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Journal articles on the topic 'EAAT4'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Abousaab, Abeer, and Florian Lang. "Up-Regulation of Excitatory Amino Acid Transporters EAAT3 and EAAT4 by Lithium Sensitive Glycogen Synthase Kinase GSK3ß." Cellular Physiology and Biochemistry 40, no. 5 (2016): 1252–60. http://dx.doi.org/10.1159/000453179.

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Background: Cellular uptake of glutamate by the excitatory amino-acid transporters (EAATs) decreases excitation and thus participates in the regulation of neuroexcitability. Kinases impacting on neuronal function include Lithium-sensitive glycogen synthase kinase GSK3ß. The present study thus explored whether the activities of EAAT3 and/or EAAT4 isoforms are sensitive to GSK3ß. Methods: cRNA encoding wild type EAAT3 (SLC1A1) or EAAT4 (SLC1A6) was injected into Xenopus oocytes without or with additional injection of cRNA encoding wild type GSK3ß or the inactive mutant K85AGSK3ß. Dual electrode

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2

Abousaab, Abeer, Jamshed Warsi, Bernat Elvira, and Florian Lang. "Caveolin-1 Sensitivity of Excitatory Amino Acid Transporters EAAT1, EAAT2, EAAT3, and EAAT4." Journal of Membrane Biology 249, no. 3 (2015): 239–49. http://dx.doi.org/10.1007/s00232-015-9863-0.

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3

Fang, Hongyu, Yueming Huang, and Zhiyi Zuo. "Enhancement of substrate-gated Cl− currents via rat glutamate transporter EAAT4 by PMA." American Journal of Physiology-Cell Physiology 290, no. 5 (2006): C1334—C1340. http://dx.doi.org/10.1152/ajpcell.00443.2005.

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Glutamate transporters (also called excitatory amino acid transporters, EAAT) are important in extracellular homeostasis of glutamate, a major excitatory neurotransmitter. EAAT4, a neuronally expressed EAAT in cerebellum, has a large portion (∼95% of the total l-aspartate-induced currents in human EAAT4) of substrate-gated Cl− currents, a distinct feature of this EAAT. We cloned EAAT4 from rat cerebellum. This molecule was predicted to have eight putative transmembrane domains. l-Glutamate induced an inward current in oocytes expressing this EAAT4 at a holding potential −60 mV. Phorbol 12-myri

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4

Søgaard, Rikke, Ivana Novak, and Nanna MacAulay. "Elevated ammonium levels: differential acute effects on three glutamate transporter isoforms." American Journal of Physiology-Cell Physiology 302, no. 6 (2012): C880—C891. http://dx.doi.org/10.1152/ajpcell.00238.2011.

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Increased ammonium (NH4+/NH3) in the brain is a significant factor in the pathophysiology of hepatic encephalopathy, which involves altered glutamatergic neurotransmission. In glial cell cultures and brain slices, glutamate uptake either decreases or increases following acute ammonium exposure but the factors responsible for the opposing effects are unknown. Excitatory amino acid transporter isoforms EAAT1, EAAT2, and EAAT3 were expressed in Xenopus oocytes to study effects of ammonium exposure on their individual function. Ammonium increased EAAT1- and EAAT3-mediated [3H]glutamate uptake and

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5

Schneider, Nicole, Sönke Cordeiro, Jan-Philipp Machtens, Simona Braams, Thomas Rauen, and Christoph Fahlke. "Functional Properties of the Retinal Glutamate Transporters GLT-1c and EAAT5." Journal of Biological Chemistry 289, no. 3 (2013): 1815–24. http://dx.doi.org/10.1074/jbc.m113.517177.

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In the mammalian retina, glutamate uptake is mediated by members of a family of glutamate transporters known as “excitatory amino acid transporters (EAATs).” Here we cloned and functionally characterized two retinal EAATs from mouse, the GLT-1/EAAT2 splice variant GLT-1c, and EAAT5. EAATs are glutamate transporters and anion-selective ion channels, and we used heterologous expression in mammalian cells, patch-clamp recordings and noise analysis to study and compare glutamate transport and anion channel properties of both EAAT isoforms. We found GLT-1c to be an effective glutamate transporter w

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6

Mim, Carsten, Poonam Balani, Thomas Rauen, and Christof Grewer. "The Glutamate Transporter Subtypes EAAT4 and EAATs 1-3 Transport Glutamate with Dramatically Different Kinetics and Voltage Dependence but Share a Common Uptake Mechanism." Journal of General Physiology 126, no. 6 (2005): 571–89. http://dx.doi.org/10.1085/jgp.200509365.

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Here, we report the application of glutamate concentration jumps and voltage jumps to determine the kinetics of rapid reaction steps of excitatory amino acid transporter subtype 4 (EAAT4) with a 100-μs time resolution. EAAT4 was expressed in HEK293 cells, and the electrogenic transport and anion currents were measured using the patch-clamp method. At steady state, EAAT4 was activated by glutamate and Na+ with high affinities of 0.6 μM and 8.4 mM, respectively, and showed kinetics consistent with sequential binding of Na+-glutamate-Na+. The steady-state cycle time of EAAT4 was estimated to be &

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7

Abousaab, Abeer, Nestor Luis Uzcategui, Bhaeldin Elsir, and Florian Lang. "Up-Regulation of the Excitatory Amino Acid Transporters EAAT1 and EAAT2 by Mammalian Target of Rapamycin." Cellular Physiology and Biochemistry 39, no. 6 (2016): 2492–500. http://dx.doi.org/10.1159/000452516.

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Background: The excitatory amino-acid transporters EAAT1 and EAAT2 clear glutamate from the synaptic cleft and thus terminate neuronal excitation. The carriers are subject to regulation by various kinases. The EAAT3 isoform is regulated by mammalian target of rapamycin (mTOR). The present study thus explored whether mTOR influences transport by EAAT1 and/or EAAT2. Methods: cRNA encoding wild type EAAT1 (SLC1A3) or EAAT2 (SLC1A2) was injected into Xenopus oocytes without or with additional injection of cRNA encoding mTOR. Dual electrode voltage clamp was performed in order to determine electrog

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8

Hu, Qiu Xiang, Sigrid Ottestad-Hansen, Silvia Holmseth, Bjørnar Hassel, Niels Christian Danbolt, and Yun Zhou. "Expression of Glutamate Transporters in Mouse Liver, Kidney, and Intestine." Journal of Histochemistry & Cytochemistry 66, no. 3 (2018): 189–202. http://dx.doi.org/10.1369/0022155417749828.

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Glutamate transport activities have been identified not only in the brain, but also in the liver, kidney, and intestine. Although glutamate transporter distributions in the central nervous system are fairly well known, there are still uncertainties with respect to the distribution of these transporters in peripheral organs. Quantitative information is mostly lacking, and few of the studies have included genetically modified animals as specificity controls. The present study provides validated qualitative and semi-quantitative data on the excitatory amino acid transporter (EAAT)1–3 subtypes in

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9

Williams, Brent L., Kavitha Yaddanapudi, Mady Hornig, and W. Ian Lipkin. "Spatiotemporal Analysis of Purkinje Cell Degeneration Relative to Parasagittal Expression Domains in a Model of Neonatal Viral Infection." Journal of Virology 81, no. 6 (2006): 2675–87. http://dx.doi.org/10.1128/jvi.02245-06.

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ABSTRACT Infection of newborn Lewis rats with Borna disease virus (neonatal Borna disease [NBD]) results in cerebellar damage without the cellular inflammation associated with infections in later life. Purkinje cell (PC) damage has been reported for several models of early-life viral infection, including NBD; however, the time course and distribution of PC pathology have not been investigated rigorously. This study examined the spatiotemporal relationship between PC death and zonal organization in NBD cerebella. Real-time PCR at postnatal day 28 (PND28) revealed decreased cerebellar levels of

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10

Machtens, Jan-Philipp, Peter Kovermann, and Christoph Fahlke. "Substrate-dependent Gating of Anion Channels Associated with Excitatory Amino Acid Transporter 4." Journal of Biological Chemistry 286, no. 27 (2011): 23780–88. http://dx.doi.org/10.1074/jbc.m110.207514.

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EAAT glutamate transporters do not only function as secondary-active glutamate transporters but also as anion channels. EAAT anion channel activity depends on transport substrates. For most isoforms, it is negligible without external Na+ and increased by external glutamate. We here investigated gating of EAAT4 anion channels with various cations and amino acid substrates using patch clamp experiments on a mammalian cell line. We demonstrate that Li+ can substitute for Na+ in supporting substrate-activated anion currents, albeit with changed voltage dependence. Anion currents were recorded in g

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11

FYK-KOLODZIEJ, BOZENA, PU QIN, ARTURIK DZHAGARYAN, and ROBERTA G. POURCHO. "Differential cellular and subcellular distribution of glutamate transporters in the cat retina." Visual Neuroscience 21, no. 4 (2004): 551–65. http://dx.doi.org/10.1017/s0952523804214067.

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Retrieval of glutamate from extracellular sites in the retina involves at least five excitatory amino acid transporters. Immunocytochemical analysis of the cat retina indicates that each of these transporters exhibits a selective distribution which may reflect its specific function. The uptake of glutamate into Müller cells or astrocytes appears to depend upon GLAST and EAAT4, respectively. Staining for EAAT4 was also seen in the pigment epithelium. The remaining transporters are neuronal with GLT-1α localized to a number of cone bipolar, amacrine, and ganglion cells and GLT-1v in cone photore

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12

Almilaji, Ahmad, Carlos Munoz, Tatsiana Pakladok, et al. "Klotho Sensitivity of the Neuronal Excitatory Amino Acid Transporters EAAT3 and EAAT4." PLoS ONE 8, no. 7 (2013): e70988. http://dx.doi.org/10.1371/journal.pone.0070988.

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13

Burckhardt, Birgitta C., and Gerhard Burckhardt. "Interaction of Excitatory Amino Acid Transporters 1 – 3 (EAAT1, EAAT2, EAAT3) with N-Carbamoylglutamate and N-Acetylglutamate." Cellular Physiology and Biochemistry 43, no. 5 (2017): 1907–16. http://dx.doi.org/10.1159/000484110.

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Background/Aims: Inborn deficiency of the N-acetylglutamate synthase (NAGS) impairs the urea cycle and causes neurotoxic hyperammonemia. Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. Due to structural similarities to glutamate, NCG may be absorbed in the intestine and taken up into the liver by excitatory amino acid transporters (EAATs). Methods: Using Xenopus laevis oocytes expressing either human EAAT1, 2, or 3, or human sodium-dependent dicarboxylate transporter 3 (NaDC

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14

Zhou, Lei, Li Yang, Yu-jin Li, et al. "MicroRNA-128 Protects Dopamine Neurons from Apoptosis and Upregulates the Expression of Excitatory Amino Acid Transporter 4 in Parkinson’s Disease by Binding to AXIN1." Cellular Physiology and Biochemistry 51, no. 5 (2018): 2275–89. http://dx.doi.org/10.1159/000495872.

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Background/Aims: Parkinson’s disease (PD) is a frequently occurring condition that resulted from the loss of midbrain neurons, which synthesize the neurotransmitter dopamine. In this study, we established mouse models of PD to investigate the expression of microRNA-128 (miR-128) and mechanism through which it affects apoptosis of dopamine (DA) neurons and the expression of excitatory amino acid transporter 4 (EAAT4) via binding to axis inhibition protein 1 (AXIN1). Methods: Gene expression microarray analysis was performed to screen differentially expressed miRNAs that are associated with PD.

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15

Zhang, Dong, Shu Xu, Yiting Wang, Peng Bin, and Guoqiang Zhu. "The Amino Acid-mTORC1 Pathway Mediates APEC TW-XM-Induced Inflammation in bEnd.3 Cells." International Journal of Molecular Sciences 22, no. 17 (2021): 9245. http://dx.doi.org/10.3390/ijms22179245.

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The blood–brain barrier (BBB) is key to establishing and maintaining homeostasis in the central nervous system (CNS); meningitis bacterial infection can disrupt the integrity of BBB by inducing an inflammatory response. The changes in the cerebral uptake of amino acids may contribute to inflammatory response during infection and were accompanied by high expression of amino acid transporters leading to increased amino acid uptake. However, it is unclear whether amino acid uptake is changed and how to affect inflammatory responses in mouse brain microvascular endothelial (bEnd.3) cells in respon

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16

Fairman, W. A., and S. G. Amara. "Functional diversity of excitatory amino acid transporters: ion channel and transport modes." American Journal of Physiology-Renal Physiology 277, no. 4 (1999): F481—F486. http://dx.doi.org/10.1152/ajprenal.1999.277.4.f481.

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Recent studies of glutamate transporters in the central nervous system indicate that in addition to their fundamental role in mediating neurotransmitter uptake, these proteins may contribute to the modulation of a variety of cellular processes. Activation of the excitatory amino acid (EAA) carriers generates an electrogenic current attibutable to ion-coupled cotransport. In addition to this transport-associated current, a substrate-gated thermodynamically uncoupled anion flux has been identified that has been proposed to dampen neuronal excitability. Arachidonic acid has been reported to modul

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17

Shigeri, Yasushi, Keiko Shimamoto, Yoshimi Yasuda-Kamatani та ін. "Effects of threo-β-hydroxyaspartate derivatives on excitatory amino acid transporters (EAAT4 and EAAT5)". Journal of Neurochemistry 79, № 2 (2008): 297–302. http://dx.doi.org/10.1046/j.1471-4159.2001.00588.x.

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18

Dalet, Antoine, Jérémie Bonsacquet, Sophie Gaboyard-Niay, et al. "Glutamate Transporters EAAT4 and EAAT5 Are Expressed in Vestibular Hair Cells and Calyx Endings." PLoS ONE 7, no. 9 (2012): e46261. http://dx.doi.org/10.1371/journal.pone.0046261.

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19

Torres-Salazar, D., and C. Fahlke. "Intersubunit Interactions in EAAT4 Glutamate Transporters." Journal of Neuroscience 26, no. 28 (2006): 7513–22. http://dx.doi.org/10.1523/jneurosci.4545-05.2006.

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20

Li, Liaoliao, and Zhiyi Zuo. "Glutamate Transporter Type 3 Knockout Reduces Brain Tolerance to Focal Brain Ischemia in MICE." Journal of Cerebral Blood Flow & Metabolism 31, no. 5 (2010): 1283–92. http://dx.doi.org/10.1038/jcbfm.2010.222.

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Excitatory amino-acid transporters (EAATs) transport glutamate into cells under physiologic conditions. Excitatory amino-acid transporter type 3 (EAAT3) is the major neuronal EAAT and also uptakes cysteine, the rate-limiting substrate for synthesis of glutathione. Thus, we hypothesize that EAAT3 contributes to providing brain ischemic tolerance. Male 8-week-old EAAT3 knockout mice on CD-1 mouse gene background and wild-type CD-1 mice were subjected to right middle cerebral artery occlusion for 90 minutes. Their brain infarct volumes, neurologic functions, and brain levels of glutathione, nitro

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21

Cater, Rosemary J., Robert J. Vandenberg, and Renae M. Ryan. "Tuning the ion selectivity of glutamate transporter–associated uncoupled conductances." Journal of General Physiology 148, no. 1 (2016): 13–24. http://dx.doi.org/10.1085/jgp.201511556.

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The concentration of glutamate within a glutamatergic synapse is tightly regulated by excitatory amino acid transporters (EAATs). In addition to their primary role in clearing extracellular glutamate, the EAATs also possess a thermodynamically uncoupled Cl− conductance. This conductance is activated by the binding of substrate and Na+, but the direction of Cl− flux is independent of the rate or direction of substrate transport; thus, the two processes are thermodynamically uncoupled. A recent molecular dynamics study of the archaeal EAAT homologue GltPh (an aspartate transporter from Pyrococcu

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22

Todd, Alison C., and Giles E. Hardingham. "The Regulation of Astrocytic Glutamate Transporters in Health and Neurodegenerative Diseases." International Journal of Molecular Sciences 21, no. 24 (2020): 9607. http://dx.doi.org/10.3390/ijms21249607.

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The astrocytic glutamate transporters excitatory amino acid transporters 1 and 2 (EAAT1 and EAAT2) play a key role in nervous system function to maintain extracellular glutamate levels at low levels. In physiology, this is essential for the rapid uptake of synaptically released glutamate, maintaining the temporal fidelity of synaptic transmission. However, EAAT1/2 hypo-expression or hypo-function are implicated in several disorders, including epilepsy and neurodegenerative diseases, as well as being observed naturally with aging. This not only disrupts synaptic information transmission, but in

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23

Mordrelle, Agnès, Eric Jullian, Cyrille Costa, et al. "EAAT1 is involved in transport ofl-glutamate during differentiation of the Caco-2 cell line." American Journal of Physiology-Gastrointestinal and Liver Physiology 279, no. 2 (2000): G366—G373. http://dx.doi.org/10.1152/ajpgi.2000.279.2.g366.

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Little is known concerning the expression of amino acid transporters during intestinal epithelial cell differentiation. The transport mechanism ofl-glutamate and its regulation during the differentiation process were investigated using the human intestinal Caco-2 cell line. Kinetic studies demonstrated the presence of a single, high-affinity,d-aspartate-sensitive l-glutamate transport system in both confluent and fully differentiated Caco-2 cells. This transport was clearly Na+ dependent, with a Hill coefficient of 2.9 ± 0.3, suggesting a 3 Na+-to-1 glutamate stoichiometry and corresponding to

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24

Hu, Wen-Hui, Winston M. Walters, Xiao-Mei Xia, Shaffiat A. Karmally, and John R. Bethea. "Neuronal glutamate transporter EAAT4 is expressed in astrocytes." Glia 44, no. 1 (2003): 13–25. http://dx.doi.org/10.1002/glia.10268.

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25

Alesutan, Ioana, Oana Ureche, Joerg Laufer, et al. "Regulation of the Glutamate Transporter EAAT4 by PIKfyve." Cellular Physiology and Biochemistry 25, no. 2-3 (2010): 187–94. http://dx.doi.org/10.1159/000276569.

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26

Kolen, Bettina, Daniel Kortzak, Arne Franzen, and Christoph Fahlke. "An amino-terminal point mutation increases EAAT2 anion currents without affecting glutamate transport rates." Journal of Biological Chemistry 295, no. 44 (2020): 14936–47. http://dx.doi.org/10.1074/jbc.ra120.013704.

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Excitatory amino acid transporters (EAATs) are prototypical dual function proteins that function as coupled glutamate/Na+/H+/K+ transporters and as anion-selective channels. Both transport functions are intimately intertwined at the structural level: Secondary active glutamate transport is based on elevator-like movements of the mobile transport domain across the membrane, and the lateral movement of this domain results in anion channel opening. This particular anion channel gating mechanism predicts the existence of mutant transporters with changed anion channel properties, but without altera

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27

Matthews, James C., Mark J. Beveridge, Marc S. Malandro, et al. "Activity and protein localization of multiple glutamate transporters in gestation day 14 vs. day 20 rat placenta." American Journal of Physiology-Cell Physiology 274, no. 3 (1998): C603—C614. http://dx.doi.org/10.1152/ajpcell.1998.274.3.c603.

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Concentrative absorption of glutamate by the developing placenta is critical for proper fetal development. The expression of GLAST1, GLT1, EAAC1, and EAAT4, known to be capable ofd-aspartate-inhibitable and Na+-coupled glutamate transport (system [Formula: see text]), was evaluated in day 14 vs. day 20 rat chorioallantoic placenta. Steady-state mRNA levels were greater at day 20 for all transporters. Immunohistochemistry determined that the expression of GLAST1, GLT1, and EAAC1 was greater throughout the day 20 placenta and was asymmetric with respect to cellular localization. EAAT4 protein wa

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28

Zink, M., B. Vollmayr, P. J. Gebicke-Haerter, and F. A. Henn. "Reduced expression of glutamate transporters vGluT1, EAAT2 and EAAT4 in learned helpless rats, an animal model of depression." Neuropharmacology 58, no. 2 (2010): 465–73. http://dx.doi.org/10.1016/j.neuropharm.2009.09.005.

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29

O'Kane, Robyn L., Itziar Martı́nez-López, Mary R. DeJoseph, Juan R. Viña, and Richard A. Hawkins. "Na+-dependent Glutamate Transporters (EAAT1, EAAT2, and EAAT3) of the Blood-Brain Barrier." Journal of Biological Chemistry 274, no. 45 (1999): 31891–95. http://dx.doi.org/10.1074/jbc.274.45.31891.

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30

Mitrovic, Ann D., Fiona Plesko, and Robert J. Vandenberg. "Zn2+Inhibits the Anion Conductance of the Glutamate Transporter EAAT4." Journal of Biological Chemistry 276, no. 28 (2001): 26071–76. http://dx.doi.org/10.1074/jbc.m011318200.

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31

Yamashita, Akihide, Koshi Makita, Toshihiko Kuroiwa, and Kohichi Tanaka. "Glutamate transporters GLAST and EAAT4 regulate postischemic Purkinje cell death: An in vivo study using a cardiac arrest model in mice lacking GLAST or EAAT4." Neuroscience Research 55, no. 3 (2006): 264–70. http://dx.doi.org/10.1016/j.neures.2006.03.007.

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32

Matott, Michael P., Brian C. Ruyle, Eileen M. Hasser, and David D. Kline. "Excitatory amino acid transporters tonically restrain nTS synaptic and neuronal activity to modulate cardiorespiratory function." Journal of Neurophysiology 115, no. 3 (2016): 1691–702. http://dx.doi.org/10.1152/jn.01054.2015.

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The nucleus tractus solitarii (nTS) is the initial central termination site for visceral afferents and is important for modulation and integration of multiple reflexes including cardiorespiratory reflexes. Glutamate is the primary excitatory neurotransmitter in the nTS and is removed from the extracellular milieu by excitatory amino acid transporters (EAATs). The goal of this study was to elucidate the role of EAATs in the nTS on basal synaptic and neuronal function and cardiorespiratory regulation. The majority of glutamate clearance in the central nervous system is believed to be mediated by

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33

Lin, Chien-Liang Glenn, Anastassios V. Tzingounis, Lin Jin, Akiko Furuta, Michael P. Kavanaugh, and Jeffrey D. Rothstein. "Molecular cloning and expression of the rat EAAT4 glutamate transporter subtype." Molecular Brain Research 63, no. 1 (1998): 174–79. http://dx.doi.org/10.1016/s0169-328x(98)00256-3.

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34

Jackson, Mandy, Wei Song, Mu-Ya Liu, et al. "Modulation of the neuronal glutamate transporter EAAT4 by two interacting proteins." Nature 410, no. 6824 (2001): 89–93. http://dx.doi.org/10.1038/35065091.

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35

Yamada, Keiko, Masahiko Watanabe, Takashi Shibata, Kohichi Tanaka, Keiji Wada, and Yoshiro Inoue. "EAAT4 is a post-synaptic glutamate transporter at Purkinje cell synapses." NeuroReport 7, no. 12 (1996): 2013–17. http://dx.doi.org/10.1097/00001756-199608120-00032.

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36

Kovermann, Peter A., and Christoph Fahlke. "Voltage-dependent Gating Of Wt And D177a Eaat4-associated Anion Channels." Biophysical Journal 96, no. 3 (2009): 472a. http://dx.doi.org/10.1016/j.bpj.2008.12.2429.

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37

Rimaniol, Anne-Cécile, Patricia Mialocq, Pascal Clayette, Dominique Dormont, and Gabriel Gras. "Role of glutamate transporters in the regulation of glutathione levels in human macrophages." American Journal of Physiology-Cell Physiology 281, no. 6 (2001): C1964—C1970. http://dx.doi.org/10.1152/ajpcell.2001.281.6.c1964.

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Cysteine is the limiting precursor for glutathione synthesis. Because of its low bioavailability, cysteine is generally produced from cystine, which may be taken up through two different transporters. The cystine/glutamate antiporter (x[Formula: see text] system) transports extracellular cystine in exchange for intracellular glutamate. The XAG transport system takes up extracellular cystine, glutamate, and aspartate. Both are sensitive to competition between cystine and glutamate, and excess extracellular glutamate thus inhibits glutathione synthesis, a nonexcitotoxic mechanism for glutamate t

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38

Tanaka, Jun, Keiko Yamada, Masahiko Watanabe, Koichii Tanaka, Keiji Wada, and Yoshiro Inoue. "910 Extrasynaptic localization of the glutamate transport EAAT4 at Purkinje cell synapses." Neuroscience Research 28 (January 1997): S113. http://dx.doi.org/10.1016/s0168-0102(97)90300-x.

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39

Itoh, Masayuki, Yukiko Watanabe, Masahiko Watanabe, Kohichi Tanaka, Keiji Wada, and Sachio Takashima. "Expression of a glutamate transporter subtype, EAAT4, in the developing human cerebellum." Brain Research 767, no. 2 (1997): 265–71. http://dx.doi.org/10.1016/s0006-8993(97)00572-6.

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40

Massie, Ann, Frans Vandesande, and Lutgarde Arckens. "Expression of the high-affinity glutamate transporter EAAT4 in mammalian cerebral cortex." Neuroreport 12, no. 2 (2001): 393–97. http://dx.doi.org/10.1097/00001756-200102120-00041.

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41

Tanaka, Jun, Ryoichi Ichikawa, Masahiko Watanabe, Kohichi Tanaka, and Yoshiro Inoue. "Extra-junctional localization of glutamate transporter EAAT4 at excitatory Purkinje cell synapses." NeuroReport 8, no. 11 (1997): 2461–64. http://dx.doi.org/10.1097/00001756-199707280-00010.

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42

Tzingounis, Anastassios V., Chien-Liang Lin, Jeffrey D. Rothstein, and Michael P. Kavanaugh. "Arachidonic Acid Activates a Proton Current in the Rat Glutamate Transporter EAAT4." Journal of Biological Chemistry 273, no. 28 (1998): 17315–17. http://dx.doi.org/10.1074/jbc.273.28.17315.

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43

Miralles, Vicente J., Itziar Martı́nez-López, Rosa Zaragozá, et al. "Na+ dependent glutamate transporters (EAAT1, EAAT2, and EAAT3) in primary astrocyte cultures: effect of oxidative stress." Brain Research 922, no. 1 (2001): 21–29. http://dx.doi.org/10.1016/s0006-8993(01)03124-9.

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44

Yukitake, Motohiro, Jun-ichi Satoh, Shigeru Katamine, and Yasuo Kuroda. "EAAT4 mRNA expression is preserved in the cerebellum of prion protein-deficient mice." Neuroscience Letters 352, no. 3 (2003): 171–74. http://dx.doi.org/10.1016/j.neulet.2003.08.057.

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45

Poulsen, Miguel V., and Robert J. Vandenberg. "Niflumic acid modulates uncoupled substrate‐gated conductances in the human glutamate transporter EAAT4." Journal of Physiology 534, no. 1 (2001): 159–67. http://dx.doi.org/10.1111/j.1469-7793.2001.00159.x.

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Böhmer, Christoph, Michaele Philippin, Jeyaganesh Rajamanickam, et al. "Stimulation of the EAAT4 glutamate transporter by SGK protein kinase isoforms and PKB." Biochemical and Biophysical Research Communications 324, no. 4 (2004): 1242–48. http://dx.doi.org/10.1016/j.bbrc.2004.09.193.

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Huang, Y. H. "Climbing Fiber Activation of EAAT4 Transporters and Kainate Receptors in Cerebellar Purkinje Cells." Journal of Neuroscience 24, no. 1 (2004): 103–11. http://dx.doi.org/10.1523/jneurosci.4473-03.2004.

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Damm-Ganamet, Kelly L., Marie-Laure Rives, Alan D. Wickenden, Heather M. McAllister, and Taraneh Mirzadegan. "A computational approach yields selective inhibitors of human excitatory amino acid transporter 2 (EAAT2)." Journal of Biological Chemistry 295, no. 13 (2020): 4359–66. http://dx.doi.org/10.1074/jbc.ac119.011190.

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Abstract:

Excitatory amino acid transporters (EAATs) represent a protein family that is an emerging drug target with great therapeutic potential for managing central nervous system disorders characterized by dysregulation of glutamatergic neurotransmission. As such, it is of significant interest to discover selective modulators of EAAT2 function. Here, we applied computational methods to identify specific EAAT2 inhibitors. Utilizing a homology model of human EAAT2, we identified a binding pocket at the interface of the transport and trimerization domain. We next conducted a high-throughput virtual scree

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Martinez, Diana, Richard C. Rogers, Eileen M. Hasser, Gerlinda E. Hermann, and David D. Kline. "Loss of excitatory amino acid transporter restraint following chronic intermittent hypoxia contributes to synaptic alterations in nucleus tractus solitarii." Journal of Neurophysiology 123, no. 6 (2020): 2122–35. http://dx.doi.org/10.1152/jn.00766.2019.

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Abstract:

Removal of excitatory amino acid transporter (EAAT) restraint increases spontaneous synaptic activity yet decreases afferent [tractus solitarii (TS)]-driven excitatory postsynaptic current (EPSC) amplitude. In the chronic intermittent hypoxia model of obstructive sleep apnea, this restraint is lost due to reduction in EAAT expression and function. Thus EAATs are important in controlling elevated glutamatergic signaling, and loss of such control results in maladaptive synaptic signaling.

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Fairman, Wendy A., Mark S. Sonders, Geoffrey H. Murdoch, and Susan G. Amara. "Arachidonic acid elicits a substrate-gated proton current associated with the glutamate transporter EAAT4." Nature Neuroscience 1, no. 2 (1998): 105–13. http://dx.doi.org/10.1038/355.

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