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Journal articles on the topic 'Excitatory amino acid transporter 1'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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1

Vandenberg, Robert J., Cheryl A. Handford, Ewan M. Campbell, Renae M. Ryan, and Andrea J. Yool. "Water and urea permeation pathways of the human excitatory amino acid transporter EAAT1." Biochemical Journal 439, no. 2 (2011): 333–40. http://dx.doi.org/10.1042/bj20110905.

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Glutamate transport is coupled to the co-transport of 3 Na+ and 1 H+ followed by the counter-transport of 1 K+. In addition, glutamate and Na+ binding to glutamate transporters generates an uncoupled anion conductance. The human glial glutamate transporter EAAT1 (excitatory amino acid transporter 1) also allows significant passive and active water transport, which suggests that water permeation through glutamate transporters may play an important role in glial cell homoeostasis. Urea also permeates EAAT1 and has been used to characterize the permeation properties of the transporter. We have pr

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2

Canul-Tec, Juan C., Reda Assal, Erica Cirri, et al. "Structure and allosteric inhibition of excitatory amino acid transporter 1." Nature 544, no. 7651 (2017): 446–51. http://dx.doi.org/10.1038/nature22064.

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3

Hediger, M. A., and T. C. Welbourne. "Introduction: Glutamate transport, metabolism, and physiological responses." American Journal of Physiology-Renal Physiology 277, no. 4 (1999): F477—F480. http://dx.doi.org/10.1152/ajprenal.1999.277.4.f477.

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The material covered in this set of articles was originally presented at Experimental Biology ’98, in San Francisco, CA, on April 20, 1998. Here, the participants recount important elements of current research on the role of glutamate transporter activity in cellular signaling, metabolism, and organ function. W. A. Fairman and S. G. Amara discuss the five subtypes of human excitatory amino acid transporters, with emphasis on the EAAT4 subtype. M. A. Hediger discusses the expression and action of EAAC1 subtype of the human excitatory amino acid transporter. I. Nissim provides an overview of the

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4

Gebhardt, Christine, Rafael Körner, and Uwe Heinemann. "Delayed Anoxic Depolarizations in Hippocampal Neurons of Mice Lacking the Excitatory Amino Acid Carrier 1." Journal of Cerebral Blood Flow & Metabolism 22, no. 5 (2002): 569–75. http://dx.doi.org/10.1097/00004647-200205000-00008.

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Hypoxia leads to a rapid increase in vesicular release of glutamate. In addition, hypoxic glutamate release might be caused by reversed operation of neuronal glutamate transporters. An increase in extracellular glutamate concentration might be an important factor in generating anoxic depolarizations (AD) and subsequent neuronal damage. To study the AD and the vesicular release in hippocampal slices from CD1 wild-type mice and mice in which the neuronal glutamate transporter excitatory amino acid carrier 1 (EAAC1) had been knocked out, the authors performed recordings of field potentials and pa

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5

Watzke, Natalie, Thomas Rauen, Ernst Bamberg, and Christof Grewer. "On the Mechanism of Proton Transport by the Neuronal Excitatory Amino Acid Carrier 1." Journal of General Physiology 116, no. 5 (2000): 609–22. http://dx.doi.org/10.1085/jgp.116.5.609.

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Uptake of glutamate from the synaptic cleft is mediated by high affinity transporters and is driven by Na+, K+, and H+ concentration gradients across the membrane. Here, we characterize the molecular mechanism of the intracellular pH change associated with glutamate transport by combining current recordings from excitatory amino acid carrier 1 (EAAC1)–expressing HEK293 cells with a rapid kinetic technique with a 100-μs time resolution. Under conditions of steady state transport, the affinity of EAAC1 for glutamate in both the forward and reverse modes is strongly dependent on the pH on the cis

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Schmidt, Robert W., and Meghan L. Thompson. "Glycinergic signaling in the human nervous system: An overview of therapeutic drug targets and clinical effects." Mental Health Clinician 6, no. 6 (2016): 266–76. http://dx.doi.org/10.9740/mhc.2016.11.266.

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Abstract Glycine and related endogenous compounds (d-serine, d-alanine, sarcosine) serve critical roles in both excitatory and inhibitory neurotransmission and are influenced by a multitude of enzymes and transporters, including glycine transporter 1 and 2 (GlyT1 and GlyT2), d-amino acid oxidase (DAAO), serine racemase (SRR), alanine-serine-cysteine transporter 1 (Asc-1), and kynurenine aminotransferase (KAT). MEDLINE, Web of Science, and PsychINFO were searched for relevant human trials of compounds. Many studies utilizing exogenous administration of small molecule agonists of the glycineB si

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7

Fujita, Hiroko, Kohji Sato, Tong-Chun Wen, Yi Peng, and Masahiro Sakanaka. "Differential Expressions of Glycine Transporter 1 and Three Glutamate Transporter mRNA in the Hippocampus of Gerbils with Transient Forebrain Ischemia." Journal of Cerebral Blood Flow & Metabolism 19, no. 6 (1999): 604–15. http://dx.doi.org/10.1097/00004647-199906000-00003.

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The extracellular concentrations of glutamate and its co-agonist for the N-methyl-d-aspartate (NMDA) receptor, glycine, may be under the control of amino acid transporters in the ischemic brain, However, there is little information on changes in glycine and glutamate transporters in the hippocampal CA1 field of gerbils with transient forebrain ischemia. This study investigated the spatial and temporal expressions of glycine transporter 1 (GLYT 1) and three glutamate transporter (excitatory amino acid carrier 1, EAAC 1; glutamate/aspartate transporter, GLAST; glutamate transporter 1, GLT1) mRNA

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8

Scott, Heather L., David V. Pow, Anthony E. G. Tannenberg, and Peter R. Dodd. "Aberrant Expression of the Glutamate Transporter Excitatory Amino Acid Transporter 1 (EAAT1) in Alzheimer's Disease." Journal of Neuroscience 22, no. 3 (2002): RC206. http://dx.doi.org/10.1523/jneurosci.22-03-j0004.2002.

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9

Meyer, Thomas, Albert C. Ludolph, Markus Morkel, Christian Hagemeier, and Astrid Speer. "Genomic organization of the human excitatory amino acid transporter gene GLT-1." NeuroReport 8, no. 3 (1997): 775–77. http://dx.doi.org/10.1097/00001756-199702100-00039.

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10

Pant, Shashank, and Emad Tajkhorshid. "Modulation of Orientational Dynamics of Excitatory Amino Acid Transporter-1 by Cholesterol." Biophysical Journal 116, no. 3 (2019): 556a. http://dx.doi.org/10.1016/j.bpj.2018.11.2990.

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11

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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12

Gilley, Jennifer A., and Steven G. Kernie. "Excitatory amino acid transporter 2 and excitatory amino acid transporter 1 negatively regulate calcium-dependent proliferation of hippocampal neural progenitor cells and are persistently upregulated after injury." European Journal of Neuroscience 34, no. 11 (2011): 1712–23. http://dx.doi.org/10.1111/j.1460-9568.2011.07888.x.

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13

Wellington, Michael O., Lucas A. Rodrigues, Qiao Li, et al. "Birth Weight and Nutrient Restriction Affect Jejunal Enzyme Activity and Gene Markers for Nutrient Transport and Intestinal Function in Piglets." Animals 11, no. 9 (2021): 2672. http://dx.doi.org/10.3390/ani11092672.

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Significant variation in the birth weight of piglets has arisen due to increased sow prolificacy. Intestinal development and function may be affected by birth weight. Low birth weight (LBW) pigs may also have reduced feed intake, leading to further impairment of intestinal development. The objective of this study was to examine the intestinal development pattern of LBW and normal birth weight (NBW) piglets with normal nutrition (NN) or restricted nutrition (RN) in the pre-weaning period. Jejunal intestinal samples were analyzed for target gene expression and enzyme activity at d 28 (weaning) a

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14

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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15

Münch, Christoph, Birgit Schwalenstöcker, Birgit Knappenberger, et al. "5′-Heterogeneity of the human excitatory amino acid transporter cDNA EAAT2 (GLT-1)." NeuroReport 9, no. 7 (1998): 1295–97. http://dx.doi.org/10.1097/00001756-199805110-00007.

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16

Jensen, Anders A., Mette N. Erichsen, Christina W. Nielsen, Tine B. Stensbøl, Jan Kehler, and Lennart Bunch. "Discovery of the First Selective Inhibitor of Excitatory Amino Acid Transporter Subtype 1." Journal of Medicinal Chemistry 52, no. 4 (2009): 912–15. http://dx.doi.org/10.1021/jm8013458.

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17

Xia, Mi, Lulu Ye, Qihang Hou, and Qinghua Yu. "Effects of arginine on intestinal epithelial cell integrity and nutrient uptake." British Journal of Nutrition 116, no. 10 (2016): 1675–81. http://dx.doi.org/10.1017/s000711451600386x.

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AbstractArginine is a multifaceted amino acid that is critical to the normal physiology of the gastrointestinal tract. Oral arginine administration has been shown to improve mucosal recovery following intestinal injury. The present study investigated the influence of extracellular arginine concentrations on epithelial cell barrier regulation and nutrition uptake by porcine small intestinal epithelial cell line (IPEC-J2). The results show that reducing arginine concentration from 0·7 to 0·2 mm did not affect the transepithelial electrical resistance value, tight-junction proteins (claudin-1, oc

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18

Takarada, T., E. Hinoi, VJ Balcar, H. Taniura, and Y. Yoneda. "Possible expression of functional glutamate transporters in the rat testis." Journal of Endocrinology 181, no. 2 (2004): 233–44. http://dx.doi.org/10.1677/joe.0.1810233.

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Neither expression nor functionality is clear in peripheral tissues with the molecular machineries required for excitatory neurotransmitter signaling by L-glutamate (Glu) in the central nervous system, while a recent study has shown that several Glu receptors are functionally expressed in the rat testis. This fact prompted us to explore the possible functional expression in the rat testis of the Glu transporters usually responsible for the regulation of extracellular Glu concentrations in the brain. RT-PCR revealed the expression, in the rat testis, of mRNA for five different subtypes of Glu t

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19

Napier, Ian A., Sarasa A. Mohammadi, and MacDonald J. Christie. "Glutamate transporter dysfunction associated with nerve injury-induced pain in mice." Journal of Neurophysiology 107, no. 2 (2012): 649–57. http://dx.doi.org/10.1152/jn.00763.2011.

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Dysfunction at glutamatergic synapses has been proposed as a mechanism in the development of neuropathic pain. Here we sought to determine whether peripheral nerve injury-induced neuropathic pain results in functional changes to primary afferent synapses. Signs of neuropathic pain as well as an induction of glial fibrillary acidic protein in immunostained spinal cord sections 4 days after partial ligation of the sciatic nerve indicated the induction of neuropathic pain. We found that following nerve injury, no discernable change to kinetics of dl-α-amino-3-hydroxy-5-methylisoxazole-propionic a

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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

Saha, Kusumika. "Lanthanide-resonance-energy-transfer-based distance measurements in the mammalian glutamate transporter (excitatory amino-acid transporter) 3." Intrinsic Activity 1, Suppl. 1 (2013): A2.3. http://dx.doi.org/10.25006/ia.1.s1-a2.3.

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22

González, Marco I., Bala T. S. Susarla, Keith M. Fournier, Amanda L. Sheldon, and Michael B. Robinson. "Constitutive endocytosis and recycling of the neuronal glutamate transporter, excitatory amino acid carrier 1." Journal of Neurochemistry 103, no. 5 (2007): 1917–31. http://dx.doi.org/10.1111/j.1471-4159.2007.04881.x.

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23

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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24

González, Marco I., Elizabeth Krizman-Genda, and Michael B. Robinson. "Caveolin-1 Regulates the Delivery and Endocytosis of the Glutamate Transporter, Excitatory Amino Acid Carrier 1." Journal of Biological Chemistry 282, no. 41 (2007): 29855–65. http://dx.doi.org/10.1074/jbc.m704738200.

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25

Furuta, Akiko, Mami Noda, Satoshi O. Suzuki, et al. "Translocation of Glutamate Transporter Subtype Excitatory Amino Acid Carrier 1 Protein in Kainic Acid-Induced Rat Epilepsy." American Journal of Pathology 163, no. 2 (2003): 779–87. http://dx.doi.org/10.1016/s0002-9440(10)63705-4.

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26

Bianchi, M. G., G. C. Gazzola, L. Tognazzi, and O. Bussolati. "C6 glioma cells differentiated by retinoic acid overexpress the glutamate transporter excitatory amino acid carrier 1 (EAAC1)." Neuroscience 151, no. 4 (2008): 1042–52. http://dx.doi.org/10.1016/j.neuroscience.2007.11.055.

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27

Ross, John R., Hariharasubramanian Ramakrishnan, Brenda E. Porter, and Michael B. Robinson. "Group I mGluR-regulated translation of the neuronal glutamate transporter, excitatory amino acid carrier 1." Journal of Neurochemistry 117, no. 5 (2011): 812–23. http://dx.doi.org/10.1111/j.1471-4159.2011.07233.x.

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28

Pant, Shashank, Qianyi Wu, Renae Ryan, and Emad Tajkhorshid. "Microscopic Characterization of the Chloride Permeation Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1)." ACS Chemical Neuroscience 13, no. 6 (2022): 776–85. http://dx.doi.org/10.1021/acschemneuro.1c00769.

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29

Tao, F., S. D. Lu, L. M. Zhang, Y. L. Huang, and F. Y. Sun. "Role of excitatory amino acid transporter 1 in neonatal rat neuronal damage induced by hypoxia-ischemia." Neuroscience 102, no. 3 (2001): 503–13. http://dx.doi.org/10.1016/s0306-4522(00)00485-1.

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30

Bianchi, M. G., R. Gatti, L. Torielli, G. Padoani, G. C. Gazzola та O. Bussolati. "The glutamate transporter excitatory amino acid carrier 1 associates with the actin-binding protein α-adducin". Neuroscience 169, № 2 (2010): 584–95. http://dx.doi.org/10.1016/j.neuroscience.2010.05.029.

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31

Beschorner, Rudi, Jens Schittenhelm, Heiko Schimmel, et al. "Choroid plexus tumors differ from metastatic carcinomas by expression of the excitatory amino acid transporter–1." Human Pathology 37, no. 7 (2006): 854–60. http://dx.doi.org/10.1016/j.humpath.2006.02.008.

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32

Waxman, Elisa A., Isabelle Baconguis, David R. Lynch, and Michael B. Robinson. "N-Methyl-d-aspartate Receptor-dependent Regulation of the Glutamate Transporter Excitatory Amino Acid Carrier 1." Journal of Biological Chemistry 282, no. 24 (2007): 17594–607. http://dx.doi.org/10.1074/jbc.m702278200.

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33

Sasaki, S., T. Komori, and M. Iwata. "Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis." Acta Neuropathologica 100, no. 2 (2000): 138–44. http://dx.doi.org/10.1007/s004019900159.

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34

Zhang, Xueshu, Wenjing Ren, Deliang Li, et al. "An excitatory amino acid transporter 1 acts as a novel glutamine transporter and immune modulator in the oyster Crassostrea gigas." International Journal of Biological Macromolecules 310 (May 2025): 143127. https://doi.org/10.1016/j.ijbiomac.2025.143127.

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35

Wang, Jiali, Peifan Li, Xiaozhen Yu, and Christof Grewer. "Observing spontaneous, accelerated substrate binding in molecular dynamics simulations of glutamate transporters." PLOS ONE 16, no. 4 (2021): e0250635. http://dx.doi.org/10.1371/journal.pone.0250635.

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Glutamate transporters are essential for removing the neurotransmitter glutamate from the synaptic cleft. Glutamate transport across the membrane is associated with elevator-like structural changes of the transport domain. These structural changes require initial binding of the organic substrate to the transporter. Studying the binding pathway of ligands to their protein binding sites using molecular dynamics (MD) simulations requires micro-second level simulation times. Here, we used three methods to accelerate aspartate binding to the glutamate transporter homologue Gltph and to investigate

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36

Chen, Zhiqiang, Sharon G. Kujawa, and William F. Sewell. "Functional Roles of High-Affinity Glutamate Transporters in Cochlear Afferent Synaptic Transmission in the Mouse." Journal of Neurophysiology 103, no. 5 (2010): 2581–86. http://dx.doi.org/10.1152/jn.00018.2010.

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In the cochlea, afferent transmission between inner hair cells and auditory neurons is mediated by glutamate receptors. Glutamate transporters located near the synapse and in spiral ganglion neurons are thought to maintain low synaptic levels of glutamate. We analyzed three glutamate transporter blockers for their ability to alter the effects of glutamate, exogenously applied to the synapse via perfusion of the scala tympani of the mouse, and compared that action to their ability to alter the effects of intense acoustic stimulation. Threo-beta-benzyloxyaspartate (TBOA) is a broad-spectrum glut

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37

Zike, Isaac D., Muhammad O. Chohan, Jared M. Kopelman, et al. "OCD candidate gene SLC1A1/EAAT3 impacts basal ganglia-mediated activity and stereotypic behavior." Proceedings of the National Academy of Sciences 114, no. 22 (2017): 5719–24. http://dx.doi.org/10.1073/pnas.1701736114.

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Obsessive-compulsive disorder (OCD) is a chronic, disabling condition with inadequate treatment options that leave most patients with substantial residual symptoms. Structural, neurochemical, and behavioral findings point to a significant role for basal ganglia circuits and for the glutamate system in OCD. Genetic linkage and association studies in OCD point to SLC1A1, which encodes the neuronal glutamate/aspartate/cysteine transporter excitatory amino acid transporter 3 (EAAT3)/excitatory amino acid transporter 1 (EAAC1). However, no previous studies have investigated EAAT3 in basal ganglia c

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38

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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39

Yaster, Myron, Xiaowei Guan, Ronald S. Petralia, Jeffery D. Rothstein, Wei Lu, and Yuan-Xiang Tao. "Effect of Inhibition of Spinal Cord Glutamate Transporters on Inflammatory Pain Induced by Formalin and Complete Freund's Adjuvant." Anesthesiology 114, no. 2 (2011): 412–23. http://dx.doi.org/10.1097/aln.0b013e318205df50.

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Background Spinal cord glutamate transporters clear synaptically released glutamate and maintain normal sensory transmission. However, their ultrastructural localization is unknown. Moreover, whether and how they participate in inflammatory pain has not been carefully studied. Methods Immunogold labeling with electron microscopy was carried out to characterize synaptic and nonsynaptic localization of glutamate transporters in the superficial dorsal horn. Their expression and uptake activity after formalin- and complete Freund's adjuvant (CFA)-induced inflammation were evaluated by Western blot

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Hung, Victor K. L., Lydia W. Tai, Xin Luo, Xiao Min Wang, Sookja K. Chung, and Chi Wai Cheung. "Targeted Overexpression of Astrocytic Endothelin-1 Attenuates Neuropathic Pain by Upregulating Spinal Excitatory Amino Acid Transporter-2." Journal of Molecular Neuroscience 57, no. 1 (2015): 90–96. http://dx.doi.org/10.1007/s12031-015-0581-y.

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Karki, Pratap, Clifford Kim, Keisha Smith, Deok-Soo Son, Michael Aschner та Eunsook Lee. "Transcriptional Regulation of the Astrocytic Excitatory Amino Acid Transporter 1 (EAAT1) via NF-κB and Yin Yang 1 (YY1)". Journal of Biological Chemistry 290, № 39 (2015): 23725–37. http://dx.doi.org/10.1074/jbc.m115.649327.

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42

Chrétien, Fabrice, Gwenaelle Le Pavec, Anne-Valérie Vallat-Decouvelaere, et al. "Expression of Excitatory Amino Acid Transporter-1 (EAAT-1) in Brain Macrophages and Microglia of Patients with Prion Diseases." Journal of Neuropathology & Experimental Neurology 63, no. 10 (2004): 1058–71. http://dx.doi.org/10.1093/jnen/63.10.1058.

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43

Igarashi, Kiharu, Makiko Takagi, and Yoichi Fukushima. "The Effects of Matcha and Decaffeinated Matcha on Learning, Memory and Proteomics of Hippocampus in Senescence-Accelerated (SAMP8) Mice." Nutrients 14, no. 6 (2022): 1197. http://dx.doi.org/10.3390/nu14061197.

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Although the benefits of the consumption of green tea and its components, including catechins and theanine, regarding aging, memory impairment and age-related cognitive decline have been investigated in senescence-accelerated prone mice (SAMP8), studies that simultaneously measured the kinds of proteins that vary in their expression due to the administration of green tea and its extracts were not found. In this study, the effect of dietary and decaffeinated matcha on protein expression in the hippocampus of SAMP 8 was examined comprehensively, mainly using proteomics. Although improvements in

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44

Takahashi, Kanako, Yuto Ishibashi, Kaori Chujo, Ikuro Suzuki, and Kaoru Sato. "Neuroprotective Potential of L-Glutamate Transporters in Human Induced Pluripotent Stem Cell-Derived Neural Cells against Excitotoxicity." International Journal of Molecular Sciences 24, no. 16 (2023): 12605. http://dx.doi.org/10.3390/ijms241612605.

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Human induced pluripotent stem cell (hiPSC)-derived neural cells have started to be used in safety/toxicity tests at the preclinical stage of drug development. As previously reported, hiPSC-derived neurons exhibit greater tolerance to excitotoxicity than those of primary cultures of rodent neurons; however, the underlying mechanisms remain unknown. We here investigated the functions of L-glutamate (L-Glu) transporters, the most important machinery to maintain low extracellular L-Glu concentrations, in hiPSC-derived neural cells. We also clarified the contribution of respective L-Glu transporte

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Hu, Hui-Juan, and Robert W. Gereau. "Metabotropic glutamate receptor 5 regulates excitability and Kv4.2-containing K+ channels primarily in excitatory neurons of the spinal dorsal horn." Journal of Neurophysiology 105, no. 6 (2011): 3010–21. http://dx.doi.org/10.1152/jn.01050.2010.

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Metabotropic glutamate (mGlu) receptors play important roles in the modulation of nociception. Previous studies demonstrated that mGlu5 modulates nociceptive plasticity via activation of ERK signaling. We have reported recently that the Kv4.2 K+ channel subunit underlies A-type currents in spinal cord dorsal horn neurons and that this channel is modulated by mGlu5-ERK signaling. In the present study, we tested the hypothesis that modulation of Kv4.2 by mGlu5 occurs in excitatory spinal dorsal horn neurons. With the use of a transgenic mouse strain expressing enhanced green fluorescent protein

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Lee, Minwoo, Dong Gyun Ko, Dae Ki Hong, Man-Sup Lim, Bo Young Choi, and Sang Won Suh. "Role of Excitatory Amino Acid Carrier 1 (EAAC1) in Neuronal Death and Neurogenesis After Ischemic Stroke." International Journal of Molecular Sciences 21, no. 16 (2020): 5676. http://dx.doi.org/10.3390/ijms21165676.

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Although there have been substantial advances in knowledge regarding the mechanisms of neuron death after stroke, effective therapeutic measures for stroke are still insufficient. Excitatory amino acid carrier 1 (EAAC1) is a type of neuronal glutamate transporter and considered to have an additional action involving the neuronal uptake of cysteine, which acts as a crucial substrate for glutathione synthesis. Previously, our lab demonstrated that genetic deletion of EAAC1 leads to decreased neuronal glutathione synthesis, increased oxidative stress, and subsequent cognitive impairment. Therefor

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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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Zheng, Shuang, Wen Xie, Longcai Fei, and Nannan Zhu. "Research on the Relationship Between Schizophrenia and Excitatory Amino Acid Transporter 1 Gene Based on Nanogold Amplification Technology." Journal of Nanoscience and Nanotechnology 21, no. 2 (2021): 1278–85. http://dx.doi.org/10.1166/jnn.2021.18659.

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Schizophrenia is one of the most common central nervous system diseases, which is caused by abnormal discharge of neurons in the brain. Its occurrence and development are affected by both genetic and environmental factors. The variation of gene level can affect the development of schizophrenia and the treatment of prognosis by affecting the susceptibility, clinical phenotype and drug response. At present, the research results of susceptibility genes screened by candidate gene association research are not consistent. The method of gene recognition on DNA was studied by QCM and nano gold composi

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He, Suifen, Wenlong Zhang, Xiuping Zhang, Pingyi Xu, Mei Hong, and Shaogang Qu. "The 4b-4c loop of excitatory amino acid transporter 1 containing four critical residues essential for substrate transport." Journal of Biomolecular Structure and Dynamics 38, no. 12 (2019): 3599–609. http://dx.doi.org/10.1080/07391102.2019.1664935.

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Vallejo-Illarramendi, Ainara, Maria Domercq, and Carlos Matute. "A novel alternative splicing form of excitatory amino acid transporter 1 is a negative regulator of glutamate uptake." Journal of Neurochemistry 95, no. 2 (2005): 341–48. http://dx.doi.org/10.1111/j.1471-4159.2005.03370.x.

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