Cited by 450Amino Acid Enzymes and MetabolismNeuroscience and Neuropharmacology ResearchIon Transport and Channel Regulation

The DOI matches its Crossref record.

The glutamate/neutral amino acid transporter family SLC1: molecular, physiological and pharmacological aspects

Kanai, Yoshikatsu, Hediger, Matthias A.·2004·Pfl�gers Archiv European Journal of Physiology

DOI 10.1007/s00424-003-1146-4

Open this paper in CoChat — free account

Abstract

The solute carrier family 1 (SLC1) includes five high-affinity glutamate transporters, EAAC1, GLT-1, GLAST, EAAT4 and EAAT5 (SLC1A1, SLC1A2, SLC1A3, SLC1A6, and SLC1A7, respectively) as well as the two neutral amino acid transporters, ASCT1 and ASCT2 (SLC1A4 and ALC1A5, respectively). Although each of these transporters have similar predicted structures, they exhibit distinct functional properties which are variations of a common transport mechanism. The high-affinity glutamate transporters mediate transport of l-Glu, l-Asp and d-Asp, accompanied by the cotransport of 3 Na(+) and 1 H(+), and the countertransport of 1 K(+), whereas ASC transporters mediate Na(+)-dependent exchange of small neutral amino acids such as Ala, Ser, Cys and Thr. The unique coupling of the glutamate transporters allows uphill transport of glutamate into cells against a concentration gradient. This feature plays a crucial role in protecting neurons against glutamate excitotoxicity in the central nervous system. During pathological conditions, such as brain ischemia (e.g. after a stroke), however, glutamate exit can occur due to "reversed glutamate transport", which is caused by a reversal of the electrochemical gradients of the coupling ions. Selective inhibition of the neuronal glutamate transporter EAAC1 (SLC1A1) may be of therapeutic interest to block glutamate release from neurons during ischemia. On the other hand, upregulation of the glial glutamate transporter GLT1 (SLC1A2) may help protect mot…

Integrity signals

Registry

Crossref · 10.1007/s00424-003-1146-4

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Sorted by citations

Items 301–395 of 395

Comparative transcriptome analyses reveal changes of gene expression in larvae hatched from fresh and cryopreserved kelp grouper (Epinephelus moara) embryos
Zhang, J.-J., Tian, Y., Wang, L.-N., Li, Z.-T., Wu, Y.-P., Li, Z., Ma, W., & Zhai, J. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2021.737459 · Cited by 6
L-Cysteine-mediated modulation of copper trafficking in prostate cancer cells: an in vitro and in vivo investigation with 64Cu and 64Cu-PET.
Bartnicka, J., Salemee, F. A., Firth, G., & Blower, P. (2020) · Metallomics · doi:10.1039/d0mt00161a · Cited by 6
Genetically-encoded halide sensor-based fluorescent assay for rapid screening of glutamate transport and inhibition.
Zielewicz, L., & Grewer, C. (2019) · ACS Sensors · doi:10.1021/acssensors.9b00944 · Cited by 6
Paired-Cysteine Scanning Reveals Conformationally Sensitive Proximity between the TM4b-4c Loop and TM8 of the Glutamate Transporter EAAT1
Qu, S., Zhang, W., He, S., & Zhang, X. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00048 · Cited by 8
Effects of alanyl-glutamine supplementation on the small intestinal mucosa barrier in weaned piglets challenged with lipopolysaccharide
Xing, S., Zhang, B.-L., Lin, M., Li, J.-L., Zhang, L., Gao, F., & Zhou, G.-H. (2017) · Canadian Journal of Animal Science · doi:10.1139/cjas-2016-0039 · Cited by 6
“In addition, the absorption of Gln depends on the amino acid transporters (Kanai and Hediger 2004).”
Background
Na+-dependent Neutral Amino Acid Transporter ASCT2 Is Downregulated in Seriously Traumatized Human Intestinal Epithelial Cells
Huang, Q., Li, N., Zhang, W., Zhu, W., Li, Q.-R., Wang, B., & Li, J.-S. (2008) · Journal of Pediatric Gastroenterology and Nutrition - JPGN · doi:10.1097/01.mpg.0000304457.22670.6f · Cited by 6
“ASCT2 also takes up glutamine with high affinity and accepts a wide panel of other amino acids with longer side chains (asparagine, leucine, and isoleucine) (25).”
Background
Chlorpromazine, clozapine and olanzapine inhibit anionic amino acid transport in cultured human fibroblasts
Marchesi, C., Dall’Asta, V., Rotoli, B., Bianchi, M., Maggini, C., Gazzola, G., & Bussolati, O. (2006) · Amino Acids · doi:10.1007/s00726-006-0312-3 · Cited by 6
“These three transporters present overlapping substrate specificities and similar operational features, although EAAT2, a transporter predominantly expressed in glial models, is peculiarly sensitive to the inhibition by dihydrokainate and kainate ( Kanai and Hediger, 2004 ).”
Background
Effects of glutamate transporter and receptor ligands on neuronal glutamate uptake.
Boeck, C., Kroth, E., Bronzatto, M., Jardim, F. M., Souza, D., & Vendite, D. (2005) · Neurosciences research · doi:10.1016/j.neures.2005.06.003 · Cited by 6
Chemical and Synthetic Approaches in Membrane Biology
Shukla, A. (2017) · Springer Protocols Handbooks · doi:10.1007/978-1-4939-6836-7 · Cited by 6
“In addition, metal nanoparticles have unique optical and electronic properties that allow detection of proteinmembrane interactions in solution [10, 11].”
Background
GABA and glutamate transporters: new events and function in the vertebrate retina
Nascimento, J. L. M. D., Sawada, L. A., Oliveira, K., Crespo-López, M., da Silva, A. O., Hamoy, M., Silva, C., Bastos, G., & Soeiro-Pantoja, W. M. (2013) · doi:10.3922/j.psns.2013.2.03 · Cited by 6
“In the CNS, excitatory amino acid transporters (EAATs) are the main transporters responsible for removal of the glutamate neurotransmitter, maintaining its extracellular concentration below excitotoxic levels (Pines et al., 1992; Danbolt, 2001; Balcar, 2002; Kanai & Hediger, 2004).”
Background
Spectrum and functions of ion channels and transporters in osteoclasts
Chen, H., Zhang, Y., Zhu, Y., Xiao, X., Huang, S., & Duan, X. (2026) · Bone Research · doi:10.1038/s41413-026-00513-9 · Cited by 4
Amino acid influx via LAT1 regulates iron demand and sensitivity to PPMX-T003 of aggressive natural killer cell leukemia
Yanagiya, R., Miyatake, Y., Watanabe, N., Shimizu, T., Kanamori, A., Ueno, M., Okabe, S., Carreras, J., Nakayama, S., Hasegawa, A., et al. (2024) · Leukemia · doi:10.1038/s41375-024-02296-6 · Cited by 5
“LAT1 is a cancer-speci ﬁ c large neutral amino acid transporter that can transport methionine [26, 27], whereas ASCT2 is annotated as a cysteine transporter [28].”
ASCT2 is the primary serine transporter in cancer cellsPreprint
Conger, K. O., Chidley, C., Ozgurses, M., Zhao, H., Kim, Y., Semina, S. E., Burns, P. A., Rawat, V., Sheldon, R., Ben-Sahra, I., et al. (2023) · bioRxiv · doi:10.1101/2023.10.09.561530 · Cited by 5
Effects of Dietary Energy and Protein Levels on Free Force-Feed Peking Ducks
Wu, Y.-Q., Liu, J., Shahid, M., Xiao, Z., Dong, X.-Y., Yin, D., & Yuan, J.-M. (2019) · Journal of Applied Poultry Research · doi:10.3382/japr/pfz011 · Cited by 5
Electrical excitability of taste cells. Mechanisms and possible physiological significance
Romanov, R. A., Rogachevskaja, O. A., Bystrova, M. F., & Kolesnikov, S. S. (2012) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747812010126 · Cited by 4
“Moreover, NTPD2 is apparently co expressed with the glutamate/aspartate transporter GLAST [72] that is responsible for glutamate clearance by glial cells [73,74].”
Background
Pharmacological characterization of glutamate Na+-independent transport in retinal cell cultures: implications in the glutathione metabolism.
Oliveira, K., Herculano, A., Crespo-López, M., & Nascimento, J. L. D. D. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2009.09.002 · Cited by 5
Amino Acid Transport in Plants and Transport of Neurotransmitters in Animals: a Common Mechanism?
Müller, T., Koch, W., & Wipf, D. (2006) · doi:10.1007/978-3-540-28516-8_11 · Cited by 5
“The SLC1 family comprises five high-affinity glutamate transporters (systemXAG)SLCA1(EAAC1,EAAT3),SLC1A2(GlT1,EAAT2),SLC1A3(GLAST, EAAT1), SLC1A6 (EAAT4) and SLC1A7 (EAAT5) and two neutral AA transporters (system ASC) SLC1A4 (ASCT1, SATT) and SLC1A5 (ASCT2, AAAT, hATB0) (Kanai and Hediger 2004).”
BackgroundInfluential
Satellite glial cell manipulation prior to axotomy enhances developing dorsal root ganglion central branch regrowth into the spinal cord
Brown, R. I., Barber, H. M., & Kucenas, S. (2024) · Glia · doi:10.1002/glia.24581 · Cited by 6
“…identity at this developmental stage was further confirmed by lack of macrophage characteristics (Figure S2) and by fluorophore expression driven by slc1a3b (Figure S3), an ortholog of the known SGC marker SLC1A3 (Kanai & Hediger, 2004; Mapps, Thomsen, et al., 2022; Tasdemir-Yilmaz et al., 2021).”
A Comprehensive Review of Membrane Transporters and MicroRNA Regulation in Alzheimer’s Disease
Mishra, S., Stany, B. K., Das, A., Deepankumar, K., & Vijayan, M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04135-2 · Cited by 5
“…of the glutamate transmitter [75] EAAT-1 Belongs to the SLC1 family, and enables, synaptic transmission by regulatory glutamate receptor activation [162] EAAT-2 Belongs to the SLC1 family, and enables, synaptic transmission by regulatory glutamate receptor activation [162] EAAT-3 Belongs to the…”
CircMAT2B facilitates the progression of head and neck squamous cell carcinoma via sponging miR-491-5p to trigger ASCT2-mediated glutaminolysis
Luo, J., Wang, Y., Wang, Y., Wang, C., Liu, R., & Zhang, Z. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04565-3 · Cited by 4
“Based on the bioinformatics analysis, we found the putative complementary binding sites between miR-491-5p and Alanine, serine, cysteine-preferring transporter 2 (ASCT2), which was identified to be a cell surface solute-carrying transporter essential for glutamine [35].”
Background
Molecular Characterization and Nutrition Regulation of the Neutral Amino Acid Transporter ASCT2 in Triploid Crucian Carp
Mao, Z., Luo, S., Zhao, D., Zhou, X., Zhang, Z.-L., Xiao, Y., Cao, S., Zhou, Y., Liu, S.-J., Tang, J.-Z., et al. (2021) · Fishes · doi:10.3390/fishes6040077 · Cited by 4
“reported that glutamate was also one of the transport substrates of ASCT2 [16].”
Background
Expression of nutrient transporter genes in response to dietary rice gluten meal and protease enzyme supplementation and the consequent effects on growth, nutrient digestibility, immunity and jejunum histomorphometry in chicken
Wani, M., Tyagi, P., Begum, J., Mir, N., Dev, K., Biswas, A., Sharma, D., & Goel, A. (2021) · Animal Biotechnology · doi:10.1080/10495398.2021.1924182 · Cited by 4
Interaction of the neutral amino acid transporter ASCT2 with basic amino acids
Ndaru, E., Garibsingh, R., Zielewicz, L., Schlessinger, A., & Grewer, C. (2020) · Biochemical Journal · doi:10.1042/bcj20190859 · Cited by 4
Substrate-Induced Motion between TM4 and TM7 of the Glutamate Transporter EAAT1 Revealed by Paired Cysteine Mutagenesis
Zhang, W.-L., Zhang, X.-P., & Qu, S.-G. (2018) · Molecular Pharmacology · doi:10.1124/mol.118.113183 · Cited by 4
Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis
Leidenheimer, N. J. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00245 · Cited by 4
“In an analogous argument made above for GABA/GABAA receptors, it is likely that ER-localized glutamate would be found at sufficient concentrations for binding nascent glutamate receptors since the intracellular glutamate concentrations are estimated to be in the low mM range (Kanai and Hediger, 2004), glutamate is con…”
Background
Modulation of intestinal L-glutamate transport by luminal leptin
Fanjul, C., Barrenetxe, J., Lostao, M., & Ducroc, R. (2015) · Journal of physiology and biochemistry · doi:10.1007/s13105-015-0414-z · Cited by 4
Broad Integration of Expression Maps and Co-Expression Networks Compassing Novel Gene Functions in the Brain
Okamura-Oho, Y., Shimokawa, K., Nishimura, M., Takemoto, S., Sato, A., Furuichi, T., & Yokota, H. (2014) · Scientific Reports · doi:10.1038/srep06969 · Cited by 4
“The graph included genes encoding molecules that are highly expressed in adult Purkinje cells, such as a morphogen, Wnt3 29 and a glutamate transporter, Slc1a6 30 , in addition to genes encoding the Wnt receptor Fzd1, the transcription factor En2, which regulates the morphological and molecular patterning of the embry…”
Background
Substrate-dependent Interference of Carbonic Anhydrases with the Glutamine Transporter SNAT3-Induced Conductance
Weise, A., Schneider, H., McKenna, R., & Deitmer, J. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000325208 · Cited by 4
Existence of an endogenous glutamate and aspartate transporter in Chinese hamster ovary cells.
Ji, X.-H., Jin, Y., Chen, Y., Li, C., & Guo, L.-H. (2007) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2007.00354.x · Cited by 4
4.7 Ion Transport and Energy Metabolism
Vergun, O., Dineley, K., & Reynolds, I. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_16 · Cited by 4
Adaptively increased intake of arginine sustains oral keratinocyte survival through alleviating oxidative stress during targeting glutamine metabolism
Lv, C., He, H., Mi, L., Li, W., Mu, W., Cheng, B., & Tao, X. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117165 · Cited by 4
Chronic social defeat stress induces the down‐regulation of the Nedd4L‐GLT ‐1 ubiquitination pathway in the prefrontal cortex of mice
Kosuge, A., Kunisawa, K., Iida, T., Wulaer, B., Kawai, T., Tanabe, M., Saito, K., Nabeshima, T., & Mouri, A. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16100 · Cited by 3
“The glutamate transporter GLT-1 plays an important role in the maintenance of homeostasis for glu - tamatergic transmission within synapses (Kanai & Hediger, 2004 ).”
Genetic factors underlying host resistance to Rhipicephalusmicroplus tick infestation in Braford cattle: a systems biology perspective
Carvalho, W. A., Gaspar, E. B., Domingues, R., Regitano, L. C. A., & Cardoso, F. (2024) · Mammalian Genome · doi:10.1007/s00335-024-10030-x · Cited by 3
Amino Acid Transporters Proteins Involved in the Glutamate-Glutamine Cycle and Their Alterations in Murine Models of Alzheimer’s Disease
Vázquez-Durán, D. L., Ortega, A., & Rodríguez, A. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-03966-3 · Cited by 4
“…mediate the Na + -dependent uni-directional cotransport of neutral amino acids into the cell interior; whereas the remaining five, Slc1a1, Slc1a2, Slc1a3, Slc1a6, and Slc1a7, cotransport into the cell one Glu or Asp molecule with three Na + molecules and one H + while releasing one K + [35–38].”
Structural basis for the transport mechanism of the human glutamine transporter SLC1A5 (ASCT2)
Yu, X., Plotnikova, O., Bonin, P., Subashi, T., McLellan, T. J., Dumlao, D., Che, Y., Dong, Y., Carpenter, E., West, G. M., et al. (2019) · bioRxiv · doi:10.1101/622563 · Cited by 3
“SLC1A5 (ASCT2) catalyzes an obligatory Na+-dependent antiport in which Na+ together with an extracellular neutral amino acid are exchanged with an intracellular neutral amino acid (1, 2).”
Background
SLC1A1 Gene Variants and Normal Tension Glaucoma: An Association Study
真美, 西., Meguro, A., Nomura, E., Yamane, T., Takeuchi, M., Ôta, M., Kashiwagi, K., Mabuchi, F., Iijima, H., Kawase, K., et al. (2016) · Ophthalmic Genetics · doi:10.3109/13816810.2015.1028649 · Cited by 4
“Among these, EAAT1 and EAAT2 are dominant transporter types.(30) A”
Background
Distribution of glutamate transporter 1 mRNA in the central nervous system of the pigeon (Columba livia).
Atoji, Y., & Islam, M. (2009) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2009.03.002 · Cited by 3
The Reciprocal Effects of Oxidative Stress and Glutamate Neurotransmission
Grignon, S., & Deslauriers, J. (2014) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-4939-0440-2_11 · Cited by 9
Sodium Signals and Their Significance for Axonal Function
Kelly, T., & Rose, C. (2010) · Springer eBooks · doi:10.1007/978-1-4419-1676-1_3 · Cited by 3
“The localisation of Na+-dependent transporters responsible for transmitter uptake into presynaptic terminals (Chen et al., 2004; Kanai and Hediger, 2004) provides”
Transport of nonessential metals across mammalian cell membranes
Ballatori, N., & Madejczyk, M. S. (2005) · Topics in current genetics · doi:10.1007/4735_102 · Cited by 4
Segment-Dependent Gene Expression Profiling of the Cartilaginous Fish Nephron Using Laser Microdissection for Functional Characterization of Nephron at Segment Levels
Horie, T., Takagi, W., Aburatani, N., Yamazaki, M., Inokuchi, M., Tachizawa, M., Okubo, K., Ohtani-Kaneko, R., Tokunaga, K., Wong, M., et al. (2023) · Zoological Science · doi:10.2108/zs220092 · Cited by 2
“Slc1a3 is a glial-type glutamate transporter (also known as a glutamate-aspartate transporter, GLAST, or an excitatory amino acid transporter, EAAT1) abundantly expressed in the cerebellum in mammals (Kanai and Hediger, 2004).”
Background
Recent progress of amino acid transporters as a novel antitumor target
Zhao, J.-Y., Lv, J., Chen, Y., Dong, Q., & Dong, H.-R. (2022) · Open Chemistry · doi:10.1515/chem-2022-0239 · Cited by 2
Glutamate and glutamine transporter genes in grass carp (Ctenopharyngodon idellus): Molecular cloning, characterization and expression in response to different stocking densities
Liang, X. H., Fang, T., Yan, F., Xu, W., Onxayvieng, K., Tang, R., Li, L., Zhang, X., Chi, W., & Li, D. (2020) · Aquaculture Research · doi:10.1111/are.14755 · Cited by 2
Thermodynamic first law efficiency of membrane proteins
Gür, M., Gölcük, M., Yilmaz, S. Z., & Taka, E. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1577759 · Cited by 2
“In neurons, the intracellular glutamate concentration is frequently taken as 10 mM (Jong & O’Malley, 2017; Kanai & Hediger, 2004) and approximately ranges between 5 and 10 mM (Featherstone, 2010; Schwartzkroin, 2009).”
Background
Transcriptome analysis and gene networks in a rare pediatric tumor
Leite, M., Vanin, E., Iannaccone, S., da Cunha, N. D., de Alencar, S. D., & Costa, F. (2019) · Biotechnology Research & Innovation · doi:10.1016/j.biori.2019.08.002 · Cited by 2
Apical Na+-dependent neutral amino acid exchanger ASCT2/ATB0 and mTOR-signaling components are expressed along the entire jejunal crypt–villus axis in young pigs fed a liquid milk replacer
Yang, C.-B., Yang, X., & Fan, M. (2016) · Canadian Journal of Animal Science · doi:10.1139/cjas-2016-0021 · Cited by 2
Tumor necrosis factor-α suppresses the protein fractional synthesis rate of the small intestine stimulated by glutamine in rats
Zhou, J.-H., Fan, S.-X., Cao, Y.-C., Zhu, M.-F., Han, Y., Cao, X., & Li, Y.-S. (2014) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2014.2129 · Cited by 2
Kidney transport of amino acids and oligopeptides, and aminoacidurias
Camargo, S., Makrides, V., Kleta, R., & Verrey, F. (2013) · doi:10.1016/b978-0-12-381462-3.00071-9 · Cited by 2
Intracellular pH regulation in unstimulated Calliphora salivary glands is Na+ dependent and requires V-ATPase activity
Schewe, B., Blenau, W., & Walz, B. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.063172 · Cited by 2
“, 1992) but is also expressed in peripheral tissues (Kanai and Hediger, 2004; Berger and Hediger, 2006).”
Background
Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin
Ikemoto, M., & Arano, T. (2012) · InTech eBooks · doi:10.5772/33889 · Cited by 2
“…function have lead to a greater appreciation of the physiological and pathophysiological relevance of EAAC1 (Aoyama et al., 2008b; Danbolt, 2001; Kanai & Hediger, 2004; Nieoullon et al., 2006), but there are many issues to be resolved for a thorough understanding of the significance of EAAC1 in…”
Background
L-glutamate: A modern view on a well-known amino acid
Kurbat, M. N. (2009) · Neurochemical Journal · doi:10.1134/s1819712409030039 · Cited by 2
Cell‐Surface Transmitter Transporters
Alexander, S. P. H., Mathie, A., & Peters, J. (2007) · doi:10.1038/sj.bjp.0707207 · Cited by 2
“In addition, a thermodynamically uncoupled Cl- flux, activated by Naþ and glutamate (Kanner & Borre, 2002; Kanai & Hediger, 2003; 2004), is sufficiently large, in the instances of EAAT4 and EAAT5, to influence neuronal excitability.”
Background
Glutamine Uptake and Immunomodulation: An Overview
Frauwirth, K. A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1932-1_4 · Cited by 5
“(2004) [ 18 ] and Mackenzie et al.”
Background
Amino acid metabolism in Chinese hamster ovary cell culture
Kyriakopoulos, S. (2014) · Spiral (Imperial College London) · doi:10.25560/25143 · Cited by 2
Measuring Electroneutral Chloride-Dependent Ion Fluxes in Mammalian Cells and in Heterologous Expression Systems
Gagnon, K. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-374373-2.00009-1 · Cited by 2
CHAPTER 72 – Amino Acids, Oligopeptides, and Hyperaminoacidurias
Silbernagl, S., & Gekle, M. (2008) · doi:10.1016/b978-012088488-9.50075-9 · Cited by 2
Lactate signaling and lactylation in retina: From physiological Warburg effect to pathological metabolic reprogramming
Gu, X., Zhuang, A., Fan, J., Wen, X., Yang, L., Jia, R., Chai, P., & Fan, X. (2026) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2026.101509 · Cited by 1
Chronic social instability stress differentially affects the behavior and the transcriptome of the anterodorsal bed nucleus of the stria terminalis between male and female micePreprint
Degroat, T. J., Moran, K. M., Denney, K., Paladino, S. E., Yasrebi, A., Knox, N., Samuels, B., & Roepke, T. A. (2025) · bioRxiv · doi:10.1101/2025.01.21.634142 · Cited by 1
“…receptor (Kurnik et al., 2006); Crh (log2FC = -0.5179, adj. p = 0.0035); Slc1a6 (log2FC = -0.4621, adj. p = 0.0370), a glutamate transporter (Kanai and Hediger, 2004); and Gabra3 (log2FC = 0.6295, adj. p < 0.0001) , a GABA A receptor subunit implicated in depression-like behaviors in mice…”
Influential
Advancing Obsessive–Compulsive Disorder Research: Insights from Transgenic Animal Models and Innovative Therapies
Huang, X., Xiao, L., Wang, M., Wu, Y., Deng, H., & Wang, W. (2025) · Brain Sciences · doi:10.3390/brainsci15010043 · Cited by 1
Transient kinetics reveal the mechanism of competitive inhibition of the neutral amino acid transporter ASCT2
Dong, Y., Wang, J., & Grewer, C. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107382 · Cited by 1
“CRL 1573) were cultured as described previously (47, 48). rASCT2 or EAAC1 complementary DNAs constructs inserted in the pBK-CMV vector were transiently transfected into cells using jet-PRIME transfection reagent.”
Prognostic stratification based on HIF-1α signaling for evaluating hypoxia status and immune landscape in hepatocellular carcinoma
Zhuang, H., Zhang, Z.-D., Chen, B., Tang, C.-W., Chen, X.-M., Tan, W.-L., Yang, L., Xie, Z.-Q., Ma, X.-W., Wang, Q.-B., et al. (2023) · Journal of Big Data · doi:10.1186/s40537-023-00752-1 · Cited by 1
“SLC1A5 is a critical glutamine transporter in malignancies, and activation of which captures huge amounts of glutamine [55, 56].”
Background
SLC1 family of amino acid transporters in GtoPdb v.2023.1
Beart, P. M. (2023) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f139/2023.1 · Cited by 1
“Bröer A, Brookes N, Ganapathy V, Dimmer KS, Wagner CA, Lang F and Bröer S. (1999) The astroglial ASCT2 amino acid transporter as a mediator of glutamine efflux.”
BackgroundInfluential
Excitotoxicity and Glaucoma
Ishikawa, M., Yoshitomi, T., & Izumi, Y. (2014) · doi:10.5772/57605 · Cited by 1
“GLAST GLAST is the prominent glutamate transporter in the retina, and mainly expressed in the Müller cells [10, 31-33, 39, 40].”
Background
The Glia Connection of the Glutamate/Glutamine Shuttle
Rodríguez, A., & Ortega, A. (2012) · Neuroscience International · doi:10.3844/amjnsp.2012.32.38 · Cited by 1
ENZYMES
Alexander, S., Mathie, A. A., & Peters, J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01649_9.x · Cited by 2
“…acid transporters Overview: The SLC1 family of sodium dependent transporters includes the plasma membrane located glutamate transporters and the neutral amino acid transporters ASCT1 and ASCT2 (Amara and Arriza, 1993; Palacín et al., 1998; Kanai and Hediger, 2003; 2004; Beart and O’Shea, 2007).”
Background
Glutamate Plasticity in an Animal Model of Parkinson’s Disease
Meshul, C. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-252-0_13 · Cited by 1
“6) [64–66].”
Background
Multifaceted In Silico and DFT-Based Analysis of 2‑Aminosuccinic Acid on Ferroptosis-Related Targets
Kebiroğlu, M. H., Azarkan, S. Y., & Çankaya, N. (2026) · ACS Omega · doi:10.1021/acsomega.6c02875
Overactive EAAT1 Cl− channels impair GABAergic tonic inhibition in SLC1A3-associated episodic ataxia
Kostritskaia, Y., Bulla-Miely, D., Engels, M., Meyer, J., Berns, J. L., Behuet, S., Bludau, S., Rose, C. R., Becker, A. J., Gensch, T., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02399-4
“Since EAAT1/GLAST is exclusively expressed in glial cells and not in neurons [31, 50], with a high expression in DG RGLs [15], a direct impact on DG granule cell excitability is not expected.”
Characteristic expression patterns of PROX1, GLAST, GFAP, and PLP1 in the cochlea of the common marmoset
Hosoya, M., Suda, S., Ueno, M., Shimanuki, M. N., Nishiyama, T., Oishi, N., & Ozawa, H. (2026) · Scientific Reports · doi:10.1038/s41598-026-60318-y
“GLAST is a protein encoded by the SLC1A3 gene in humans 32 .”
An ATP-associated membrane interface integrating methionine flux with redox-regulated signaling in cancer
Benavides, M. A. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1779365
Construction and mechanistic exploration of a ferroptosis related gene based prognostic model for cisplatin resistance in bladder cancer.
Shao, Y.-Q., Yu, Q.-Y., Zhu, J., & Wang, X. (2025) · Computer Methods in Biomechanics and Biomedical Engineering · doi:10.1080/10255842.2025.2585143
THE FIRST LAW OF THERMODYNAMICS ANALYSIS OF TRANSPORTERS INVOLVED IN THE GLUTAMATE/GABA-GLUTAMINE CYCLE
Gur, M., Yilmaz, S., & Taka, E. (2021) · Isı Bilimi ve Tekniği Dergisi · doi:10.47480/isibted.1025952
Defining compartmentalized stem and progenitor populations with distinct cell division frequency in the ocular surface epithelium
Ishii, R., Yanagisawa, H., & Sada, A. (2020) · bioRxiv · doi:10.1101/2020.06.23.156505
“Slc1a3 gene encodes a glutamate/aspartate transporter and functions for glutamatergic neurotransmission in brain (Kanai and Hediger, 2004).”
Background
Relation between executive functions and polymorphisms in COMT, MAO-A, HTTLPR, SLC1A1 and HT2A in a sample of children with Obsessive Compulsive DisorderPreprint
Ávila-Campos, J. E., Dussan, M. C. P., Barreto, Á. M. P., Guerrero, E., Rojas, R., & Granados, H. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/452193
“And the gene encoding the glutamate transporter (SLC1A1) (Arnold et al., 2009; Arnold et al., 2006; Bailey et al., 2011; Kanai and Hediger 2004; Samuels et al., 2011; Shugart et al., 2009; Stewart, Mayerfeld, et al., 2013; Veenstra-VanderWeele et al., 2001; Rosenberg et al., 2004).”
Background
Nutrient Digestion, Absorption, and Sensing
Bishu, S., & Quigley, E. M. M. (2015) · Wiley eBooks · doi:10.1002/9781118512074.ch29 · Cited by 6
Directed Mutagenesis in Structure Activity Studies of Neurotransmitter Transporters
Carland, J., Edington, A. R., Scopelliti, A., Ryan, R., & Vandenberg, R. (2013) · InTech eBooks · doi:10.5772/45721
“The SLC1 family of neurotransmitter transporters includes five human excitatory amino acid transporters (EAAT1 to EAAT5) (Slotboom et al., 1999) and two neutral amino acid transporters (ASCT1 and ASCT2) (Arriza et al., 1993; Kanai & Hediger, 2004).”
Background
Modulateurs du transport vésiculaire du glutamate : développement d’outils pharmacologiques et de diagnostic pour la maladie d’Alzheimer
Favre-Besse, F.-C. (2012) · theses.fr (ABES) · doi:10.70675/5bb71069z5b5az4767zaea3zf859650fb47d
“Les résultats des essais réalisés sont résumés dans le Tableau VII-6.”
NUCLEAR RECEPTORS
Alexander, S., Mathie, A. A., & Peters, J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01649_6.x
“…acid transporters Overview: The SLC1 family of sodium dependent transporters includes the plasma membrane located glutamate transporters and the neutral amino acid transporters ASCT1 and ASCT2 (Amara and Arriza, 1993; Palacín et al., 1998; Kanai and Hediger, 2003; 2004; Beart and O’Shea, 2007).”
Consultants
Alexander, S., Mathie, A., & Peters, J. (2011) · doi:10.1111/j.1476-5381.2011.01649_2.x
“…acid transporters Overview: The SLC1 family of sodium dependent transporters includes the plasma membrane located glutamate transporters and the neutral amino acid transporters ASCT1 and ASCT2 (Amara and Arriza, 1993; Palacín et al., 1998; Kanai and Hediger, 2003; 2004; Beart and O’Shea, 2007).”
CNS ‐ Transporters as Drug Targets
Gundertofte, K. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627424.ch4
Cell‐Surface Transmitter Transporters
Alexander, S., Mathie, A., & Peters, J. (2008) · doi:10.1038/sj.bjp.0707758
CELL SURFACE TRANSMITTER TRANSPORTERS
(2006) · doi:10.1038/sj.bjp.0706706
Glutamate (excitatory amino acid)
Alexander, S. P. H., Mathie, A., & Peters, J. (2006) · doi:10.1038/sj.bjp.0706487
Cell Surface Transmitter Transporters
(2005) · doi:10.1038/sj.bjp.0706164
“In addition, a thermodynamically uncoupled Cl- flux, activated by Naþ and glutamate (Kanner & Borre, 2002; Kanai & Hediger, 2003; 2004), is sufficiently large, in the instances of EAAT4 and EAAT5, to influence neuronal excitability.”
Cell Surface Transmitter Transporters
(2004) · doi:10.1038/sj.bjp.0705678
Glial Cells
Williams, M. R., Macdonald, C., & Cordero, M. D. (2021) · Springer eBooks · doi:10.1007/978-3-030-68308-5_12
Electrophysiology of the Inner Retina in Health and Disease: EAAT5 in the Rod Bipolar Cell and Oscillatory Potentials in Diabetes
Bligard, G. W. (2020) · doi:10.7936/7g4b-nf08
“EAATs are members of the solute carrier family 1 (SLC1), which also includes two neutral amino-acid transporters, ASCT1 and ASCT2 [62], and are distinct from vesicular glutamate transporters.”
Background
Glutamaterges System
Böhm, S. (2020) · Pharmakologie und Toxikologie · doi:10.1007/978-3-662-58304-3_13
Der Einfluss von Clostridium botulinum C3 Proteinen auf die neuronale Glutamat-Aufnahme
Piepgras, J. (2019) · doi:10.17169/refubium-25991
Bioinformatic approaches for identifying single nucleotide variants and profiling alternative expression in cancer transcriptomes
Goya, R. (2017) · doi:10.14288/1.0362107
“SLC1A5 Encodes a neutral amino acid transporter involved in glutamate uptake [376], a mechanism that can cover a tumour’s metabolism demands [377] and which can be targeted to stop tumour growth in different cancer types [378–380].”
Background
Curriculum Vitae and Publications
Rummel, R. (2017) · doi:10.1007/978-3-319-54463-2_13
Probing the Dynamics of Plasma Membrane Glutamate Transporters in Real Time by Total Internal Fluorescence Reflection Microscopy
Cairano, E. S. D., Marciani, P., Moretti, S., & Perego, C. (2016) · Springer protocols handbooks/Springer protocols · doi:10.1007/8623_2016_9
A Molecular View of the Synapse
Fantini, J., & Yahi, N. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800111-0.00005-9
Control of Intracellular pH
Bevensee, M. O., & Boron, W. F. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381462-3.00052-5 · Cited by 41
Function of Neurotransmitter Amino Acid Transporters
Shigeri, Y., & Shimamoto, K. (2006) · doi:10.2142/biophys.46.10

Authors: Kanai, Y., & Hediger, M. A.
Affiliations: Kyorin University (JP)
Brigham and Women's Hospital (US)
Corresponding author: Hediger, Matthias A.
ORCID: Kanai, Yoshikatsu
Hediger, Matthias A.
Venue: Pfl�gers Archiv European Journal of Physiology
Publisher: Springer Science and Business Media LLC
Published: 2004-02-01
Volume: 447
Issue: 5
Pages: 469-479
ISSN: 0031-6768 (ISSN-L)
1432-2013
DOI: 10.1007/s00424-003-1146-4
OpenAlex: W1998475753
Cited by: 450
References: 0
Citations by year: 2026: 8 · 2025: 11 · 2024: 13 · 2023: 11 · 2022: 16 · 2021: 20 · 2020: 18 · 2019: 26 · 2018: 10 · 2017: 18 · 2016: 18 · 2015: 15 · 2014: 24 · 2013: 33 · 2012: 29
FWCI: 10.30
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Pflügers Archiv - European Journal of Physiology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords: glutamate transporters, neutral amino acid transporter, EAAC1, GLT-1, GLAST, EAAT4, ASCT1, ASCT2, glutamate excitotoxicity, cerebral ischemia, glutamate release, amyotrophic lateral sclerosis, motor neuron protection
MeSH terms: Animals, Biological Transport, Multigene Family, Humans, Glutamic Acid, Amino Acids, Neutral, Amino Acid Transport System X-AG

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The glutamate/neutral amino acid transporter family SLC1: molecular, physiological and pharmacological aspects

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cited by

Metadata

Record

About these checks