Hostname: page-component-78c5997874-j824f Total loading time: 0 Render date: 2024-11-10T15:15:28.477Z Has data issue: false hasContentIssue false

Abnormalities in extracellular glycine and glutamate levels in the striatum of sandy mice

Published online by Cambridge University Press:  26 February 2013

Yuji Kitaichi
Affiliation:
Department of Psychiatry, Hokkaido University Graduate School of Medicine, Kita-ku, Sapporo, Japan
Ryota Hashimoto*
Affiliation:
Molecular Research Center for Children's Mental Development, United Graduate School of Child Development, Osaka University, Osaka, Japan Department of Psychiatry, Osaka University Graduate School of Medicine, Osaka, Japan Department of Mental Disorder Research, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan
Takeshi Inoue
Affiliation:
Department of Psychiatry, Hokkaido University Graduate School of Medicine, Kita-ku, Sapporo, Japan
Tomohiro Abekawa
Affiliation:
Department of Psychiatry, Hokkaido University Graduate School of Medicine, Kita-ku, Sapporo, Japan
Aya Kakuta
Affiliation:
Department of Psychiatry, Hokkaido University Graduate School of Medicine, Kita-ku, Sapporo, Japan
Satoko Hattori
Affiliation:
Department of Mental Disorder Research, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan
Tsukasa Koyama
Affiliation:
Department of Psychiatry, Hokkaido University Graduate School of Medicine, Kita-ku, Sapporo, Japan
*
Dr. Ryota Hashimoto, Molecular Research Center for Children's Mental Development, United Graduate School of Child Development, Osaka University, D3, 2-2, Yamadaoka, Suita, Osaka 565-0871, Japan. Tel: +81-6-6879-3074; Fax: +81-6-6879-3074; E-mail: hashimor@psy.med.osaka-u.ac.jp

Abstract

Objective

Glycine regulates glutamatergic neurotransmission, and several papers have reported the relationship between glycine and schizophrenia. The dysbindin-1 (DTNBP1: dystrobrevin-binding protein 1) gene is related to glutamatergic neurotransmission and has been found to be a strong candidate gene for schizophrenia. In this study, we clarified the relationship between dysbindin, glutamate, and glycine with in vivo microdialysis methods.

Methods

We measured extracellular glycine and glutamate levels in the striatum of sandy (sdy) mice using in vivo microdialysis methods. Sdy mice express no dysbindin protein owing to a deletion in the dysbindin-1 gene. In addition, we measured changes in those amino acids after methamphetamine (METH) administration.

Results

The basal levels of extracellular glycine and glutamate in the striatum of sdy mice were elevated. These extracellular glutamate levels decreased gradually after METH administration and were not subsequently different from those of wild-type mice.

Conclusions

These results suggest that dysbindin might modulate glycine and glutamate release in vivo.

Type
Original Articles
Copyright
Copyright © Scandinavian College of Neuropsychopharmacology 2013 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Yang, CR, Svensson, KA. Allosteric modulation of NMDA receptor via elevation of brain glycine and d-serine: the therapeutic potentials for schizophrenia. Pharmacol Ther 2008;120:317332.Google Scholar
2.Javitt, DC. Glutamatergic theories of schizophrenia. Isr J Psychiatry Relat Sci 2010;47:416.Google Scholar
3.Hons, J, Zirko, R, Ulrychova, M, Cermakova, E, Doubek, P, Libiger, J. Glycine serum level in schizophrenia: relation to negative symptoms. Psychiatry Res 2010;176:103108.Google Scholar
4.Labrie, V, Lipina, T, Roder, JC. Mice with reduced NMDA receptor glycine affinity model some of the negative symptoms of schizophrenia. Psychopharmacology (Berl) 2008;200:217230.CrossRefGoogle Scholar
5.Kanahara, N, Shimizu, E, Ohgake, Set al. Glycine and d-serine, but not d-cycloserine, attenuate prepulse inhibition deficits induced by NMDA receptor antagonist MK-801. Psychopharmacology (Berl) 2008;198:363374.Google Scholar
6.Allen, NC, Bagade, S, McQueen, MBet al. Systematic meta-analyses and field synopsis of genetic association studies in schizophrenia: the SzGene database. Nat Genet 2008;40:827834.Google Scholar
7.Talbot, K, Eidem, WL, Tinsley, CLet al. Dysbindin-1 is reduced in intrinsic, glutamatergic terminals of the hippocampal formation in schizophrenia. J Clin Invest 2004;113:13531363.Google Scholar
8.Weickert, CS, Straub, RE, McClintock, BWet al. Human dysbindin (DTNBP1) gene expression in normal brain and in schizophrenic prefrontal cortex and midbrain. Arch Gen Psychiatry 2004;61:544555.Google Scholar
9.Hashimoto, R, Noguchi, H, Hori, Het al. A genetic variation in the dysbindin gene (DTNBP1) is associated with memory performance in healthy controls. World J Biol Psychiatry 2010;11:431438.Google Scholar
10.Hashimoto, R, Noguchi, H, Hori, Het al. Association between the dysbindin gene (DTNBP1) and cognitive functions in Japanese subjects. Psychiatry Clin Neurosci 2009;63:550556.CrossRefGoogle ScholarPubMed
11.Olgiati, P, Mandelli, L, Lorenzi, Cet al. Schizophrenia: genetics, prevention and rehabilitation. Acta Neuropsychiatr 2009;21:109120.Google Scholar
12.Hattori, S, Murotani, T, Matsuzaki, Set al. Behavioral abnormalities and dopamine reductions in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia. Biochem Biophys Res Commun 2008;373:298302.CrossRefGoogle ScholarPubMed
13.Takao, K, Toyama, K, Nakanishi, Ket al. Impaired long-term memory retention and working memory in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia. Mol Brain 2008;1. doi:10.1186/1756-6606-1-11.Google Scholar
14.Nihonmatsu-Kikuchi, N, Hashimoto, R, Hattori, Set al. Reduced rate of neural differentiation in the dentate gyrus of adult dysbindin null (sandy) mouse. PLoS One 2011;6:e15886.Google Scholar
15.Kobayashi, K, Umeda-Yano, S, Yamamori, H, Takeda, M, Suzuki, H, Hashimoto, R. Correlated alterations in serotonergic and dopaminergic modulations at the hippocampal mossy fiber synapse in mice lacking dysbindin. PLoS One 2011;6:e18113.Google Scholar
16.Nagai, T, Kitahara, Y, Shiraki, Aet al. Dysfunction of dopamine release in the prefrontal cortex of dysbindin deficient sandy mice: an in vivo microdialysis study. Neurosci Lett 2010;470:134138.Google Scholar
17.Numakawa, T, Yagasaki, Y, Ishimoto, Tet al. Evidence of novel neuronal functions of dysbindin, a susceptibility gene for schizophrenia. Hum Mol Genet 2004;13:26992708.Google Scholar
18.Kishimoto, M, Ujike, H, Motohashi, Yet al. The dysbindin gene (DTNBP1) is associated with methamphetamine psychosis. Biol Psychiatry 2008;63:191196.Google Scholar
19.Abekawa, T, Ito, K, Nakagawa, S, Nakato, Y, Koyama, T. Olanzapine and risperidone block a high dose of methamphetamine-induced schizophrenia-like behavioral abnormalities and accompanied apoptosis in the medial prefrontal cortex. Schizophr Res 2008;101:8494.Google Scholar
20.Ito, K, Abekawa, T, Koyama, T. Relationship between development of cross-sensitization to MK-801 and delayed increases in glutamate levels in the nucleus accumbens induced by a high dose of methamphetamine. Psychopharmacology (Berl) 2006;187:293302.Google Scholar
21.Paxinos, G, Franklin, KBJ. The mouse brain in stereotaxic coordinates. San Diego: Academic Press, 2001.Google Scholar
22.Abekawa, T, Ito, K, Koyama, T. Role of the simultaneous enhancement of NMDA and dopamine D1 receptor-mediated neurotransmission in the effects of clozapine on phencyclidine-induced acute increases in glutamate levels in the rat medial prefrontal cortex. Naunyn Schmiedebergs Arch Pharmacol 2006;374:177193.Google Scholar
23.Chefer, VI, Shippenberg, TS. Paradoxical effects of prodynorphin gene deletion on basal and cocaine-evoked dopaminergic neurotransmission in the nucleus accumbens. Eur J Neurosci 2006;23:229238.Google Scholar
24.Feng, YQ, Zhou, ZY, He, Xet al. Dysbindin deficiency in sandy mice causes reduction of snapin and displays behaviors related to schizophrenia. Schizophr Res 2008;106:218228.Google Scholar
25.Hikita, T, Taya, S, Fujino, Yet al. Proteomic analysis reveals novel binding partners of dysbindin, a schizophrenia-related protein. J Neurochem 2009;110:15671574.CrossRefGoogle ScholarPubMed
26.Legendre, P. The glycinergic inhibitory synapse. Cell Mol Life Sci 2001;58:760793.CrossRefGoogle ScholarPubMed
27.Perry, KW, Falcone, JF, Fell, MJet al. Neurochemical and behavioral profiling of the selective GlyT1 inhibitors ALX5407 and LY2365109 indicate a preferential action in caudal vs. cortical brain areas. Neuropharmacology 2008;55:743754.Google Scholar
28.Labrie, V, Clapcote, SJ, Roder, JC. Mutant mice with reduced NMDA-NR1 glycine affinity or lack of d-amino acid oxidase function exhibit altered anxiety-like behaviors. Pharmacol Biochem Behav 2009;91:610620.Google Scholar
29.Shimazaki, T, Kaku, A, Chaki, S. d-Serine and a glycine transporter-1 inhibitor enhance social memory in rats. Psychopharmacology (Berl) 2010;209:263270.Google Scholar
30.Gaspar, PA, Bustamante, ML, Silva, H, Aboitiz, F. Molecular mechanisms underling glutamatergic dysfunction in schizophrenia: therapeutic implications. J Neurochem 2009;111:891900.Google Scholar
31.Abekawa, T, Ohmori, T, Koyama, T. Effects of repeated administration of a high dose of methamphetamine on dopamine and glutamate release in rat striatum and nucleus accumbens. Brain Res 1994;643:276281.CrossRefGoogle ScholarPubMed
32.Karlsgodt, KH, Robleto, K, Trantham-Davidson, Het al. Reduced dysbindin expression mediates N-methyl-d-aspartate receptor hypofunction and impaired working memory performance. Biol Psychiatry 2011;69:2834.Google Scholar
33.Dyck, B, Guest, K, Sookram, C, Basu, D, Johnson, R, Mishra, RK. PAOPA, a potent analogue of Pro–Leu–glycinamide and allosteric modulator of the dopamine D2 receptor, prevents NMDA receptor antagonist (MK-801)-induced deficits in social interaction in the rat: implications for the treatment of negative symptoms in schizophrenia. Schizophr Res 2011;125:8892.Google Scholar
34.Karlsson, RM, Tanaka, K, Saksida, LM, Bussey, TJ, Heilig, M, Holmes, A. Assessment of glutamate transporter GLAST (EAAT1)-deficient mice for phenotypes relevant to the negative and executive/cognitive symptoms of schizophrenia. Neuropsychopharmacology 2009;34:15781589.Google Scholar
35.Nestler, EJ, Hyman, SE, Malenka, RC, eds. Molecular neuropharmacology: a foundation for clinical neuroscience. New York: McGraw Hill, 2001.Google Scholar