glun2b antagonist ro 25-6981 Search Results


ro 25 6981 maleate  (Tocris)
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Tocris ro 25 6981 maleate
Ro 25 6981 Maleate, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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glun2b blocker ro 25 6981  (Tocris)
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Tocris glun2b blocker ro 25 6981
Corticosterone alters surface <t>GluN2B-NMDAR</t> clustering. ( A ) Dendritic fragments of GluN2A- and GluN2B-SEP expressing neurons before and after exposure to corticosterone (100 nM). Scale bar = 5 µm, scale bar inset = 1 µm. ( B ) Example of fluorescence intensity of GluN2A- (n = 12 dendritic fields, N = 5 neurons) and GluN2B-SEP (n = 15 dendritic fields, N = 5 neurons) clusters over time. ( C ) Comparison of GluN2A- and GluN2B-SEP cluster fluorescence intensity before and after exposure to corticosterone. ***p < 0.001, paired Student t-test. ( D ) Live immunostaining of GluN2A and GluN2B subunits in Homer 1c-DsRed expressing neurons. Scale bar = 10 µm, scale bar inset = 5 µm. ( E ) Immunostaining of surface GluN2A and GluN2B subunits before and after exposure to corticosterone. Scale bar = 5 µm. ( F ) Comparison of the fluorescence intensity of GluN2A (n = 12 dendritic fields, N = 5 neurons) and GluN2B (n = 11 dendritic fields, N = 5 neurons) subunit clusters (expressed as ratio) -SEP before and after exposure to corticosterone (50 nM, 20 min). *p < 0.05, Student t-test.
Glun2b Blocker Ro 25 6981, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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glun2b antagonist ro 25 6981  (TargetMol)
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TargetMol glun2b antagonist ro 25 6981
Fig. 5. The pro-survival effect of <t>GluN2B</t> and its transcriptional upregulation by THSG following OGD/R. (A) The relative mRNA levels of GluN2A and GluN2B in neurons after OGD/R by real-time PCR (n = 3, from independent experiments). (B) Cell viability in different concentrations of PEAQX and <t>Ro</t> <t>25–6981</t> by CCK-8 (n = 3, from independent experiments). (C) Effect of PEAQX (0.27 μM) and Ro 25–6981(0.9 nM) on autophagic flux and the number of autophagosomes (yellow column) and autolysosomes in neurons (red column), Bar: 40 μm (n = 3). (D) The relative mRNA levels of GluN2B after THSG treatment. The cells were treated with 1 μM THSG. Statistical comparisons were performed with one-way ANOVA. ###p < 0.001 vs. control group. *p < 0.05, ***p < 0.001 vs. model group. Data are shown as the mean ± SEM.
Glun2b Antagonist Ro 25 6981, supplied by TargetMol, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/glun2b+antagonist+ro+25-6981/Ro+25-6981/pm38677275-61-33-39
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Image Search Results


Corticosterone alters surface GluN2B-NMDAR clustering. ( A ) Dendritic fragments of GluN2A- and GluN2B-SEP expressing neurons before and after exposure to corticosterone (100 nM). Scale bar = 5 µm, scale bar inset = 1 µm. ( B ) Example of fluorescence intensity of GluN2A- (n = 12 dendritic fields, N = 5 neurons) and GluN2B-SEP (n = 15 dendritic fields, N = 5 neurons) clusters over time. ( C ) Comparison of GluN2A- and GluN2B-SEP cluster fluorescence intensity before and after exposure to corticosterone. ***p < 0.001, paired Student t-test. ( D ) Live immunostaining of GluN2A and GluN2B subunits in Homer 1c-DsRed expressing neurons. Scale bar = 10 µm, scale bar inset = 5 µm. ( E ) Immunostaining of surface GluN2A and GluN2B subunits before and after exposure to corticosterone. Scale bar = 5 µm. ( F ) Comparison of the fluorescence intensity of GluN2A (n = 12 dendritic fields, N = 5 neurons) and GluN2B (n = 11 dendritic fields, N = 5 neurons) subunit clusters (expressed as ratio) -SEP before and after exposure to corticosterone (50 nM, 20 min). *p < 0.05, Student t-test.

Journal: Scientific Reports

Article Title: Stress hormone rapidly tunes synaptic NMDA receptor through membrane dynamics and mineralocorticoid signalling

doi: 10.1038/s41598-017-08695-3

Figure Lengend Snippet: Corticosterone alters surface GluN2B-NMDAR clustering. ( A ) Dendritic fragments of GluN2A- and GluN2B-SEP expressing neurons before and after exposure to corticosterone (100 nM). Scale bar = 5 µm, scale bar inset = 1 µm. ( B ) Example of fluorescence intensity of GluN2A- (n = 12 dendritic fields, N = 5 neurons) and GluN2B-SEP (n = 15 dendritic fields, N = 5 neurons) clusters over time. ( C ) Comparison of GluN2A- and GluN2B-SEP cluster fluorescence intensity before and after exposure to corticosterone. ***p < 0.001, paired Student t-test. ( D ) Live immunostaining of GluN2A and GluN2B subunits in Homer 1c-DsRed expressing neurons. Scale bar = 10 µm, scale bar inset = 5 µm. ( E ) Immunostaining of surface GluN2A and GluN2B subunits before and after exposure to corticosterone. Scale bar = 5 µm. ( F ) Comparison of the fluorescence intensity of GluN2A (n = 12 dendritic fields, N = 5 neurons) and GluN2B (n = 11 dendritic fields, N = 5 neurons) subunit clusters (expressed as ratio) -SEP before and after exposure to corticosterone (50 nM, 20 min). *p < 0.05, Student t-test.

Article Snippet: In a separate series of experiments, testing the involvement of GluN2B subunits, the selective GluN2B- blocker Ro 25–6981 (3 μM, Tocris) or vehicle (DMSO) was also directly added into the extracellular solution while recording.

Techniques: Expressing, Fluorescence, Comparison, Immunostaining

Corticosterone specifically decreases the surface dynamics of GluN2B-NMDAR in hippocampal neurons exposed to corticosterone. ( A ) Representative trajectories of single GluN2A- and GluN2B-NMDAR in hippocampal neurons (DIC images) exposed to either buffer or corticosterone (100 nM, 20 min). Scale bar, 5 µm; scale bar inset, 1 µm. ( B ) Comparison of the cumulative distributions of GluN2A- (buffer, n = 112 trajectories; corticosterone, n = 143 trajectories) and GluN2B-NMDAR (buffer, n = 189 trajectories; corticosterone, n = 191 trajectories) instantaneous diffusion coefficients in buffer and corticosterone conditions. ***p < 0.001, Kolmogorov-Smirnov test.

Journal: Scientific Reports

Article Title: Stress hormone rapidly tunes synaptic NMDA receptor through membrane dynamics and mineralocorticoid signalling

doi: 10.1038/s41598-017-08695-3

Figure Lengend Snippet: Corticosterone specifically decreases the surface dynamics of GluN2B-NMDAR in hippocampal neurons exposed to corticosterone. ( A ) Representative trajectories of single GluN2A- and GluN2B-NMDAR in hippocampal neurons (DIC images) exposed to either buffer or corticosterone (100 nM, 20 min). Scale bar, 5 µm; scale bar inset, 1 µm. ( B ) Comparison of the cumulative distributions of GluN2A- (buffer, n = 112 trajectories; corticosterone, n = 143 trajectories) and GluN2B-NMDAR (buffer, n = 189 trajectories; corticosterone, n = 191 trajectories) instantaneous diffusion coefficients in buffer and corticosterone conditions. ***p < 0.001, Kolmogorov-Smirnov test.

Article Snippet: In a separate series of experiments, testing the involvement of GluN2B subunits, the selective GluN2B- blocker Ro 25–6981 (3 μM, Tocris) or vehicle (DMSO) was also directly added into the extracellular solution while recording.

Techniques: Comparison, Diffusion-based Assay

Aldosterone, a MR activator, alters the surface distribution and dynamics of GluN2B-NMDAR. ( A ) Dendritic fragments of GluN2B-SEP expressing neurons before and after exposure to aldosterone (10 nM). Scale bar = 5 µm, scale bar inset = 1 µm. ( B ) Example of fluorescence intensity of GluN2B-SEP clusters over time, before and after aldosterone application. ( C ) Comparison of GluN2B-SEP cluster fluorescence intensity before and after exposure to aldosterone (10 nM, 25 min exposure; n = 10 dendritic fields, N = 5 neurons). ***p < 0.001, paired Student t-test. ( D ) Representative trajectories of single GluN2B-NMDAR in hippocampal neurons (DIC images) exposed to either buffer solution, aldosterone (10 nM, 20 min), corticosterone BSA (50 nM, 20 min), or RU28392 (GR agonist, 50 nM, 20 min). Scale bar, 5 µm. ( E ) Comparison of the cumulative distributions of GluN2B-NMDAR instantaneous diffusion coefficients between aldosterone (buffer, n = 214 trajectories; aldosterone, n = 225 trajectories), corticosterone BSA (buffer, n = 539 trajectories; 5min corticosterone BSA, n = 855 trajectories; 20min corticosterone BSA, n = 864 trajectories), or RU28392 (buffer, n = 229 trajectories; 5min RU28392, n = 175 trajectories; 20min RU28392, n = 119 trajectories). ***p < 0.001, Kolmogorov-Smirnov test.

Journal: Scientific Reports

Article Title: Stress hormone rapidly tunes synaptic NMDA receptor through membrane dynamics and mineralocorticoid signalling

doi: 10.1038/s41598-017-08695-3

Figure Lengend Snippet: Aldosterone, a MR activator, alters the surface distribution and dynamics of GluN2B-NMDAR. ( A ) Dendritic fragments of GluN2B-SEP expressing neurons before and after exposure to aldosterone (10 nM). Scale bar = 5 µm, scale bar inset = 1 µm. ( B ) Example of fluorescence intensity of GluN2B-SEP clusters over time, before and after aldosterone application. ( C ) Comparison of GluN2B-SEP cluster fluorescence intensity before and after exposure to aldosterone (10 nM, 25 min exposure; n = 10 dendritic fields, N = 5 neurons). ***p < 0.001, paired Student t-test. ( D ) Representative trajectories of single GluN2B-NMDAR in hippocampal neurons (DIC images) exposed to either buffer solution, aldosterone (10 nM, 20 min), corticosterone BSA (50 nM, 20 min), or RU28392 (GR agonist, 50 nM, 20 min). Scale bar, 5 µm. ( E ) Comparison of the cumulative distributions of GluN2B-NMDAR instantaneous diffusion coefficients between aldosterone (buffer, n = 214 trajectories; aldosterone, n = 225 trajectories), corticosterone BSA (buffer, n = 539 trajectories; 5min corticosterone BSA, n = 855 trajectories; 20min corticosterone BSA, n = 864 trajectories), or RU28392 (buffer, n = 229 trajectories; 5min RU28392, n = 175 trajectories; 20min RU28392, n = 119 trajectories). ***p < 0.001, Kolmogorov-Smirnov test.

Article Snippet: In a separate series of experiments, testing the involvement of GluN2B subunits, the selective GluN2B- blocker Ro 25–6981 (3 μM, Tocris) or vehicle (DMSO) was also directly added into the extracellular solution while recording.

Techniques: Expressing, Fluorescence, Comparison, Diffusion-based Assay

Corticosterone and aldosterone decrease GluN2B-NMDAR surface dynamics within synapses. ( A ) Representative trajectories of surface GluN2B-NMDAR in hippocampal synapses exposed to either buffer solution, aldosterone (10 nM, 20 min), or corticosterone (100 nM, 20 min). Scale bar, 200 nm. ( B ) Comparison of the synaptic GluN2B-NMDAR instantaneous diffusion coefficients between buffer and corticosterone (buffer, n = 141 trajectories; corticosterone, n = 138 trajectories), and buffer and aldosterone (buffer, n = 291 trajectories; aldosterone, n = 402 trajectories). Data are expressed as median diffusion coefficient ±25–75% IQR. *p < 0.05, two-tailed Mann-Whitney test.

Journal: Scientific Reports

Article Title: Stress hormone rapidly tunes synaptic NMDA receptor through membrane dynamics and mineralocorticoid signalling

doi: 10.1038/s41598-017-08695-3

Figure Lengend Snippet: Corticosterone and aldosterone decrease GluN2B-NMDAR surface dynamics within synapses. ( A ) Representative trajectories of surface GluN2B-NMDAR in hippocampal synapses exposed to either buffer solution, aldosterone (10 nM, 20 min), or corticosterone (100 nM, 20 min). Scale bar, 200 nm. ( B ) Comparison of the synaptic GluN2B-NMDAR instantaneous diffusion coefficients between buffer and corticosterone (buffer, n = 141 trajectories; corticosterone, n = 138 trajectories), and buffer and aldosterone (buffer, n = 291 trajectories; aldosterone, n = 402 trajectories). Data are expressed as median diffusion coefficient ±25–75% IQR. *p < 0.05, two-tailed Mann-Whitney test.

Article Snippet: In a separate series of experiments, testing the involvement of GluN2B subunits, the selective GluN2B- blocker Ro 25–6981 (3 μM, Tocris) or vehicle (DMSO) was also directly added into the extracellular solution while recording.

Techniques: Comparison, Diffusion-based Assay, Two Tailed Test, MANN-WHITNEY

Fig. 5. The pro-survival effect of GluN2B and its transcriptional upregulation by THSG following OGD/R. (A) The relative mRNA levels of GluN2A and GluN2B in neurons after OGD/R by real-time PCR (n = 3, from independent experiments). (B) Cell viability in different concentrations of PEAQX and Ro 25–6981 by CCK-8 (n = 3, from independent experiments). (C) Effect of PEAQX (0.27 μM) and Ro 25–6981(0.9 nM) on autophagic flux and the number of autophagosomes (yellow column) and autolysosomes in neurons (red column), Bar: 40 μm (n = 3). (D) The relative mRNA levels of GluN2B after THSG treatment. The cells were treated with 1 μM THSG. Statistical comparisons were performed with one-way ANOVA. ###p < 0.001 vs. control group. *p < 0.05, ***p < 0.001 vs. model group. Data are shown as the mean ± SEM.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 5. The pro-survival effect of GluN2B and its transcriptional upregulation by THSG following OGD/R. (A) The relative mRNA levels of GluN2A and GluN2B in neurons after OGD/R by real-time PCR (n = 3, from independent experiments). (B) Cell viability in different concentrations of PEAQX and Ro 25–6981 by CCK-8 (n = 3, from independent experiments). (C) Effect of PEAQX (0.27 μM) and Ro 25–6981(0.9 nM) on autophagic flux and the number of autophagosomes (yellow column) and autolysosomes in neurons (red column), Bar: 40 μm (n = 3). (D) The relative mRNA levels of GluN2B after THSG treatment. The cells were treated with 1 μM THSG. Statistical comparisons were performed with one-way ANOVA. ###p < 0.001 vs. control group. *p < 0.05, ***p < 0.001 vs. model group. Data are shown as the mean ± SEM.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Real-time Polymerase Chain Reaction, CCK-8 Assay, Control

Fig. 6. Upregulation of GluN2B protein by THSG and the reversion of Ro 25–6981. (A-B) Expression of GluN2B in penumbra or in primary neurons after CI/R by WB and the Semi-quantitation (n = 3). (C) Representative TTC-stained brain slices and brain infarct volumes of each group shown in bar graph (n = 6). (D) neurological deficit scores of each group shown in bar graph (n = 6). (E) HE and Nissl staining showing neuron injury in rats after CI/R (blue arrows indicate nuclear pyknosis, green arrows indicate neuronal edema and black arrows indicate Nissl bodies). Bar: 2000 μm (upper panels), 80 μm, (lower panels). (F) Expression of Bcl-2, Bax, Caspase-3 in penumbra by WB and the semi-quantitation (n = 3). (G) Cell viability by CCK8 (n = 3). (H) Expression of Bcl-2, Bax, Caspase-3 in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in C-F and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in B, G-H. Statistical comparisons were performed with one-way ANOVA. ##p < 0.01, ###p < 0.001 vs. control group. *p < 0.05, **p < 0.01, ***p < 0.001 vs. model group. &p < 0.05, &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 6. Upregulation of GluN2B protein by THSG and the reversion of Ro 25–6981. (A-B) Expression of GluN2B in penumbra or in primary neurons after CI/R by WB and the Semi-quantitation (n = 3). (C) Representative TTC-stained brain slices and brain infarct volumes of each group shown in bar graph (n = 6). (D) neurological deficit scores of each group shown in bar graph (n = 6). (E) HE and Nissl staining showing neuron injury in rats after CI/R (blue arrows indicate nuclear pyknosis, green arrows indicate neuronal edema and black arrows indicate Nissl bodies). Bar: 2000 μm (upper panels), 80 μm, (lower panels). (F) Expression of Bcl-2, Bax, Caspase-3 in penumbra by WB and the semi-quantitation (n = 3). (G) Cell viability by CCK8 (n = 3). (H) Expression of Bcl-2, Bax, Caspase-3 in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in C-F and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in B, G-H. Statistical comparisons were performed with one-way ANOVA. ##p < 0.01, ###p < 0.001 vs. control group. *p < 0.05, **p < 0.01, ***p < 0.001 vs. model group. &p < 0.05, &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Expressing, Quantitation Assay, Staining, Control

Fig. 7. The activation of PINK1/PARK2 pathway by THSG treatment and the reversion of Ro 25–6981. (A) PARK2 level in neurons of penumbra by IF. Bar: 100 μm. (B) Expression of PINK1, PARK2 in penumbra by WB and the semi-quantitation (n = 3). (C) The colocalization of PARK2 with mitochondria in neurons after OGD/R. Bar: 10 μm. (D) Expression of PINK1, PARK2 in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in A-B and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in C-D. Statistical comparisons were performed with one-way ANOVA. #p < 0.05, ###p < 0.001 vs. control group. *p < 0.05, **p < 0.01, ***p < 0.001 vs. model group. &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 7. The activation of PINK1/PARK2 pathway by THSG treatment and the reversion of Ro 25–6981. (A) PARK2 level in neurons of penumbra by IF. Bar: 100 μm. (B) Expression of PINK1, PARK2 in penumbra by WB and the semi-quantitation (n = 3). (C) The colocalization of PARK2 with mitochondria in neurons after OGD/R. Bar: 10 μm. (D) Expression of PINK1, PARK2 in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in A-B and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in C-D. Statistical comparisons were performed with one-way ANOVA. #p < 0.05, ###p < 0.001 vs. control group. *p < 0.05, **p < 0.01, ***p < 0.001 vs. model group. &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Activation Assay, Expressing, Quantitation Assay, Control

Fig. 9. The upregulation of CaMKII and ERK1/2 phosphorylation by THSG and the reversion of Ro 25–6981. (A) Expression of ERK1/2, P-ERK1/2, CaMKII and P- CaMKII in penumbra by WB and the semi-quantitation (n = 3). (B) P-ERK1/2 level in neurons after OGD/R by IF, Bar: 20 μm. (C) Expression of ERK1/2, P-ERK1/2, CaMKII and P-CaMKII in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in A, and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in B-C. Statistical comparisons were performed with one-way ANOVA. ###p < 0.001 vs. control group. *p < 0.05, ***p < 0.001 vs. model group. &p < 0.05, &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 9. The upregulation of CaMKII and ERK1/2 phosphorylation by THSG and the reversion of Ro 25–6981. (A) Expression of ERK1/2, P-ERK1/2, CaMKII and P- CaMKII in penumbra by WB and the semi-quantitation (n = 3). (B) P-ERK1/2 level in neurons after OGD/R by IF, Bar: 20 μm. (C) Expression of ERK1/2, P-ERK1/2, CaMKII and P-CaMKII in neurons after OGD/R by WB and the semi-quantitation (n = 3). The rats were treated with 10 mg/kg Ro 25–6981 in A, and the cells were administrated with 1 μM THSG and 0.9 nM Ro 25–6981 in B-C. Statistical comparisons were performed with one-way ANOVA. ###p < 0.001 vs. control group. *p < 0.05, ***p < 0.001 vs. model group. &p < 0.05, &&p < 0.01, &&&p < 0.001 vs. THSG group. Data are shown as the mean ± SEM.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Phospho-proteomics, Expressing, Quantitation Assay, Control

Fig. 11. The neuroprotective effect of THSG against CI/R injury and the underlying mechanisms. THSG promotes the expression of GluN2B, induces the phos phorylation of CaMKII and ERK1/2, enhances the PINK1/PARK2-mediated mitophagy and suppresses the apoptosis of neurons in CI/R injury.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 11. The neuroprotective effect of THSG against CI/R injury and the underlying mechanisms. THSG promotes the expression of GluN2B, induces the phos phorylation of CaMKII and ERK1/2, enhances the PINK1/PARK2-mediated mitophagy and suppresses the apoptosis of neurons in CI/R injury.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Expressing

Fig. 10. Molecular docking analysis of the interaction between THSG and GluN2B. (A) Structure of GluN2B protein from PDB(ID-4PE5). (B) Predicted binding energy and binding values. (C) Docking complex of GluN2B protein with THSG.

Journal: Phytomedicine : international journal of phytotherapy and phytopharmacology

Article Title: THSG alleviates cerebral ischemia/reperfusion injury via the GluN2B-CaMKII-ERK1/2 pathway.

doi: 10.1016/j.phymed.2024.155595

Figure Lengend Snippet: Fig. 10. Molecular docking analysis of the interaction between THSG and GluN2B. (A) Structure of GluN2B protein from PDB(ID-4PE5). (B) Predicted binding energy and binding values. (C) Docking complex of GluN2B protein with THSG.

Article Snippet: At the onset of reperfusion, the rats were administered THSG (10, 20, and 40 mg/kg; Topscience, T4956; purity: 98 % determined by highperformance liquid chromatography; chemical structure displayed in Fig. 1B) and the GluN2B antagonist Ro 25–6981 (10 mg/kg; Topscience, T12758) via intraperitoneal injection, and salvianic acid A sodium (SAS) (30 mg/kg, Selleck, S2401; purity: 98 % determined by highperformance liquid chromatography) intravenously.

Techniques: Binding Assay