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Glutamate Receptor

Glutamate Receptors are a class of ionotropic and metabotropic receptors that bind the neurotransmitter glutamate, a key excitatory signaling molecule in the mammalian central nervous system.
These receptors play crucial roles in neuronal communication, synaptic plasticity, and various neurological processes.
Thhey are involved in a range of functions, including learning, memory, and excitotoxicity, and have been implicated in the pathology of numerous neurological and psychiatric disorders.
Understanding the structure, function, and regulation of Glutamate Receptors is essential for advancing research and developing targeted therapeutic interventions in the field of neuroscience.

Most cited protocols related to «Glutamate Receptor»

1
Quantitative PCR Analysis of Gene Expression
Cited 21 times
qPCR was performed in triplicate on the same microdissected frozen tissue samples subjected to the RNA amplification procedures. Samples were assayed on a real-time PCR cycler (7900HT, Applied Biosystems). Mouse TaqMan hydrolysis probes designed against the AMPA glutamate receptor subunit 1 (GRIA1) (Mn00514377_m1), beta actin (ACTB; Mm00447557_m1), and glyceraldehyde-3 phosphate dehydrogenase (GAPDH; Hs00266705_g1) were utilized (Applied Biosystems). Standard curves and cycle threshold (Ct) were generated using standards obtained from total mouse brain RNA. The ddCT method was employed to determine relative gene level differences. A total of 3-4 independent samples per RNA concentration were assayed in triplicate. Negative controls were used for each assay, and consisted of the reaction mixture without input RNA.
Alldred M.J., Che S, & Ginsberg S.D. (2008). Terminal Continuation (TC) RNA Amplification Enables Expression Profiling Using Minute RNA Input Obtained from Mouse Brain. International Journal of Molecular Sciences, 9(11), 2091-2104.
Publication 2008
alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid AMPA Receptors beta-Actin Biological Assay Brain Freezing GAPDH protein, human Genes Glutamate Glutamate Receptor Glyceraldehyde-3-Phosphate Dehydrogenases Hydrolysis Mice, House Protein Subunits Real-Time Polymerase Chain Reaction RNA Amplification Techniques Tissues
2
Membrane Protein Dynamics in a Realistic Plasma Membrane
Cited 12 times
The detailed methods are described in the Supporting Information. In summary, we embedded 10 membrane proteins in
a previously characterized model of the plasma membrane.20 (link) The starting structures of the 10 membrane proteins
simulated in this study were taken from the Protein Data Bank or obtained
from the corresponding publication: aquaporin-1 (AQP1, PDB ID 1J4N);98 (link) prostaglandin H2 synthase (COX1, PDB ID 1Q4G);99 (link) the dopamine transporter (DAT, PDB ID 4M48);44 (link) the epidermal growth factor receptor (EGFR);77 (link) AMPA-sensitive glutamate receptor 2 (GluA2,
PDB ID 3KG2);100 (link) glucose transporter 1 (GluT1, PDB ID 4PYP);101 (link) voltage-dependent Shaker potassium channel 1.2 (Kv1.2,
PDB ID 3LUT,102 (link) residues 32 to 4421 for each monomer); sodium,
potassium pump (Na,K-ATPase, PDB ID 4HYT);103 (link) δ-opioid
receptor (δ-OPR, PDB ID 4N6H);104 (link) and P-glycoprotein
(P-gp, PDB ID 4M1M).105 (link) In each system, four copies of each
protein were included and positioned at a distance of ca. 20 nm from
each other. Proteins were simulated using standard Martini protocols
with minor variations between systems to accommodate system-specific
issues (Supporting Information). The following
lipid classes were included: cholesterol (CHOL), in both leaflets;
charged lipids phosphatidylserine (PS), phosphatidic acid (PA), phosphatidylinositol
(PI), and the PI-phosphate, PI-bisphosphate, and PI-trisphosphate
(PIPs) placed in the inner leaflet; and ganglioside (GM) in the outer
leaflet. The zwitterionic phosphatidylcholine (PC), phosphatidylethanolamine
(PE), and sphingomyelin (SM) lipids were placed in both leaflets,
with PC and SM primarily in the outer leaflet and PE in the inner
leaflet. Ceramide (CER), diacylglycerol (DAG), and lysophosphatidylcholine
(LPC) lipids were also included, with all the LPC in the inner leaflet,
and CER and DAG primarily in the outer leaflet. The details of the
Martini lipids used in this study can be found on the Martini Lipidome
webpage (http://www.cgmartini.nl/index.php/force-field-parameters/lipids) and are described by Ingolfsson et al., and Wassenaar et al.20 (link),106 (link) The exact lipid composition of each system is given in the Supporting Information. The systems are ca. 42
× 42 nm in the membrane plane (x and y), including 4 proteins and ca. 6000 lipids.
Production
runs were performed in the presence of weak position
restraints applied to the protein backbone beads, with a force constant
of 1 kJ mol–1 nm–2, preventing
proteins from associating with each other. Each of the systems has
been simulated for 30 μs, which turned out to be adequate to
obtain convergence of major lipid components in the lipid shells around
the individual copies of the proteins (Supporting Information). Additional control simulations were performed
in the AQP1 system, in order to test the effects of simulation length,
position restraints on the proteins, lipid composition, and water
model on the results of lipid composition near the proteins (Supporting Information).
Simulations were
performed using the GROMACS simulation package
version 4.6.3,107 (link) with the Martini v2.2
force field parameters,62 (link),63 (link) and standard simulation
settings.108 (link) Additional details are provided
in Supporting Information. All the analyses
were performed on the last 5 μs of each simulation system.
Corradi V., Mendez-Villuendas E., Ingólfsson H.I., Gu R.X., Siuda I., Melo M.N., Moussatova A., DeGagné L.J., Sejdiu B.I., Singh G., Wassenaar T.A., Delgado Magnero K., Marrink S.J, & Tieleman D.P. (2018). Lipid–Protein Interactions Are Unique Fingerprints for Membrane Proteins. ACS Central Science, 4(6), 709-717.
Publication 2018
Adenosinetriphosphatase alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid AMPA Receptors AQP1 protein, human Aquaporin 1 Cell Membrane Proteins Ceramides Cholesterol Debility Diacylglycerol Dopamine Transporter Epidermal Growth Factor Receptor Gangliosides Glucose Transporter Glutamate Glutamate Receptor Lipids Lysophosphatidylcholines Na(+)-K(+)-Exchanging ATPase P-Glycoproteins Phosphates Phosphatidic Acid Phosphatidylcholines phosphatidylethanolamine Phosphatidylinositols Phosphatidylserines Potassium Channel Proteins PTGS1 protein, human SLC2A1 protein, human Sphingomyelins Tissue, Membrane Vertebral Column
3
Quantitative PCR Analysis of Hippocampal Genes
Cited 11 times

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Publication 2008
alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid AMPA Receptors Anabolism beta-Actin Brain Freezing GAPDH protein, human Genes, Housekeeping Glutamate Glutamate Receptor Glyceraldehyde-3-Phosphate Dehydrogenases Homo sapiens Hydrolysis Mice, Laboratory neuro-oncological ventral antigen 2, human Proteins Protein Subunits Real-Time Polymerase Chain Reaction RNA Amplification Techniques Synaptophysin Technique, Dilution Tissues
4
Postnatal Rat Cochlear Explant Culture
Cited 8 times
Protocols for all experiments involving animals were approved by the University Animal Care and Use Committee. Postnatal day 4–6 (P4–P6) rat cochleae of both sexes were dissected in ice-cold PBS. The membranous labyrinth was separated from the modiolus and the stria vascularis and spiral ligament were carefully removed. With the organ of Corti and spiral ganglion kept intact, Reissner’s membrane and tectorial membrane were removed with fine forceps. Only the middle part of the middle turn was used for each culture in our studies to avoid differing region-specific effects of neurotrophins. The explants were placed in a well on a coverglass (Lab-Tek #155411 multichambered coverglass system) coated with polyornithine (100 μg/ml) and laminin (20 μg/ml), to which they adhere. The cultures were evaluated the following day using DIC optics for adhesion to the substrate. Explants that failed to completely adhere to the cover slip were discarded; all others were used for these experiments.
Unless otherwise indicated, the explants were cultured in N2-supplemented DMEM with 10% fetal bovine serum at 37°, 6.5% CO2. The explants can be cultured for at least two weeks (data not shown); however, in this paper we used cultures of, at most 4, days in vitro (DIV). All procedures, including imaging, were performed in the culture well with the explants remaining attached to the cover slip. This facilitates preservation of the morphology.
To cause excitotoxic trauma, we exposed the explants, after 24 h in culture (1 DIV), to glutamate receptor agonists NMDA (0.5 mM, Tocris, Ellisville, MO, cat. #0114) and kainic acid (0.5 mM, Tocris, cat. #0222 or Sigma, Saint Louis, MO, cat. #K2389) for 2 h (“NK” treatment). Following NK treatment, the explants were maintained up to 72 h (4 DIV in total) in control culture medium or in culture medium containing BDNF (3.6 nM, Invitrogen, cat. #10908010) or NT-3 (3.6 nM, Sigma, cat. #N1905) or TrkC-IgG protein (2 μg/ml) or TrkB-IgG protein (2 μg/ml). The cultures were then fixed and prepared for immunofluorescence (IF).
Wang Q, & Green S.H. (2011). Functional Role of Neurotrophin-3 in Synapse Regeneration by Spiral Ganglion Neurons on Inner Hair Cells after Excitotoxic Trauma In Vitro. The Journal of Neuroscience, 31(21), 7938-7949.
Publication 2011
agonists Animals Biologic Preservation Cochlea Common Cold Culture Media Eye Fetal Bovine Serum Fluorescent Antibody Technique Forceps Ganglion of Corti Glutamate Receptor Kainic Acid Laminin Membranous Labyrinths N-Methylaspartate Nerve Growth Factors Neurotrophic Tyrosine Kinase Receptor Type 3 Organ of Corti polyornithine Proteins Spiral Ligament of Cochlea Stria Vascularis Tectorial Membrane Tissue, Membrane tropomyosin-related kinase-B, human Wounds and Injuries
5
Investigating Neuronal Electrophysiology and Synaptic Dynamics
Cited 7 times
The neurons were recorded by MultiClamp-700B amplifier under voltage-clamp for their synaptic activity and the current-clamp for their intrinsic property. Electrical signals were inputted to pClamp-10 (Axon Instrument Inc.) for data acquisition and analysis. An output bandwidth of the amplifier was set at 3kHz. The pipette solution for recording excitatory events included (mM) 150 K-gluconate, 5 NaCl, 5 HEPES, 0.4 EGTA, 4 Mg-ATP, 0.5 Tris-GTP, and 5 phosphocreatine (pH 7.35; Ge et al., 2011 (link); Yang et al., 2014 (link)). The solution for studying inhibitory synapses contained (mM) 130 K-gluconate, 20 KCl, 5 NaCl, 5 HEPES, 0.5 EGTA, 4 Mg-ATP, 0.5 Tris–GTP, and 5 phosphocreatine (F. Zhang et al., 2012 (link)). These pipette solutions were freshly made and filtered (0.1 μm). The osmolarity was 295 to 305 mOsmol and pipette resistance was 5 to 6 MΩ.
The functions of GABAergic neurons were assessed including their active intrinsic properties and inhibitory outputs (J.-H. Wang, 2003 (link)). The inhibitory outputs were assessed by recording spontaneous inhibitory postsynaptic currents (sIPSC) on glutamatergic neurons in the presence of 10 μM 6-Cyano-7-nitroquinoxaline-2,3-dione and 40 µM D-amino-5-phosphonovanolenic acid in the ACSF to block ionotropic glutamatergic receptors. A total of 10 µM bicuculline was washed onto the slices at the end of experiments for blocking sIPSCs to test that synaptic responses were mediated by GABAAR. The pipette solution with a high concentration of chloride ions makes the reversal potential -42 mV. sIPSCs are inward when membrane potential is held at -65 mV (Wei et al., 2004 (link); F. Zhang et al., 2012 (link)).
The functions of excitatory neurons were evaluated based on their active intrinsic properties and excitatory output (J.-H. Wang, 2003 (link)). The excitatory outputs were assessed by recording spontaneous excitatory postsynaptic currents (sEPSC) on GABAergic neurons in the presence of 10 µM bicuculline in the ACSF to block GABAAR (J.-H. Wang, 2003 (link); Yu et al., 2012 (link)). A total of 10 μM 6-cyano-7-nitroquinoxaline-2,3-dione and 40 µM D-amino-5-phosphonovanolenic acid were added into the ACSF at the end of experiments to test whether synaptic responses were mediated by glutamate receptor, which blocked sEPSCs in our studies.
The recording of spontaneous synaptic currents, instead of evoked synaptic currents, is based on the following reasons. sEPSC and sIPSC amplitudes represent the responsiveness and densities of postsynaptic receptors. The frequencies imply the probability of transmitter release from an axon terminal and the number of presynaptic axons innervated on the recorded neuron (Zucker and Regehr, 2002 (link); Stevens, 2004 (link)). Such parameters can be used to analyze presynaptic and postsynaptic mechanisms as well as to compare them with morphological data about neuronal interaction. The evoked postsynaptic currents cannot separate these mechanisms. We did not use tetrodotoxin in the ACSF to record miniature postsynaptic currents, since we had to record neuronal excitability. As the frequency of synaptic activities was less than those of sequential spikes (Figures 2, 4–5) and spontaneous spikes were never recorded on the neurons in our cortical slices, sIPSCs and sEPSCs were not generated from spontaneous action potentials. Synaptic events in our recording are presumably miniature postsynaptic currents. This point is granted by a single peak of postsynaptic currents in our study.
Action potentials at the cortical neurons were induced by injecting the depolarization pulse. Their excitability was assessed by input-outputs (spikes vs normalized stimuli) when various stimuli were given (Chen et al., 2006 (link)). We did not measure rheobase to show cellular excitability, as this strength-duration relationship was used to assess the ability to fire single spike. We measured the ability of firing sequential spikes (J. H. Wang et al., 2008 (link)).
Data were analyzed if the recorded neurons had the resting membrane potentials negatively more than -60 mV and action potential amplitudes more than 90 mV. The criteria for the acceptance of each experiment also included <5% changes in resting membrane potential, spike magnitude, and input resistance throughout each recording. The series and input resistances in all neurons were monitored by injecting hyperpolarization pulses (5 mV/50ms) and calculated by voltage pulses vs instantaneous and steady-state currents.
Xu A., Cui S, & Wang J.H. (2015). Incoordination among Subcellular Compartments Is Associated with Depression-Like Behavior Induced by Chronic Mild Stress. International Journal of Neuropsychopharmacology, 19(5), pyv122.
Publication 2015
Action Potentials Amino Acids ARID1A protein, human Axon Bicuculline Cells Chlorides Cortex, Cerebral Egtazic Acid Electricity Excitatory Postsynaptic Currents GABAergic Neurons gluconate Glutamate Receptor HEPES Inhibitory Postsynaptic Currents Ions Membrane Potentials Neurons Osmolarity Phosphocreatine Post-Synaptic Density Postsynaptic Current Psychological Inhibition Pulse Rate Pulses Resting Potentials Sodium Chloride Synapses Tetrodotoxin Tromethamine

Most recents protocols related to «Glutamate Receptor»

1
Striatal Synaptic Plasticity in Mice
Brains of slightly anesthetized mice (P21–P53; isoflurane) were prepared into ice-cold sucrose-based cutting solution (in mM: 85 sucrose, 60 NaCl, 3.5 KCl, 6 MgCl2, 0.5 CaCl2, 38 NaHCO3, 1.25 NaH2PO4, 10 HEPES, 25 glucose). Coronal slices (250 µm) were cut (Vibroslice 7000smz, Campden Instruments, UK), incubated in artificial cerebrospinal fluid (aCSF; in mM: 120 NaCl, 3.5 KCl, 1 MgCl2, 2 CaCl2, 30 NaHCO3, 1.25 NaH2PO4, 15 glucose) supplemented with 5 mM HEPES, 1 MgCl2 for 30 min at 35 °C and allowed to recover at room temperature for at least 40 min.
MSN were identified as in20 (link). They were recorded in the current clamp configuration with the bridge mode enabled (EPC-10 amplifier, Patch- and Fitmaster software; HEKA, Lambrecht, Germany). The internal solution contained (in mM): 150 K-gluconate, 10 NaCl, 3 Mg-ATP, 0.5 GTP, 10 HEPES and 0.05 EGTA adjusted to pH = 7.3 and 310 mOsm with the liquid junction potential (15 mV) corrected online. Slices were perfused (2–3 ml/min, aCSF, 21–24 °C) in presence of the GABAAR antagonist gabazine (SR-95531, 10 µM, Sigma). All solutions were continuously oxygenated with 95% O2, 5% CO2 gas.
Glutamatergic excitatory afferents where stimulated intrastriatally with aCSF-filled theta-glass electrodes typically ~ 100–150 µm away from the MSN soma (position of stimulation electrode between MSN and corpus callosum). A bipolar voltage pulse (0.1 ms, ± 5 to ± 30 V) at 0.2 Hz induced subthreshold excitatory postsynaptic potentials (EPSPs; 4–10 mV). Following 10–15 min baseline recording synaptic plasticity was induced by a high frequency protocol (four 100 Hz tetani, 3 s long, separated by 30 s; holding potential − 70 mV). Recordings were rejected if the membrane potential was more positive than − 80 mV or the input resistance changed by more than 30%. We verified that no background long-term potentiation was present as APV ((2R)-amino-5-phosphonovaleric acid), a specific blocker of a subtype of glutamate receptors, did not alter the effect in wildtype mice9 (link).
Bornschein U., Zeberg H., Enard W., Hevers W, & Pääbo S. (2023). Functional dissection of two amino acid substitutions unique to the human FOXP2 protein. Scientific Reports, 13, 3747.
Publication 2023
Amino Acids Bicarbonate, Sodium Brain Cerebrospinal Fluid Cold Temperature Corpus Callosum Egtazic Acid Excitatory Postsynaptic Potentials gabazine gluconate Glucose Glutamate Receptor HEPES Isoflurane Long-Term Potentiation Magnesium Chloride Membrane Potentials Mus Neuronal Plasticity Pulse Rate Sodium Chloride SR 95531 Sucrose
2
Optogenetically Evoked Inhibitory Currents in Nucleus Accumbens
Whole-cell patch-clamp recordings were obtained in the medial shell of the NAc (NAcSh). Data were collected with a Multiclamp 700B amplifier, Digidata 1550B (Molecular Devices, US), and using Clampex 11 (pClamp; Molecular Devices, US). All recordings were acquired in voltage clamp at 34° Celsius and were digitized at 10 kHz and low pass filtered at 2 kHz. Patch pipette was filled with internal solution containing (in mM): 143 CsCl, 10 HEPES, 0.25 EGTA, 5 Phosphocreatine, 4 MgATP, 0.3 NaGTP (295–305 mOsm, pH 7.4 with CsOH) and 1 mg/ml Neurobiotin (cat # SP-1120, Vector Labs, US). CNQX (50 μM, cat # 0190, Tocris Biosciences, UK) and AP5 (10 µM, cat # 0106, Tocris Biosciences, UK) were added to aCSF to block glutamate receptors. All pipettes (3–4 MΩ) were pulled from borosilicate glass (cat # PC-100, Narishige, US). Series resistance (Rs) was monitored throughout the recording for patch sealing. Once whole-cell configuration was obtained, holding potential was set at −70 mV and a 1 ms, 5 mW light pulse was delivered every 10 s (0.1 Hz) through a 40× objective. Once current response was obtained, picrotoxin (100 µM, cat # P1675, Sigma-Aldrich, US) was washed in the recording chamber to verify that optically evoked inhibitory postsynaptic current (oIPSC) was mediated by GABAa receptor activation. Once recording was complete slices were transferred to 4% PFA overnight at 4° Celsius then to 0.1 M PB for post hoc processing of Neurobiotin (cat # SP-1120, Vector Labs, US)51 (link).
Birnie M.T., Short A.K., de Carvalho G.B., Taniguchi L., Gunn B.G., Pham A.L., Itoga C.A., Xu X., Chen L.Y., Mahler S.V., Chen Y, & Baram T.Z. (2023). Stress-induced plasticity of a CRH/GABA projection disrupts reward behaviors in mice. Nature Communications, 14, 1088.
Publication 2023
6-Cyano-7-nitroquinoxaline-2,3-dione Adenosine Triphosphate, Magnesium Salt Cardiac Arrest Cells cesium chloride Cloning Vectors Egtazic Acid GABA-A Receptor Glutamate Receptor HEPES Inhibitory Postsynaptic Currents Light Medical Devices neurobiotin Phosphocreatine Picrotoxin Pulse Rate
3
Patch-clamp analysis of glutamate receptor-expressing HEK cells
Patch-clamp recordings of HEK cells co-expressing glutamate receptors and SnFR/SnFR-γ2/SnFR-γ8 were performed 2–3 days after transfection. Whole HEK293 cells were lifted into the outflow of a piezo-driven fast perfusion switcher for activation by glutamate. For whole-cell patch-clamp recordings, the external solution was composed as follows (in mM): 158 NaCl, 20 HEPES, 3 KCl, and 1 CaCl2 (pH 7.4). The intracellular (pipette) solution contained (in mM): 135 KCl, 20 KF, 20 HEPES, 3 NaCl, 1 MgCl2, and 2 Ethylene Glycol Tetraacetic Acid (EGTA) (pH 7.4). Pipettes had a resistance of 3–5 MΩ when filled with intracellular solution, and we used ISO-type pipette holders (G23 Instruments) to minimise pipette drift. After whole-cell configuration was obtained, cells were held at −50 mV and the currents were recorded using Axograph X (Axograph Scientific) via an Instrutech ITC-18 D-A interface (HEKA Elektronik). Excitation by a 488-nm diode laser (iChrome MLE, Toptica Photonics) for GFP was directed through a manual total internal reflection fluorescence (TIRF) input to an Olympus IX81 microscope. We used a ×40 Olympus objective (NA 0.6) for all recordings on HEK cells. Fluorescence intensities in response to 488-nm excitation were recorded sequentially with 20-ms exposure time, without binning, on a Prime 95B CMOS camera (Photometrics). Laser emission and camera exposure were triggered in hardware directly from the digitizer. Images were recorded with MicroManager (Edelstein et al., 2014 (link)) and analyzed with Fiji (Schindelin et al., 2012 (link)).
Hao Y., Toulmé E., König B., Rosenmund C, & Plested A.J. (2023). Targeted sensors for glutamatergic neurotransmission. eLife, 12, e84029.
Publication 2023
ARID1A protein, human Cells Chronic multifocal osteomyelitis Egtazic Acid Fluorescence Glutamate Glutamate Receptor HEK293 Cells HEPES Lasers, Semiconductor Magnesium Chloride Microscopy Perfusion Protoplasm Reflex Sodium Chloride Transfection
4
Labeling Seizure-Activated Adult-Born Neurons
Cited 1 time
Seizure-induced immediate-early gene, Arc, expression has been used for labeling adult-born, circuit-incorporated neurons, primarily due to synapse and glutamate receptor formation [68 (link)]. An intraperitoneal (i.p.) kainic acid injection (10 mg/kg; Sigma, St. Louis, MO, USA. Cat. No. K0250) was given to induce mice’s tonic and clonic seizures [69 (link)]. Such kainic acid treatment may strongly stimulate dorsal DG BrdU-labeled neurons via epileptic activation onto their newly-formed synapses with other extant ones [26 (link)]. Approximately 25–35 min after the kainic acid injection, mice exhibited initial seizure activity by exhibiting head nodding, followed by forelimb clonus, and progressively to a seizure stage, characterized by repeated rearing and falling episodes. An i.p. sodium pentobarbital (50 mg/kg, SCI Pharmtech, Inc., Taoyuan, Taiwan, Cat. No. 051100) was given 30 min after the onset of the stage 5 seizure [70 (link)] to prevent further seizures. Animals were then perfused 60 min after the injection. Their brains were removed and postfixed in a 4% paraformaldehyde solution overnight at 4 °C and subsequently cryoprotected in a 30% sucrose solution for 48 h at 4 °C. Coronal sections, at 20 μm thickness, were made using a microtome (Thermo Fisher Scientific, Cleveland, OH, USA, Model: CryoStar NX50 OP). Triple staining for BrdU, NeuN, and Arc was conducted using mouse anti-BrdU (1:500, Millipore, Temecula, CA, USA, Cat. No. B5002), rabbit anti-Arc (1:1000, Synaptic Systems, Goettingen, Germany, Cat. No. 156 003), and chicken anti-NeuN (1:100, Millipore, Temecula, CA, USA, Cat. No. ABN91) primary antibodies (Supplementary Table S1) in blocking buffer, and incubated with Alexa Fluor 488-conjugated sheep anti-mouse (1:500, Jackson ImmunoResearch, West Grove, PA, USA, Cat. No. 515-545-062), Alexa Fluor 594-conjugated goat anti-rabbit (1:1000, Jackson ImmunoResearch, West Grove, PA, USA, Cat. No. 111-585-045), and CF350 conjugated donkey anti-chicken (1:100, Sigma, St. Louis, MO, USA, Cat. No. SAB4600219) secondary antibodies (Supplementary Table S1) in PBS and imaged with an Olympus fluorescent microscope (Olympus, Tokyo, Japan, Model: IX71).
Sun L.H., Liao Y.H., Chan Y.H., Yu A.E., Wu C.H., Kuo I.T, & Yu L. (2023). Male Stressed Mice Having Behavioral Control Exhibit Escalations in Dorsal Dentate Adult-Born Neurons and Spatial Memory. International Journal of Molecular Sciences, 24(3), 1983.
Publication 2023
Adult Alexa594 alexa fluor 488 Animals Antibodies Brain Bromodeoxyuridine Buffers Chickens Childbirth Clonic Seizures Domestic Sheep Epilepsy Equus asinus Forelimb Genes, Immediate-Early Glutamate Receptor Goat Head Kainic Acid Microscopy Microtomy Mus Neurons paraform Pentobarbital Sodium Rabbits Seizures Sucrose Synapses
5
GABA and Glutamate Receptor Modulation in Mouse Brain Slices
Isoflurane (Patterson Veterinary)-anesthetized mice (30–45 days old; male and female) were euthanized by rapid decapitation and the brains were immediately removed, sectioned into 220 μm-thick coronal slices (Leica VT1000S, Vashaw Scientific, Roswell, GA, USA), and incubated for 60 min at 34 °C in preoxygenated (95% O2/5% CO2) aCSF consisting of (in mM): 126 NaCl, 2.5 KCl, 1.2 NaH2PO4, 1.2 MgCl2, 21.4 NaHCO3, and 11 d-glucose. The cutting solution also contained either the NMDA GLU antagonist MK801 (10 µM; (5S,10R)-(+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine; Abcam, Cambridge, UK) or the GLU antagonist kynurenic acid (2 mM) for the blockade of ionotropic GLU receptors. After incubation, the tissue was transferred to aCSF (34 °C) with kynurenic acid (2 mM) for recording the GABA currents (equilibrium potential approximately −40 mV) through sIPSCs or picrotoxin (100 µM) for recording sEPSCs. Kynurenic acid was used as a non-selective glutamate receptor blocker [78 (link),79 (link),80 (link)]. The following concentrations of drugs (acquired from either Sigma-Aldrich or Tocris Bioscience) were both applied for slice electrophysiology experiments where specified: the MOR agonist DAMGO (10 μM), the nonselective opioid receptor antagonist naloxone (1 μM), the cAMP phosphodiesterase inhibitor IBMX (100 μM), the adenosine A1R agonist N6CPA (1 μM), or the A1R antagonist DPCPX (300 nM).
Ronström J.W., Johnson N.L., Jones S.T., Werner S.J., Wadsworth H.A., Brundage J.N., Stolp V., Graziane N.M., Silberman Y., Steffensen S.C, & Yorgason J.T. (2023). Opioid-Induced Reductions in Amygdala Lateral Paracapsular GABA Neuron Circuit Activity. International Journal of Molecular Sciences, 24(3), 1929.
Publication 2023
1,3-dipropyl-8-cyclopentylxanthine 1-Methyl-3-isobutylxanthine Adenosine Bicarbonate, Sodium Brain Decapitation Enkephalin, Ala(2)-MePhe(4)-Gly(5)- Females gamma Aminobutyric Acid Glucose Glutamate Receptor Imines Isoflurane Kynurenic Acid Magnesium Chloride Males Mice, House MK-801 N-Methylaspartate Naloxone Narcotic Antagonists Pharmaceutical Preparations Phosphodiesterase Inhibitors Picrotoxin Sodium Chloride Tissues

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Lipofectamine 2000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Canada, Japan, France, Italy, Switzerland, Australia, Spain, Belgium, Denmark, Singapore, India, Netherlands, Sweden, New Zealand, Portugal, Poland, Israel, Lithuania, Hong Kong, Argentina, Ireland, Austria, Czechia, Cameroon, Taiwan, Province of China, Morocco
Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
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Quantity one software by Bio-Rad
Sourced in United States, China, Germany, Italy, United Kingdom, Spain, Japan, France, Canada, Sweden, Israel, Australia
Quantity One software is a powerful and versatile tool for analyzing and quantifying data from gel electrophoresis and imaging experiments. It provides a suite of analytical tools for researchers to accurately measure and compare the size, intensity, and other properties of bands or spots in their samples.
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Picrotoxin by Merck Group
Sourced in United States, United Kingdom, Germany, France, Sao Tome and Principe, Canada, Israel, Australia, Italy, Japan
Picrotoxin is a chemical compound that acts as a GABA antagonist. It is primarily used in scientific research as a tool to study the function of GABA receptors.
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4 aminopyridine 4 ap by Merck Group
Sourced in United States, United Kingdom, Brazil, Mexico
4-aminopyridine (4-AP) is a chemical compound used in research and laboratory settings. It serves as a potassium channel blocker, a function that is utilized in various scientific applications. The core purpose of 4-AP is to provide a tool for researchers to investigate and study physiological and biochemical processes.

More about "Glutamate Receptor"

Glutamate receptors are a critical component of the mammalian central nervous system, playing pivotal roles in neuronal communication, synaptic plasticity, and various neurological processes.
These ionotropic and metabotropic receptors bind the neurotransmitter glutamate, a key excitatory signaling molecule.
Understanding the structure, function, and regulation of glutamate receptors is essential for advancing research and developing targeted therapeutic interventions in the field of neuroscience.
Glutamate receptors are involved in a range of functions, including learning, memory, and excitotoxicity.
They have been implicated in the pathology of numerous neurological and psychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and epilepsy.
Researchers often utilize various tools and techniques to study glutamate receptor-mediated signaling, including the use of mouse monoclonal antibodies (e.g., Mouse (IgG1) anti-CtBP2), fetal bovine serum (FBS), and pharmacological agents like tetrodotoxin (TTX), MK-801, bicuculline, and picrotoxin.
The Odyssey Infrared Imaging System and Quantity One software are commonly used to visualize and quantify the expression and distribution of glutamate receptors.
Additionally, lipid-based transfection reagents, such as Lipofectamine 2000, are employed to introduce genetic constructs into cells to investigate the functional and regulatory aspects of these receptors.
By leveraging the insights gained from the MeSH term description and the power of PubCompare.ai, researchers can optimize their glutamate receptor studies, locate the best procedures from literature, pre-prints, and patents, and enhance the reproducibility and accuracy of their findings.
Explore PubCompare.ai today and take your glutamate receptor research to new heights.