Glutathione is a physiologic reservoir of neuronal glutamate
Open accessAbstract
Glutamate, the principal excitatory neurotransmitter of the brain, participates in a multitude of physiologic and pathologic processes, including learning and memory. Glutathione, a tripeptide composed of the amino acids glutamate, cysteine, and glycine, serves important cofactor roles in antioxidant defense and drug detoxification, but glutathione deficits occur in multiple neuropsychiatric disorders. Glutathione synthesis and metabolism are governed by a cycle of enzymes, the γ-glutamyl cycle, which can achieve intracellular glutathione concentrations of 1-10mM. Because of the considerable quantity of brain glutathione and its rapid turnover, we hypothesized that glutathione may serve as a reservoir of neural glutamate. We quantified glutamate in HT22 hippocampal neurons, PC12 cells and primary cortical neurons after treatment with molecular inhibitors targeting three different enzymes of the glutathione metabolic cycle. Inhibiting 5-oxoprolinase and γ-glutamyl transferase, enzymes that liberate glutamate from glutathione, leads to decreases in glutamate. In contrast, inhibition of γ-glutamyl cysteine ligase, which uses glutamate to synthesize glutathione, results in substantial glutamate accumulation. Increased glutamate levels following inhibition of glutathione synthesis temporally precede later effects upon oxidative stress.
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Glutathione, the main antioxidant and redox regulator, constitutes a neuronal reservoir of glutamate.
“Moreover, glutathione (GSH), the main antioxidant and redox regulator, constitutes a neuronal reservoir of glutamate (Koga et al., 2011).”
From Redox dysregulation, neuroinflammation, and NMDA receptor hypofunction: A “central hub” in schizophrenia pathophysiology? (2016) · cites this paper as Koga et al., 2011
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Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Tietze, F. (1969) · Analytical Biochemistry · doi:10.1016/0003-2697(69)90064-5 · Cited by 6,077 · see citing works
Hayes, J. D., Flanagan, J. U., & Jowsey, I. R. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095857 · Cited by 3,565 · see citing works
Glutathione: overview of its protective roles, measurement, and biosynthesis
Forman, H. J., Zhang, H., & Rinna, A. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.006 · Cited by 2,636 · see citing works
Rahman, I., Kode, A., & Biswas, S. K. (2006) · Nature Protocols · doi:10.1038/nprot.2006.378 · Cited by 2,262 · see citing works
Glutathione metabolism and its selective modification.
Meister, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77815-6 · Cited by 2,012 · see citing works
The glutamate homeostasis hypothesis of addiction
Kalivas, P. W. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2515 · Cited by 1,350 · see citing works
Setsukinai, K.-I., Urano, Y., Kakinuma, K., Majima, H. J., & Nagano, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209264200 · Cited by 1,301 · see citing works
Selective Modification of Glutathione Metabolism
Meister, A. (1983) · Science · doi:10.1126/science.6836290 · Cited by 1,267 · cited 2× · see citing works
“1), for which glutamate is specifically added and liberated at discrete steps [5,11].”
BackgroundGlutathione dysregulation and the etiology and progression of human diseases
Ballatori, N., Krance, S. M., Notenboom, S., Shi, S., Tieu, K., & Hammond, C. L. (2009) · Biological Chemistry · doi:10.1515/bc.2009.033 · Cited by 1,118 · see citing works
Targeting the glutamatergic system to develop novel, improved therapeutics for mood disorders
Sanacora, G., Zarate, C. A., Krystal, J. H., & Manji, H. K. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2462 · Cited by 894 · see citing works
Glutamate and Neurotrophic Factors in Neuronal Plasticity and Disease
Mattson, M. P. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1418.005 · Cited by 640 · see citing works
Hertz, L. (1979) · Progress in Neurobiology · doi:10.1016/0301-0082(79)90018-2 · Cited by 629 · see citing works
Unraveling mechanisms of homeostatic synaptic plasticity
Pozo, K., & Goda, Y. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.028 · Cited by 565 · see citing works
Glutathione in Defense and Signaling
Dickinson, D. A., & Forman, H. J. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04690.x · Cited by 468 · see citing works
Kanai, Y., & Hediger, M. A. (2004) · Pfl�gers Archiv European Journal of Physiology · doi:10.1007/s00424-003-1146-4 · Cited by 450 · cited 2× · see citing works
“Substantial proportions of glutamate neurotransmitter pools (50-60%) have long thought to be derived from the glutamine-glutamate shuttle [16,17], with much smaller amounts arising from glycolysis [18-20].”
BackgroundHamberger, A., Chiang, G. H., Nylen, E. S., Scheff, S. W., & Cotman, C. W. (1979) · Brain Research · doi:10.1016/0006-8993(79)90306-8 · Cited by 418 · see citing works
Disrupted-in-Schizophrenia 1 (DISC1) regulates spines of the glutamate synapse via Rac1
Hayashi-Takagi, A., Takaki, M., Graziane, N., Seshadri, S., Murdoch, H., Dunlop, A. J., Makino, Y., Seshadri, A. J., Ishizuka, K., Srivastava, D. P., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2487 · Cited by 399 · see citing works
Self-citationRedox dysregulation, neurodevelopment, and schizophrenia
Do, K. Q., Cabungcal, J. H., Frank, A., Steullet, P., & Cuenod, M. (2009) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2009.05.001 · Cited by 384 · see citing works
Regulation of Neuronal Glutathione Synthesis
Aoyama, K., Watabe, M., & Nakaki, T. (2008) · Journal of Pharmacological Sciences · doi:10.1254/jphs.08r01cr · Cited by 356 · see citing works
Handbook of Neurochemistry and Molecular Neurobiology
Lajtha, Á., Galoyan, A. A., & Besedovsky, H. O. (2007) · Springer eBooks · doi:10.1007/978-0-387-30398-7 · Cited by 350 · see citing works
Histochemical evaluation of glutathione in brain
Slivka, A., Mytilineou, C., & Cohen, G. (1987) · Brain Research · doi:10.1016/0006-8993(87)90712-8 · Cited by 249 · see citing works
Dynamic Regulation of Synaptic GABA Release by the Glutamate-Glutamine Cycle in Hippocampal Area CA1
Liang, S., Carlson, G. C., & Coulter, D. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0329-06.2006 · Cited by 203 · see citing works
A Single Packet of Transmitter Does Not Saturate Postsynaptic Glutamate Receptors
Ishikawa, T., Sahara, Y., & Takahashi, T. (2002) · Neuron · doi:10.1016/s0896-6273(02)00692-x · Cited by 176 · see citing works
Orrego, F., & Villanueva, S. (1993) · Neuroscience · doi:10.1016/0306-4522(93)90355-j · Cited by 150 · see citing works
Chinta, S. J., Kumar, M. J., Hsu, M., Rajagopalan, S., Kaur, D., Rane, A., Nicholls, D. G., Choi, J., & Andersen, J. K. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3885-07.2007 · Cited by 145 · see citing works
Vesicular glutamate transporters (VGLUTs): The three musketeers of glutamatergic system
Liguz‐Lecznar, M., & Skangiel-Kramska, J. (2007) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2007-1649 · Cited by 133 · see citing works
Excitatory Synaptic Transmission Persists Independently of the Glutamate–Glutamine Cycle
Kam, K., & Nicoll, R. A. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1198-07.2007 · Cited by 124 · see citing works
Reis, H. J., Guatimosim, C., Paquet, M., Santos, M., Ribeiro, F. M., Kümmer, A., Pereira, G. S., Salgado, J. V., Vieira, L. B., Teixeira, A. L., et al. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787549271 · Cited by 111 · see citing works
Handbook of Neurochemistry and Molecular Neurobiology
Perez-Polo, J. R., & Lajtha, Á. (2006) · Springer eBooks · doi:10.1007/978-0-387-30380-2 · Cited by 109 · see citing works
Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A., & Yoshino, H. (1983) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.47.1323 · Cited by 98 · see citing works
In Vivo Release from Cerebral Cortex of [14C]Glutamate Synthesized from [U‐14C]Glutamine
Thanki, C. M., Sugden, D., Thomas, A. J., & Bradford, H. F. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb04785.x · Cited by 91 · see citing works
Hausch, F., Halttunen, T., Mäki, M., & Khosla, C. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00045-0 · Cited by 89 · see citing works
Sun, X., Shih, A. Y., Johannssen, H. C., Erb, H., Li, P., & Murphy, T. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601567200 · Cited by 89 · see citing works
Gamma‐Glutamyl Transpeptidase Substrate Specificity and Catalytic Mechanism
Keillor, J. W., Castonguay, R., & Lherbet, C. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01027-x · Cited by 80 · see citing works
Yamashita, T., Ishikawa, T., & Takahashi, T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-09-03633.2003 · Cited by 72 · see citing works
Werf, P. V. D., Stephani, R. A., & Meister, A. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1026 · Cited by 70 · see citing works
Nj�lsson, R., Ristoff, E., Carlsson, K., Winkler, A., Larsson, A., & Norgren, S. (2005) · Human Genetics · doi:10.1007/s00439-005-1255-6 · Cited by 68 · see citing works
Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A., & Yoshino, H. (1983) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1983.10866079 · Cited by 65 · see citing works
Chapman, J., & Zhou, M. (1999) · Analytica Chimica Acta · doi:10.1016/s0003-2670(99)00533-4 · Cited by 64 · see citing works
Patients with genetic defects in the γ-glutamyl cycle
Ristoff, E., & Larsson, A. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00155-5 · Cited by 57 · see citing works
Vesicular Glutamate Transporters In Cognito
Otis, T. S. (2001) · Neuron · doi:10.1016/s0896-6273(01)00176-3 · Cited by 51 · see citing works
Shupliakov, O., Atwood, H., Ottersen, O. P., Storm‐Mathisen, J., & Brodin, L. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-11-07168.1995 · Cited by 34 · see citing works
Pileblad, E., Eriksson, P. S., & Hansson, E. (1991) · Journal of Neural Transmission · doi:10.1007/bf01250374 · Cited by 31 · see citing works
Kinetic properties and inhibition of Acinetobacter glutaminase-asparaginase
Steckel, J., Roberts, J., Philips, F. S., & Chou, T. (1983) · Biochemical Pharmacology · doi:10.1016/0006-2952(83)90613-5 · Cited by 22 · see citing works
Janáky, R., Cruz-Aguado, R., Oja, S. S., & Shaw, C. (2007) · Springer eBooks · doi:10.1007/978-0-387-30373-4_15 · Cited by 20 · see citing works
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Rae, C. D. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1199-5 · Cited by 491 · see citing works
Steullet, P., Cabungcal, J. H., Monin, A., Dwir, D., O'Donnell, P., Cuenod, M., & Do, K. Q. (2016) · Schizophrenia Research · doi:10.1016/j.schres.2014.06.021 · Cited by 262 · see citing works
Insulin Resistance and Oxidative Stress in the Brain: What’s New?
Maciejczyk, M., Żebrowska, E., & Chabowski, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040874 · Cited by 262 · see citing works
Glutathione in Brain Disorders and Aging
Iskusnykh, I. Y., Zakharova, A. A., & Pathak, D. (2022) · Molecules · doi:10.3390/molecules27010324 · Cited by 213 · see citing works
The energetic brain—A review from students to students
Bordone, M. P., Salman, M. M., Titus, H. E., Amini, E., Andersen, J. V., Chakraborti, B., Diuba, A. V., Dubouskaya, T. G., Ehrke, E., Espindola de Freitas, A., et al. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14829 · Cited by 205 · see citing works
Transcriptional profiling and therapeutic targeting of oxidative stress in neuroinflammation
Mendiola, A. S., Ryu, J. K., Bardehle, S., Meyer-Franke, A., Ang, K. K.-H., Wilson, C., Baeten, K. M., Hanspers, K., Merlini, M., Thomas, S., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0654-0 · Cited by 199 · see citing works
Rae, C. D., & Williams, S. R. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.12.022 · Cited by 164 · see citing works
Implications for reactive oxygen species in schizophrenia pathogenesis
Koga, M., Serritella, A. V., Sawa, A., & Sedlak, T. W. (2015) · Schizophrenia Research · doi:10.1016/j.schres.2015.06.022 · Cited by 158 · see citing works
Self-citationThe glutathione cycle shapes synaptic glutamate activity
Sedlak, T., Paul, B., Parker, G. M., Hester, L., Snowman, A., Taniguchi, Y., Kamiya, A., Snyder, S., & Sawa, A. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1817885116 · Cited by 141 · see citing works
Self-citationPehrson, A. L., & Sánchez, C. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s62912 · Cited by 143 · see citing works
Cárdenas, A., Koestler, D. C., Houseman, E. A., Jackson, B. P., Kile, M. L., Karagas, M. R., & Marsit, C. J. (2015) · Epigenetics · doi:10.1080/15592294.2015.1046026 · Cited by 128 · see citing works
The dark side of gamma-glutamyltransferase (GGT): Pathogenic effects of an ‘antioxidant’ enzyme
Corti, A., Belcastro, E., Dominici, S., Maellaro, E., & Alfonso Pompella, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.005 · Cited by 120 · see citing works
Das, T. K., Javadzadeh, A., Dey, A., Sabesan, P., Théberge, J., Raduà, J., & Palaniyappan, L. K. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.08.006 · Cited by 114 · see citing works
Xin, L., Ralf Mekle, A., Fournier, M., Baumann, P., Ferrari, C., Alameda, L., Jenni, R., Lu, H., Schaller, B., Cuénod, M., et al. (2016) · Schizophrenia Bulletin · doi:10.1093/schbul/sbw038 · Cited by 100 · see citing works
Ramos-Chávez, L. A., Rendón-López, C. R. R., Zepeda, A., Silva‐Adaya, D., Razo, L. M. D., & Gonsebatt, M. E. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00021 · Cited by 100 · see citing works
Nucifora, L. G., Tanaka, T., Hayes, L. N., Kim, M., Lee, B. J., Matsuda, T., Nucifora, F. C., Sedlak, T. W., Mojtabai, R., Eaton, W. W., et al. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.178 · Cited by 94 · see citing works
Self-citationRosa, A. R., Singh, N., Whitaker, E., de Brito, M., Lewis, A. M., Vieta, E., Churchill, G. C., Geddes, J. R., & Goodwin, G. M. (2014) · Psychological Medicine · doi:10.1017/s0033291714000014 · Cited by 91 · see citing works
Sedlak, T. W., Nucifora, L. G., Koga, M., Shaffer, L. S., Higgs, C. P., Tanaka, T., Wang, A. M., Coughlin, J. M., Barker, P. B., Fahey, J. W., et al. (2017) · Complex Psychiatry · doi:10.1159/000487639 · Cited by 77 · see citing works
Self-citationLee, T.-M., Lee, K.-M., Lee, C.-Y., Lee, H., Tam, K., & Loh, E. (2020) · Australian & New Zealand Journal of Psychiatry · doi:10.1177/0004867420952540 · Cited by 75 · see citing works
Pariset, E., Malkani, S., Cekanaviciute, E., & Costes, S. V. (2020) · International Journal of Radiation Biology · doi:10.1080/09553002.2020.1820598 · Cited by 61 · see citing works
Cattani, D., Goulart, P. B., Cavalli, V. L. D. L. O., Duarte, E. C. W., dos Santos, A. Q., Pierozan, P., de Souza, D. F., Woehl, V. M., Fernandes, M. D. C., Silva, F. R. M. B., et al. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.05.001 · Cited by 60 · see citing works
Jouroukhin, Y., Zhu, X., Shevelkin, A. V., Hasegawa, Y., Abazyan, B. N., Saito, A., Pevsner, J., Kamiya, A., & Pletnikov, M. V. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.07.024 · Cited by 53 · see citing works
Bano, K., Kumar, B., Alyemeni, M. N., & Ahmad, P. (2022) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2022.07.026 · Cited by 51 · see citing works
Is There a Glutathione Centered Redox Dysregulation Subtype of Schizophrenia?
Palaniyappan, L. K., Park, M. T. M., Jeon, P., Limongi, R., Yang, K., Sawa, A., & Théberge, J. (2021) · Antioxidants · doi:10.3390/antiox10111703 · Cited by 57 · see citing works
Self-citationOxidative Stress and Emergence of Psychosis
Rambaud, V., Marzo, A., & Chaumette, B. (2022) · Antioxidants · doi:10.3390/antiox11101870 · Cited by 47 · see citing works
Coughlin, J. M., Yang, K., Marsman, A., Pradhan, S., Wang, M., Ward, R. E., Bonekamp, S., Ambinder, E. B., Higgs, C. P., Kim, P. K., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-00901-5 · Cited by 43 · see citing works
Self-citationLally, N., An, L., Banerjee, D., Niciu, M. J., Luckenbaugh, D. A., Richards, E. M., Roiser, J. P., Shen, J., Zarate, C. A., & Nugent, A. C. (2015) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.24970 · Cited by 44 · see citing works
Endres, D., van Elst, L. T., Meyer, S. A., Feige, B., Nickel, K., Bubl, A., Riedel, A., Ebert, D., Lange, T., Glauche, V., et al. (2017) · Molecular Autism · doi:10.1186/s13229-017-0122-3 · Cited by 41 · see citing works
Liver Enzymes and Risk of Stroke: The Atherosclerosis Risk in Communities (ARIC) Study
Ruban, A., Daya, N. R., Schneider, A. L. C., Gottesman, R. F., Selvin, E., Coresh, J., Lazo, M., & Koton, S. (2020) · Journal of Stroke · doi:10.5853/jos.2020.00290 · Cited by 40 · see citing works
Forgetting generates a novel state that is reactivatable
Liu, H., Wu, T., Canales, X. G., Wu, M. H., Choi, M.-K., Duan, F., Calarco, J. A., & Zhang, Y. (2022) · Science Advances · doi:10.1126/sciadv.abi9071 · Cited by 38 · see citing works
Metabolomic responses of Haliotis diversicolor to organotin compounds
Lü, J., Feng, J., Cai, S., & Chen, Z. (2016) · Chemosphere · doi:10.1016/j.chemosphere.2016.10.124 · Cited by 37 · see citing works
Rice, S. A., Have, G. A. M. T., Reisz, J. A., Gehrke, S. A., Stefanoni, D., Frare, C., Barati, Z., Coker, R. H., D’Alessandro, A., Deutz, N. E. P., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00312-4 · Cited by 36 · see citing works
Caballero, J. L., Pacchiarotti, I., Murru, A., Valentí, M., Colom, F., Benach, B., Pérez, V., Dalmau, J. O., & Vieta, E. (2015) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2015.05.012 · Cited by 36 · see citing works
Coughlin, J. M., Tanaka, T., Marsman, A., Wang, H., Bonekamp, S., Kim, P. K., Higgs, C., Varvaris, M., Edden, R. A. E., Pomper, M. G., et al. (2015) · Current Molecular Medicine · doi:10.2174/1566524015666150303104811 · Cited by 32 · see citing works
Self-citationHeavy Metals in Umbilical Cord Blood: Effects on Epigenetics and Child Development
Dutta, S., & Ruden, D. M. (2024) · Cells · doi:10.3390/cells13211775 · Cited by 30 · see citing works
Rasool, M., Malik, A., Saleem, S., Ashraf, M. A. B., Khan, A. Q., Waquar, S., Zahid, A., Shaheen, S., Abu-Elmagd, M. M., Gauthaman, K., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.646287 · Cited by 29 · see citing works
Sun, X., Wu, B., Tu, K., Zhou, L., Yang, A., & Liu, Z. (2022) · Aquaculture Reports · doi:10.1016/j.aqrep.2022.101368 · Cited by 28 · see citing works
Maciejczyk, M., Żebrowska, E., Nesterowicz, M., Żendzian‐Piotrowska, M., & Zalewska, A. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7450514 · Cited by 27 · see citing works
Girgis, R. R., Baker, S. C., Mao, X., Gil, R. B., Javitt, D. C., Kantrowitz, J. T., Gu, M., Spielman, D. M., Ojeil, N., Xu, X., et al. (2019) · Psychiatry Research · doi:10.1016/j.psychres.2019.03.018 · Cited by 26 · see citing works
Palaniyappan, L. K., Sabesan, P., Li, X., & Luo, Q. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.796466 · Cited by 23 · see citing works
Baghcheghi, Y., Salmani, H., Beheshti, F., & Hosseini, M. (2017) · Advanced Biomedical Research · doi:10.4103/2277-9175.206699 · Cited by 22 · see citing works
Neuroprotective effects of Magnoliae Flos extract in mouse hippocampal neuronal cells
Jung, Y. S., Weon, J. B., Yang, W. S., Ryu, G., & Ma, C. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-28055-z · Cited by 21 · see citing works
Suhaibani, A. A., Bacha, A. G. B., Alonazi, M. A., Bhat, R. S., & El-Ansary, A. K. (2021) · Food Science & Nutrition · doi:10.1002/fsn3.2418 · Cited by 19 · see citing works
Rogóż, Z., Kamińska, K., Lech, M. A., & Lorenc-Koci, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042125 · Cited by 18 · see citing works
Breakdown and repair of metabolism in the aging brain
Shichkova, P., Coggan, J. S., Kanari, L., Boci, E., Favreau, C., Antonel, S., Keller, D. X., & Markram, H. (2025) · Frontiers in Science · doi:10.3389/fsci.2025.1441297 · Cited by 20 · see citing works
He, M., Shi, J., Wu, C., Xu, Y., & Liu, Y. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c04994 · Cited by 18 · see citing works
Chang, C.-T., Hsieh, P.-J., Lee, H., Lo, C.-H., Tam, K., & Loh, E. (2021) · Clinical Psychopharmacology and Neuroscience · doi:10.9758/cpn.2021.19.2.282 · Cited by 18 · see citing works
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Mitchell, S. C. (2021) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2021.02.014 · Cited by 16 · see citing works
Transsulfuration pathway: a targeting neuromodulator in Parkinson’s disease
Corona-Trejo, A., Gonsebatt, M. E., Trejo‐Solís, C., Campos‐Peña, V., Granados, L. I. Q., Villegas‐Vázquez, E. Y., Reyes‐Hernández, O. D., Hernández-Abad, V. J., Figueroa‐González, G., & Silva‐Adaya, D. (2023) · Reviews in the Neurosciences · doi:10.1515/revneuro-2023-0039 · Cited by 16 · see citing works
Glutathione in the nucleus accumbens regulates motivation to exert reward-incentivized effort
Zalachoras, I., Ramos‐Fernández, E., Hollis, F., Trovò, L., Rodrigues, J., Strasser, A., Zanoletti, O., Steiner, P., Preitner, N., Xin, L., et al. (2022) · eLife · doi:10.7554/elife.77791 · Cited by 17 · see citing works
Salem, S., Leghouchi, E., Soulimani, R., & Bouayed, J. (2019) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831/a000620 · Cited by 13 · see citing works
Profiling transcriptomes of human SH-SY5Y neuroblastoma cells exposed to maleic acid
Wang, C., Lin, Y.-C., Cheng, Y.-H., & Tung, C.-W. (2017) · PeerJ · doi:10.7717/peerj.3175 · Cited by 9 · see citing works
Sim, H. I., Kim, D. H., & Kim, M. (2022) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-022-00408-6 · Cited by 8 · see citing works
Antioxidants l-carnitine and d-methionine modulate neuronal activity through GABAergic inhibition
Wu, C., Gopal, K. V., Moore, E. J., & Gross, G. W. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1170-x · Cited by 8 · see citing works
Górny, M., Bilska-Wilkosz, A., Iciek, M., Rogóż, Z., & Lorenc-Koci, E. (2023) · The FEBS Journal · doi:10.1111/febs.16944 · Cited by 8 · see citing works
Wang, Z., Li, X., Shi, S., Shen, R., Yang, Y., Sun, C., Liu, Z., Zhang, H., & Zhang, B. (2025) · Chemical Communications · doi:10.1039/d5cc00870k · Cited by 6 · see citing works
Tzanetakos, D., Kyrozis, A., Karavasilis, E., Velonakis, G., Tzartos, J. S., Toulas, P., Sotirli, S. A., Evdokimidis, I., Tsivgoulis, G. K., Potagas, C. M., et al. (2023) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2023.12048 · Cited by 6 · see citing works
Ma, X., Shi, T., Zhang, M., Lu, X., Yang, C., Zhu, D., Shi, D.-X., Yang, Y. J., Wang, C.-L., Zhang, S., et al. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.02.009 · Cited by 6 · see citing works
González-Llorente, L., Gasco, M. Á. A., Aranda, M. A. G., Rabadán-Ros, R., Perez, R. Z., Núñez‐Delicado, E., Menéndez-Coto, N., García-González, C., Baena-Huerta, F. J., Coto‐Montes, A. M., et al. (2025) · Biomedicines · doi:10.3390/biomedicines13040949 · Cited by 5 · see citing works
Liu, J., Gong, Z., & Liu, L. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12735 · Cited by 4 · see citing works
Tejero, A., León, D., & Martı́n, M. (2025) · Membranes · doi:10.3390/membranes15050152 · Cited by 2 · see citing works
Araujo, C. D. S., Cavalcante, D. G. S. M., Braga, N. O., Gomes, A. S., Yoshihara, E., Kerche, L. E., & Job, A. E. (2019) · Colloquium Vitae · doi:10.5747/cv.2019.v11.n3.v268 · Cited by 2 · see citing works
Chapa‐Dubocq, X. R., Vita, S. M., Guzman‐Hernandez, R. A., & Molina, P. E. (2026) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.70267 · Cited by 1 · see citing works
Wang, R., Li, Y., Shi, D., Huang, H., Ren, Z., Ge, Y., Chang, Y., & Yan, G. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104215 · Cited by 1 · see citing works
Metabolic Brain Disorders: Prodromes, Symptoms, and Syndromes
Błaszczyk, J. W. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27125190 · Cited by 1 · see citing works
Bandaru, N., Ramu, A., & Vidhyadhara, S. (2020) · Toxicology International · doi:10.18311/ti/2020/v27i1-2/25580 · Cited by 1 · see citing works
Cattani, D. (2013) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 1 · see citing works
Dong, Y., Lin, H., Rattelle, A., Panzer, J. A., & Lynch, D. R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.65836-1
Wang, J., Li, F., Ren, F., Ma, W., Liu, Y., Zhang, W., Li, X., Bi, Y., Qian, X., & Gao, F. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05011-3
Kanagasabai, K., Oran, O., Palaniyappan, L. K., & Théberge, J. (2026) · NMR in Biomedicine · doi:10.1002/nbm.70385
Andreu, S., Gizzi, V., Pasco, U., Sebih, F., Zitouni, Y., Jimenez, P., Rolland, V., Chavanieu, A., Estaran, S., Rousset, M., et al. (2026) · British Journal of Pharmacology · doi:10.1111/bph.70650
- Authors
- Koga, M., Serritella, A. V., Messmer, M. M., Hayashi-Takagi, A., Hester, L. D., Snyder, S. H., Sawa, A., & Sedlak, T. W.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Sedlak, Thomas W.
- ORCID
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2011-06
- Volume
- 409
- Issue
- 4
- Pages
- 596-602
- ISSN
- 0006-291X (ISSN-L)
- PMC
- PMC3923312
- OpenAlex
- W2027589595
- Cited by
- 73
- References
- 46
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 9 · 2021: 6 · 2020: 8 · 2019: 6 · 2018: 3 · 2017: 7 · 2016: 3 · 2015: 7 · 2014: 4 · 2013: 3 · 2012: 1
- FWCI
- 1.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (MH084018, R01MH018501, MH 092443, P20MH084018, R37MH018501, MH-18501, R01MH092443)
- National Institute of Neurological Disorders and Stroke (K08NS057824)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione, glutamate, glutathione metabolism, gamma-glutamyl cycle, glutathione synthesis, glutathione depletion, 5-oxoprolinase, gamma-glutamyl transferase, hippocampal neurons, cortical neurons, oxidative stress, excitatory neurotransmitter, antioxidant defense
- MeSH terms
- Animals, Enzyme Inhibitors, gamma-Glutamyltransferase, Glutathione, Hippocampus, Isoxazoles, Neurons, Pyroglutamate Hydrolase, Glutamic Acid, Buthionine Sulfoximine, Cell Line, Tumor, Imidazolines, Mice, Rats
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