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Aim. Diabetes with its associated hyperglycemia induces various type of peripheral damage and also impairs the central nervous system (CNS). This study is aimed at clarifying the precise mechanism of diabetes-induced dementia as an impairment of CNS. Methods. The proteomic analysis of the hippocampus and cortex in streptozotocin- (STZ-) treated mouse diabetic model showing dementia was performed using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (n=3/group). Results. Significant changes in the expression of 32 proteins and 7 phosphoproteins were observed in the hippocampus and cortex. These identified proteins and phosphoproteins could be functionally classified as cytoskeletal protein, oxidoreductase, protein deubiquitination, energy metabolism, GTPase activation, heme binding, hydrolase, iron storage, neurotransmitter release, protease inhibitor, transcription, glycolysis, antiapoptosis, calcium ion binding, heme metabolic process, protein degradation, vesicular transport, and unknown in the hippocampus or cortex. Additionally, Western blotting validated the changes in translationally controlled tumor protein, ATP-specific succinyl-CoA synthetase beta subunit, and gamma-enolase isoform 1. Conclusions. These findings showed that STZ-induced diabetes changed the expression of proteins and phosphoproteins in the hippocampus and cortex. We propose that alterations in expression levels of these proteins play an important role in diabetes-induced dementia.
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Dissertations / Theses on the topic "Neurotransmitter Transport Proteins"

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Gabriel, Luke R. "Dynamic Regulation at the Neuronal Plasma Membrane: Novel Endocytic Mechanisms Control Anesthetic-Activated Potassium Channels and Amphetamine-Sensitive Dopamine Transporters: A Dissertation." eScholarship@UMMS, 2013. http://escholarship.umassmed.edu/gsbs_diss/725.

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Endocytic trafficking dynamically regulates neuronal plasma membrane protein presentation and activity, and plays a central role in excitability and plasticity. Over the course of my dissertation research I investigated endocytic mechanisms regulating two neuronal membrane proteins: the anesthetic-activated potassium leak channel, KCNK3, as well as the psychostimulant-sensitive dopamine transporter (DAT). My results indicate that KCNK3 internalizes in response to Protein Kinase C (PKC) activation, using a novel pathway that requires the phosphoserine binding protein, 14-3-3β, and demonstrates for the first time regulated KCNK3 channel trafficking in neurons. Additionally, PKC-mediated KCNK3 trafficking requires a non-canonical endocytic motif, which is shared exclusively between KCNK3 and sodium-dependent neurotransmitter transporters, such as DAT. DAT trafficking studies in intact ex vivo adult striatal slices indicate that DAT endocytic trafficking has both dynamin-dependent and –independent components. Moreover, DAT segregates into two populations at the neuronal plasma membrane: trafficking-competent and -incompetent. Taken together, these results demonstrate that novel, non-classical endocytic mechanisms dynamically control the plasma membrane presentation of these two important neuronal proteins.
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2

Seneca, Nicholas. "Pet imaging of two monoaminergic neurotransmitter systems in brain : studies of the norepinephrine transporter and dopamine D₂ receptor /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-923-8/.

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Naudon, Laurent. "Recherche d'une participation du transporteur neuronal de la dopamine et du transporteur vésiculaire à l'adaptation neuronale." Rouen, 1994. http://www.theses.fr/1994ROUES066.

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L'ensemble des résultats que nous avons obtenus semblent indiquer que le transporteur neuronal de la dopamine et le transporteur vésiculaire des monoamines, malgré leurs rôles essentiels dans la transmission synaptique, ne participent que faiblement à l'adaptation des neurones dopaminergiques
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Arac-Ozkan, Demet. "Mechanism of synaptotagmin action in neurotransmitter release." 2005. http://edissertations.library.swmed.edu/pdf/Arac-OzkanD121905/Arac-OzkanDemet.pdf.

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Chen, Xiaocheng. "Unraveling the role of SNARE interactions in neurotransmitter release." 2005. http://edissertations.library.swmed.edu/pdf/ChenX050405/ChenXiaocheng.pdf.

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Piekarz, Andrew D. "Increased Resurgent Sodium Currents (INaR) in Inherited and Acquired Disorders of Excitability." Thesis, 2012. http://hdl.handle.net/1805/2886.

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Indiana University-Purdue University Indianapolis (IUPUI)
Voltage-gated sodium channels (VGSCs) are dynamic membrane spanning proteins which mediate the rapid influx of Na+ during the upstroke of the action potential (AP). In addition to the large inward Na+ currents responsible for the upstroke of the AP, some VGSC isoforms produce smaller, subthreshold Na+ currents, which can influence the excitable properties of neurons. An example of such a subthreshold current is resurgent Na+ current (INaR). These unusual currents are active during repolarization of the membrane potential, where the channel is normally refractory to activity. INaR exhibit slow gating kinetics and unusual voltage-dependence derived from a novel mechanism of channel inactivation which allows the channel to recover through an open configuration resulting in membrane depolarization early in the falling phase of the AP, ultra-fast re-priming of channels, and multiple AP spikes. Although originally identified in fast spiking central nervous system (CNS) neurons, INaR has recently been observed in a subpopulation of peripheral dorsal root ganglion (DRG) neurons. Because INaR is believed to contribute to spontaneous and high frequency firing of APs, I have hypothesized that increased INaR may contribute to ectopic AP firing associated with inherited and acquired disorders of excitability. Specifically, this dissertation explores the mechanisms which underlie the electrogenesis of INaR in DRG neurons and determines whether the biophysical properties of these unique currents were altered by mutations that cause inherited muscle and neuronal channelopathies or in an experimental model of nerve injury. The results demonstrate that (1) multiple Na+ channel isoforms are capable of producing INaR in DRG neurons, including NaV1.3, NaV1.6, and NaV1.7, (2) inherited muscle and neuronal channelopathIy mutations that slow the rate of channel inactivation increase INaR amplitude, (3) temperature sensitive INaR produced by select skeletal muscle channelopthy mutations may contribute to the triggering of cold-induced myotonia, and (4) INaR amplitude and distribution is significantly increased two weeks post contusive spinal cord injury (SCI). Taken together, results from this dissertation provide foundational knowledge of the properties and mechanism of INaR in DRG neurons and indicates that increased INaR likely contributes to the enhanced membrane excitability associated with multiple inherited and acquired disorders of excitability.
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Books on the topic "Neurotransmitter Transport Proteins"

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A, Lappi Douglas, ed. Suicide transport and immunolesioning. Austin: R.G. Landes, 1994.

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Napier, Susan. Transporters as Targets for Drugs. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009.

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Serotonin receptor technologies. New York: Humana Press, 2015.

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A, Reith Maarten E., ed. Neurotransmitter transporters: Structure, function, and regulation. 2nd ed. Totowa, NJ: Humana Press, 2002.

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A, Reith Maarten E., ed. Neurotransmitter transporters: Structure, function, and regulation. 2nd ed. Totowa, NJ: Humana Press, 2002.

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A, Reith Maarten E., ed. Neurotransmitter transporters: Structure, function, and regulation. 2nd ed. Totowa, NJ: Humana Press, 2002.

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A, Reith Maarten E., ed. Neurotransmitter transporters: Structure, function, and regulation. Totowa, N.J: Humana Press, 1997.

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Reith, Maarten E. A. Neurotransmitter Transporters: Structure, Function, and Regulation (Contemporary Neuroscience). 2nd ed. Humana Press, 2002.

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Neurotransmitter Transporters: Structure, Function, and Regulation (Contemporary Neuroscience). Humana Press, 1997.

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(Editor), Stephen Moss, and Jeremy Henley (Editor), eds. Receptor and Ion-Channel Trafficking: Cell Biology of Ligand-Gated and Voltage Sensitive Ion Channels. Oxford University Press, USA, 2002.

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Book chapters on the topic "Neurotransmitter Transport Proteins"

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Patel, Amrat P. "Neurotransmitter Transporter Proteins." In Neurotransmitter Transporters, 241–62. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-59259-470-2_8.

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Gedeon, Patrick C., James R. Thomas, and Jeffry D. Madura. "Accelerated Molecular Dynamics and Protein Conformational Change: A Theoretical and Practical Guide Using a Membrane Embedded Model Neurotransmitter Transporter." In Methods in Molecular Biology, 253–87. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1465-4_12.

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Benarroch, Eduardo E. "Axon and Myelin." In Neuroscience for Clinicians, edited by Eduardo E. Benarroch, 156–76. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780190948894.003.0010.

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Axons allow the initiation and conduction of the action potential and neurotransmitter release and have unique structure and physiology. Myelin has a unique composition of lipids and proteins. Each compartment of myelinated axons expresses a unique repertoire of ion channels, adaptor molecules, and adhesion molecules. There is a reciprocal interaction between the axons and myelinating cells. Axons are also vulnerable structures, as they may extend for long distances away from the cell body, which renders them highly dependent on mitochondrial energy metabolism, cytoskeletal integrity, and axonal transport for their maintenance and response to injury. Immune, metabolic, or degenerative disorders affecting these interactions result in a wide variety of peripheral neuropathies and leukoencephalopathies.
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Koch, Christof. "Ionic Channels." In Biophysics of Computation. Oxford University Press, 1998. http://dx.doi.org/10.1093/oso/9780195104912.003.0014.

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In the previous chapters, we studied the spread of the membrane potential in passive or active neuronal structures and the interaction among two or more synaptic inputs. We have yet to give a full account of ionic channels, the elementary units underlying all of this dizzying variety of electrical signaling both within and between neurons. Ionic channels are individual proteins anchored within the bilipid membrane of neurons, glia, or other cells, and can be thought of as water-filled macromolecular pores that are permeable to particular ions. They can be exquisitely voltage sensitive, as the fast sodium channel responsible for the sodium spike in the squid giant axon, or they can be relatively independent of voltage but dependent on the binding of some neurotransmitter, as is the case for most synaptic receptors, such as the acetylcholine receptor at the vertebrate neuromuscular junction or the AMPA and GABA synaptic receptors mediating excitation and inhibition in the central nervous system. Ionic channels are ubiquitous and provide the substratum for all biophysical phenomena underlying information processing, including mediating synaptic transmission, determining the membrane voltage, supporting action potential initiation and propagation, and, ultimately, linking changes in the membrane potential to effective output, such as the secretion of a neurotransmitter or hormone or the contraction of a muscle fiber. Individual ionic channels are amazingly specific. A typical potassium channel can distinguish a K+ ion with a 1.33 Å radius from a Na+ ion of 0.95 Å radius, selecting the former over the latter by a factor of 10,000. This single protein can do this selection at a rate of up to 100 million ions each second (Doyle et al, 1998). At the time of Hodgkin and Huxley’s seminal study in the early 1950s, two broad classes of transport mechanisms were competing as plausible ways for carrying ionic fluxes across the membrane: carrier molecules and pores. At the time, no direct evidence for either one existed. It was not until the early 1970s that the fast ACh synaptic receptor and the Na channel were chemically isolated and purified and identified as proteins.
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Levitan, Irwin B., and Leonard K. Kaczmarek. "Neurotransmitters and Neurohormones." In The Neuron, 213–38. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199773893.003.0010.

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A multitude of chemicals called neurotransmitters mediate intercellular communication in the nervous system. These include acetylcholine, the catecholamines, serotonin, glutamate, GABA, glycine, and a wide variety of neuropeptides. Although they exhibit great diversity in many of their properties, all are stored in vesicles in nerve terminals and are released to the extracellular space via a process requiring calcium ions. Their actions are terminated by reuptake into the presynaptic terminal or nearby glial cells by specific transporter proteins or by their destruction in the extracellular space. The role of neurotransmitters is to alter the properties—chemical, electrical, or both—of some target cell. With the arrival on the scene of the neuropeptides, it has become evident that signaling in the nervous system occurs through the use of rich and varied forms of chemical currency, and that some neurons use more than one type of currency simultaneously.
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