<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="other" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Annals of Clinical and Experimental Neurology</journal-id><journal-title-group><journal-title xml:lang="en">Annals of Clinical and Experimental Neurology</journal-title><trans-title-group xml:lang="ru"><trans-title>Анналы клинической и экспериментальной неврологии</trans-title></trans-title-group></journal-title-group><issn publication-format="print">2075-5473</issn><issn publication-format="electronic">2409-2533</issn><publisher><publisher-name xml:lang="en">Eco-Vector</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">419</article-id><article-id pub-id-type="doi">10.17816/psaic419</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>Reviews</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>Обзоры</subject></subj-group><subj-group subj-group-type="article-type"><subject>Unknown</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Glutamate receptors in neuronal and immune system cells</article-title><trans-title-group xml:lang="ru"><trans-title>Глутаматные рецепторы в клетках нервной и иммунной систем</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Davydova</surname><given-names>O. N.</given-names></name><name xml:lang="ru"><surname>Давыдова</surname><given-names>O. Н.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>platonova@neurology.ru</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Boldyrev</surname><given-names>A. A.</given-names></name><name xml:lang="ru"><surname>Болдырев</surname><given-names>A. A.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>platonova@neurology.ru</email><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Research Center of Neurology</institution></aff><aff><institution xml:lang="ru">Научный центр неврологии РАМН</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2007-12-14" publication-format="electronic"><day>14</day><month>12</month><year>2007</year></pub-date><volume>1</volume><issue>4</issue><issue-title xml:lang="en"/><issue-title xml:lang="ru"/><fpage>35</fpage><lpage>42</lpage><history><date date-type="received" iso-8601-date="2017-02-07"><day>07</day><month>02</month><year>2017</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2007, Davydova O.N., Boldyrev A.A.</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2007, Davydova O.N., Boldyrev A.A.</copyright-statement><copyright-year>2007</copyright-year><copyright-holder xml:lang="en">Davydova O.N., Boldyrev A.A.</copyright-holder><copyright-holder xml:lang="ru">Davydova O.N., Boldyrev A.A.</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/><license><ali:license_ref xmlns:ali="http://www.niso.org/schemas/ali/1.0/">https://creativecommons.org/licenses/by/4.0</ali:license_ref></license></permissions><self-uri xlink:href="https://annaly-nevrologii.com/pathID/article/view/419">https://annaly-nevrologii.com/pathID/article/view/419</self-uri><abstract xml:lang="en"><p>The role of glutamatergic system in synaptic transmission and excitotoxicity is well established. Moreover, expression of glutamate receptors in a number of non-neuronal cells, where they may perform specific, as yet unknown functions, becomes evident. While the role of glutamic acid in the non-neuronal cells is not totally understood, this compound can be considered as a specific regulatory molecule not only for the central nervous system. Actually, recent publications demonstrate that glutamate receptors expressed in lymphocytes take part in the processes of their activation. Therefore, within the framework of the well-known paradigm of interaction between nervous and immune systems, glutamate can be regarded as neuroimmune modulator. Glutamate action on the immune cells may play an important role in the pathogenesis of different diseases, especially those accompanied by inflammatory reactions and/or increased levels of glutamate in brain and peripheral blood stream.</p></abstract><trans-abstract xml:lang="ru"><p>Роль глутаматных рецепторов в процессах синаптической трансмиссии и экзайтотоксичности достаточно хорошо изучена. Наряду с этим на сегодняшний день становится очевидной экспрессия глутаматных рецепторов в различных типах не нейрональных клеток, где они выполняют иные, зачастую еще неизвестные функции. Несмотря на то, что роль глутаминовой кислоты вне нервной системы пока мало изучена, это соединение можно рассматривать как регуляторную молекулу широкого спектра действия, функции которой не ограничены ЦНС. В частности, недавние исследования показали, что глутаматные рецепторы, экспрессирующиеся в лимфоцитах, участвуют в процессах активации данного типа клеток. В связи с этим в рамках сложившихся представлений о взаимной регуляции иммунной и нервной систем глутамат может рассматриваться как нейроиммуномодулятор. Действие глутамата на иммунокомпетентные клетки может играть важную роль в патогенезе различных заболеваний, в частности, сопровождающихся процессами нейровоспаления и/или повышением уровня глутамата в веществе мозга и периферическом кровотоке.</p></trans-abstract><kwd-group xml:lang="en"><kwd>glutamate</kwd><kwd>NMDA receptors</kwd><kwd>neurons</kwd><kwd>central nervous system</kwd><kwd>lymphocytes</kwd><kwd>intracellular signaling</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>глутамат</kwd><kwd>NMDA-рецепторы</kwd><kwd>нейроны</kwd><kwd>центральная нервная система</kwd><kwd>лимфоциты</kwd><kwd>внутриклеточная сигнализация</kwd></kwd-group><funding-group/></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Костанян И.А., Наволоцкая Е.В., Нуриева Р.И. и др. Взаимодействие L-глутаминовой кислоты с Т-лимфоцитами человека. Биоорг. хим. 1997; 23: 805–808.</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Крыжановский Г.Н., Магаева С.В., Макаров С.В., Сепиашвили Р.И. Нейроиммунопатология. Руководство. М.: Изд-во НИИ общей патологии и патофизиологии, 2003.</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Balazs R. Trophic effect of glutamate. Curr. Top. Med. Chem. 2006; 6: 961–968.</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Beal M.F. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 1995; 38: 357–366.</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Bhave S.V., Ghoda L., Hoffman P.L. Brain-derived neurotrophic factor mediates the anti-apoptotic effect of NMDA in cerebellar granule neurons: signal transduction cascades and site of ethanol action. J. Neurosci. 1999; 19: 3277–3286.</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Blondeau N., Widmann C., Lazdunski M., Heurteaux C. Activation of the nuclear factor-kappa B is a key event in brain tolerance. J. Neurosci. 2001; 21: 4668–4677.</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Boldyrev A.A, Kazey V.I., Leinsoo T.A. et al. Rodent lymphocytes express functionally active glutamate receptors. Biochem. Biophys. Res. Commun. 2004; 324: 133–139.</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Boldyrev A.A., Carpenter D.O., Johnson P. Emerging evidence for a similar role of glutamate receptors in the nervous and immune systems. J. Neurochem. 2005; 95: 913–918.</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Carroll R.C., Zukin R.S. NMDA-receptor trafficking and targeting: implications for synaptic transmission and plasticity. Trends. Neurosci. 2002; 25: 571–577.</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Danysz W., Parsons C.G. Glycine and N-methyl-D-aspartate receptors: physiological significance and possible therapeutic applications. Pharmacol. Rev. 1998; 50: 597–664.</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Dingledine R., Borges K., Bowie D., Traynelis S.F. The glutamate receptor ion channels. Pharmacol. Rev. 1999; 51: 7–61.</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Droge W., Eck H.P., Betzler M. et al. Plasma glutamate concentration and lymphocyte activity. J. Cancer Res. Clin. Oncol. 1988; 114: 124–128.</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Eck H.P., Frey H., Droge W. Elevated plasma glutamate concentrations in HIV-1-infected patients may contribute to loss of macrophage and lymphocyte functions. Int. Immunol. 1989; 1: 367–372.</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Eck H.P., Mertens T., Rosokat H. et al. T4+ cell numbers are correlated with plasma glutamate and cystine levels: association of hyperglutamataemia with immunodeficiency in diseases with different aetiologies. Int. Immunol. 1992; 4: 7–13.</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>FioricaHowells E., Gambale F., Horn R. et al. Phencyclidine blocks voltage-dependent potassium currents in murine thymocytes. J. Pharmacol. Exp. Ther. 1990; 252: 610–615.</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Franconi F., Miceli M., De Montis M.G. et al. NMDA receptors play an anti-aggregating role in human platelets. Thromb. Haemost. 1996; 76: 84–87.</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Ganor Y., Besser M., BenZakay N. et al. Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration. J. Immunol. 2003; 170: 4362–4372.</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Ganor Y., Teichberg V.I., Levite M. TCR activation eliminates glutamate receptor GluR3 from the cell surface of normal human T cells, via an autocrine/paracrine granzyme B-mediated proteolytic cleavage. J. Immunol. 2007; 178: 683–692.</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Genever P.G., Skerry T.M. Regulation of spontaneous glutamate release activity in osteoblastic cells and its role in differentiation and survival: evidence for intrinsic glutamatergic signaling in bone. FASEB J. 2001; 15: 1586–1588.</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Genever P.G., Wilkinson D.J., Patton A.J. et al. Expression of a functional N-methyl-D-aspartate-type glutamate receptor by bone marrow megakaryocytes. Blood 1999; 93: 2876–2883.</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Gill S.S., Mueller R.W., McGuire P.F., Pulido O.M. Potential target sites in peripheral tissues for excitatory neurotransmission and excitotoxicity. Toxicol. Pathol. 2000; 28: 277–284.</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Gill S.S., Pulido O.M., Mueller R.W., McGuire P.F. Molecular and immunochemical characterization of the ionotropic glutamate receptors in the rat heart. Brain. Res. Bull. 1998; 46: 429–434.</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Gill S.S., Pulido O.M., Mueller R.W., McGuire P.F. Immunochemical localization of the metabotropic glutamate receptors in the rat heart. Brain. Res. Bull. 1999; 48: 143–146.</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Grant S.G. Synapse signalling complexes and networks: machines underlying cognition. Bioessays 2003; 25: 1229–1235.</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Hetman M., Kharebava G. Survival signaling pathways activated by NMDA receptors. Curr. Top. Med. Chem. 2006; 6: 787–799.</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Hinoi E., Fujimori S., Nakamura Y., and Yoneda Y. Group III metabotropic glutamate receptors in rat cultured calvarial osteoblasts. Biochem. Biophys. Res. Commun. 2001; 281: 341–346.</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Hinoi E., Fujimori S., Yoneda Y. Modulation of cellular differentiation by N-methyl-D-aspartate receptors in osteoblasts. FASEB J. 2003; 17: 1532–1534.</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Hinoi E., Takarada T., Yoneda Y. Glutamate signaling system in bone. J. Pharmacol. Sci. 2004; 94: 215–220.</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Hitchcock I.S., Skerry T.M., Howard M.R., Genever P.G. NMDA-receptor-mediated regulation of human megakaryocytopoiesis. Blood 2003; 102: 1254–1259.</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Jiang X., Tian F., Mearow K. et al. The excitoprotective effect of N-methyl-D-aspartate receptors is mediated by a brain-derived neurotrophic factor autocrine loop in cultured hippocampal neurons. J. Neurochem. 2005; 94: 713–722.</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Jiang X., Zhu D., Okagaki P. N-methyl-D-aspartate and TrkB receptor activation in cerebellar granule cells: an in vitro model of preconditioning to stimulate intrinsic survival pathways in neurons. Ann. N. Y. Acad. Sci. 2003; 993: 134–145.</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Kalariti N., Pissimissis N., Koutsilieris M. The glutamatergic system outside the CNS and in cancer biology. Expert Opin. Investig. Drugs 2005; 14: 1487–1496.</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Kato H., Liu Y., Araki T., Kogure K. MK-801, but not anisomycin, inhibits the induction of tolerance to ischemia in the gerbil hippocampus. Neurosci. Lett. 1992; 139: 118–121.</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Khansari N., Whitten H.D., Fudenberg H.H. Phencyclidine-induced immunodepression. Science 1984; 225: 76–78.</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Khodorov B. Glutamate-induced deregulation of calcium homeostasis and mitochondrial dysfunction in mammalian central neurones. Prog. Biophys. Mol. Biol. 2004; 86: 279–351.</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Komuro H., Rakic P. Modulation of neuronal migration by NMDA receptors. Science 1993; 260: 95–97.</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Lewis R.S. Calcium signaling mechanisms in T lymphocytes. Ann. Rev. Immunol. 2001; 19: 497–521.</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Lewis R.S. Calcium oscillations in T-cells: mechanisms and consequences for gene expression. Biochem. Soc. Trans. 2003; Oct. 31 (Pt. 5): 925–929.</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Lombardi G., Dianzani Ch., Miglio G. et al. Characterization of ionotropic glutamate receptor in human lymphocytes. Br. J. Pharmacol. 2001; 133: 936–944.</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Low C.M., Lyuboslavsky P., French A. et al. Molecular determinants of proton-sensitive N-methyl-D-aspartate receptor gating. Mol. Pharmacol. 2003; 63: 1212–1222.</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Manabe S., Lipton S.A. Divergent NMDA signals leading to proapoptotic and antiapoptotic pathways in the rat retina. Invest. Ophthalmol. Vis. Sci. 2003; 44: 385–392.</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Mardiney M.R.Jr., Bredt A.B. The immunosuppressive effect of amantadine upon the response of lymphocytes to specific antigens in vitro. Transplantation 1971; 12: 183–188.</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Martino G., Hartung H.P. Immunopathogenesis of multiple sclerosis: the role of T cells. Curr. Opin. Neurol. 1999; 12: 309–321.</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Mashkina A.P., Tyulina O.V., Solovyova T. I. et al. The excitotoxic effect of NMDA on human lymphocyte immune function. Neurochem. Int. 2007; article in press (available online 4 May 2007).</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Mattson M.P., Meffert M.K. Roles for NF-kappa B in nerve cell survival, plasticity, and disease. Cell Death Differ. 2006; 13: 852–860.</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Miglio G., Varsaldi F., Dianzani C. et al. Stimulation of group I metabotropic glutamate receptors evokes calcium signals and c-jun and c-fos gene expression in human T cells. Biochem. Pharmacol. 2005; 70: 189–199.</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Miglio G., Varsaldi F., Lombardi G. Human T lymphocytes express N-methyl-D-aspartate receptors functionally active in controlling T cell activation. Biochem. Biophys. Res. Commun. 2005; 338: 1875–1883.</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Moalem G., Gdalyahu A., Shani Y. et al. Production of neurotrophins by activated T cells: implications for neuroprotective autoimmunity. J. Autoimmun. 2000; 5: 331–345.</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Nitsch R., Pohl E.E, Smorodchenko A. et al. Direct impact of T cells on neurons revealed by two-photon microscopy in living brain tissue. J. Neurosci. 2004; 24: 2458–2464.</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Pacheco R., Ciruela F., Casado V. et al. Group I metabotropic glutamate receptors mediate a dual role of glutamate in T cell activation. J. Biol. Chem. 2004; 279: 33352–33358.</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Pacheco R., Oliva H., MartinezNavio J.M. et al. Glutamate released by dendritic cells as a novel modulator of T cell activation. J. Immunol. 2006; 177: 6695–6704.</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Pollock P.M., CohenSolal K., Sood R. et. al. Melanoma mouse model implicates metabotropic glutamate signaling in melanocytic neoplasia. Nat. Genet. 2003; 34: 108–112.</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Poulopoulou C., Davaki P., Koliaraki V. et al. Reduced expression of metabotropic glutamate receptor 2mRNA in T cells of ALS patients. Ann. Neurol. 2005; 58: 946–949.</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Poulopoulou C., Markakis I., Davaki P. et al. Modulation of voltage- gated potassium channels in human T lymphocytes by extracellular glutamate. Mol. Pharmacol. 2005; 67: 856–867.</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Ravati A., Ahlemeyer B., Becker A. et al. Preconditioning-induced neuroprotection is mediated by reactive oxygen species and activation of the transcription factor nuclear factor-kappa B. J. Neurochem. 2001; 78: 909–919.</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Riccio A., Ahn S., Davenport C.M. et al. Mediation by a CREB family transcription factor of NGF-dependent survival of sympathetic neurons. Science 1999; 286: 2358–2361.</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Rzeski W., Turski L., Ikonomidou C. Glutamate antagonists limit tumor growth. Proc. Natl. Acad. Sci. USA, 2001; 98: 6372–6377.</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Said S.I., Dey R.D., Dickman K. Glutamate signaling in the lung. Trends. Pharmacol. Sci. 2001; 22: 344–345.</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Schwartz M., Shaked I., Fisher J. et al. Protective autoimmunity against the enemy within: fighting glutamate toxicity. Trends. Neurosci. 2003; 26: 297–302.</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Shamloo M., Rytter A., Wieloch T. Activation of the extracellular signal-regulated protein kinase cascade in the hippocampal CA1 region in a rat model of global cerebral ischemic preconditioning. Neuroscience 1999; 93: 81–88.</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Stepulak A., Sifringer M., Rzeski W. et al. NMDA antagonist inhibits the extracellular signal-regulated kinase pathway and suppresses cancer growth. Proc. Natl. Acad. Sci. USA, 2005; 102: 15605–15610.</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Storto M., De Grazia U., Battaglia G. et al. Expression of metabotropic glutamate receptors in murine thymocytes and thymic stromal cells. J. Neuroimmunol. 2000; 109: 112–120.</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Storto M., De Grazia U., Knopfler T. et al. Selective blockade of mGluR5 metabotropic glutamate receptors protect rat hepatocytes against hypoxic damage. J. Hepatol. 2003; 38: 179–187.</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Storto M., Sallese M., Salvatore L. et al. Expression of metabotropic glutamate receptors in the rat and human testis. J. Endocrinol. 2001; 170: 71–78.</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Thomas J., Carver M., Haisch C. et al. Differential effects of intravenous anaesthetic agents on cell-mediated immunity in the Rhesus monkey. Clin. Exp. Immunol. 1982; 47: 457–466.</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>Van Beek J., Elward K., Gasque P. Activation of complement in the central nervous system: roles in neurodegeneration and neuroprotection. Ann. N. Y. Acad. Sci. 2003; 992: 56–71.</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>Wang J.Q., Fibuch E.E., Mao L. Regulation of mitogen activated protein kinases by glutamate receptors. J. Neurochem. 2007; 100: 1–11.</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>Whitney K.D., McNamara J.O. GluR3 autoantibodies destroy neural cells in a complement-dependent manner modulated by complement regulatory proteins. J. Neurosci. 2000; 20: 7307–7316.</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>Winter C.R., Baker R.C. L-glutamate-induced changes in intracellular calcium oscillation frequency through non-classical glutamate receptor binding in cultured rat myocardial cells. Life Sci. 1995; 57: 1925–1934.</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>Yoo B.C., Jeon E., Hong S.H. et al. Metabotropic glutamate receptor 4-mediated 5-fluorouracil resistance in a human colon cancer cell line. Clin. Cancer Res. 2004; 10: 4176–4184.</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>Zhu D., Wu X., Strauss K.I. et al. N-methyl-D-aspartate and TrkB receptors protect neurons against glutamate excitotoxicity through an extracellular signal-regulated kinase pathway. J. Neurosci. Res. 2005; 80: 104–113.</mixed-citation></ref></ref-list></back></article>
