Cloning of a  -Serine-Regulated Transcript dsr-1 from the Rat Cerebral Cortex

Tsuchida, Hideto; Yamamoto, Naoki; Kajii, Yasushi; Umino, Asami; Fukui, Kenji; Nishikawa, Toru

doi:10.1006/bbrc.2001.4255

Cited by 10 publications

(18 citation statements)

References 31 publications

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“…We have recently isolated two novel transcripts, dsr-1 (D-serine-responsive transcript-1) 40) and dsr-2, 41) of which the expressions are selectively induced by D-serine but not by L-serine. A part of dsr-1 is homologous with the M9.2 gene that encodes the proton ATPase subunit, suggesting its possible involvement in the D-serine uptake and release.…”

Section: ) D-serine Responsive Novel Genesmentioning

confidence: 99%

“…A part of dsr-1 is homologous with the M9.2 gene that encodes the proton ATPase subunit, suggesting its possible involvement in the D-serine uptake and release. 40) Also, dsr-2 seems to be involved in the metabolism or functions of D-serine, because the mRNAs of dsr-2 are exclusively expressed in the brain and show a D-serine-and NMDA receptor R2B subunit-like distribution in the brain. (Fig.…”

Section: ) D-serine Responsive Novel Genesmentioning

confidence: 99%

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Metabolism and Functional Roles of Endogenous D-Serine in Mammalian Brains

Nishikawa

2005

Biological & Pharmaceutical Bulletin

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Section: ) D-serine Responsive Novel Genesmentioning

confidence: 99%

Section: ) D-serine Responsive Novel Genesmentioning

confidence: 99%

Metabolism and Functional Roles of Endogenous D-Serine in Mammalian Brains

Nishikawa

2005

Biological & Pharmaceutical Bulletin

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“…The cRNA probes were synthesized in the presence of 35 S-CTP and had a specific activity of 10 8 cpm/g RNA. In situ hybridization was performed on cryostat sections of rat brain (19).…”

Section: Methodsmentioning

confidence: 99%

“…Bicistronic mRNAs in mammalian brain are rare but do exist (35); however, there is no demonstration that both ORFs of previously identified bicistronic brain mRNA are coordinately translated.…”

Section: Pro1-pro2 Co-expression Needed For Formation Of a Tcp-bindingmentioning

confidence: 97%

A Rat Brain Bicistronic Gene with an Internal Ribosome Entry Site Codes for a Phencyclidine-binding Protein with Cytotoxic Activity

Hui

Kumar

Mach

et al. 2009

Journal of Biological Chemistry

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The cloning and characterization of the gene for the fourth subunit of a glutamate-binding protein complex in rat brain synaptic membranes are described. The cloned rat brain cDNA contained two open reading frames (ORFs) encoding 8.9-(PRO1) and 9.5-kDa (PRO2) proteins. The cDNA sequence matched contiguous genomic DNA sequences in rat chromosome 17. Both ORFs were expressed within the structure of a single brain mRNA and antibodies against unique sequences in PRO1-and PRO2-labeled brain neurons in situ, indicative of bicistronic gene expression. Dicistronic vectors in which ORF1 and ORF2 were substituted by either two different fluorescent proteins or two luciferases indicated concurrent, yet independent translation of the two ORFs. Transfection with noncapped mRNA led to cap-independent translation of only ORF2 through an internal ribosome entry sequence preceding ORF2. In vitro or cell expression of the cloned cDNA led to the formation of multimeric protein complexes containing both PRO1 and PRO2. These complexes had low affinity (؉)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine (MK-801)-sensitive phencyclidine-binding sites. Overexpression of PRO1 and PRO2 in CHO cells, but not neuroblastoma cells, caused cell death within 24 -48 h. The cytotoxicity was blocked by concurrent treatment with MK-801 or by two tetrahydroisoquinolines that bind to phencyclidine sites in neuronal membranes. Co-expression of two of the other subunits of the protein complex together with PRO1/PRO2 abrogated the cytotoxic effect without altering PRO1/PRO2 protein levels. Thus, this rare mammalian bicistronic gene coded for two tightly interacting brain proteins forming a low affinity phencyclidine-binding entity in a synaptic membrane complex.A complex of four proteins purified from brain synaptic membranes was shown to have recognition sites for L-glutamate, N-methyl-D-aspartate (NMDA), 4 and other ligands characteristic of NMDA receptors in brain, including binding sites for the co-agonist glycine, the modulator spermine, the competitive antagonist (ϩ)-3-(2-carboxypiperazin-4-yl)-propyl-1-phosphonic acid (CPP), and the ion channel inhibitors thienylcyclohexylpiperidine (TCP) and (ϩ)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine (MK-801) (1, 2). Reconstitution of the purified complex into planar lipid bilayer membranes leads to the formation of channels with four ion conductance levels upon activation by glutamate or NMDA in the presence of glycine (3). These conductances differ from either the predominant NMDA-activated receptor-ion channels of brain neurons or those formed by reconstitution of the NMDA receptor subunits (4), but are similar to those described for ion channels in rat spinal cord motor neurons (5).The genes for three of the proteins in this complex have been cloned and expressed in heterologous cells (6 -10). The gene GRINA for the glutamate-binding protein (GBP) subunit was identified as part of a "learning and memory" module of genes expressed in the entorhinal cortex of the mammalian b...

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“…In the mammalian brain, 7) D-serine serves as an endogenous ligand for the N-methyl-D-aspartate receptor and is related to the transcription of the gene encoding a putative membrane protein in the rat cerebral cortex. 8) There being stage-speciˆc changes in the D-serine and D-DAP concentrations implies that these two amino acids have some physiological functions in silkworm larvae.…”

Section: ) D-mentioning

confidence: 99%