rabbit anti gdh antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti gdh antibody
    Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic <t>enzymes</t> <t>(LCAD,</t> <t>GDH,</t> AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.
    Rabbit Anti Gdh Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Resveratrol mediates mitochondrial function through the sirtuin 3 pathway to improve abnormal metabolic remodeling in atrial fibrillation"

    Article Title: Resveratrol mediates mitochondrial function through the sirtuin 3 pathway to improve abnormal metabolic remodeling in atrial fibrillation

    Journal: European Journal of Histochemistry : EJH

    doi: 10.4081/ejh.2024.4004

    Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic enzymes (LCAD, GDH, AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.
    Figure Legend Snippet: Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic enzymes (LCAD, GDH, AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot

    gdh  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc gdh
    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation"

    Article Title: Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation

    Journal: Cell Proliferation

    doi: 10.1111/cpr.13324

    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Figure Legend Snippet: Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Techniques Used: Expressing, Activity Assay, Western Blot, ECAR Assay

    anti gdh mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gdh mab
    Anti Gdh Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti gdh mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gdh mab
    (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and <t>GDH</t> levels. HK, Hexokinase; G6PD, glucose-6-phosphate <t>dehydrogenase;</t> <t>GAPDH,</t> Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.
    Anti Gdh Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "GDAP1 loss of function inhibits the mitochondrial pyruvate dehydrogenase complex by altering the actin cytoskeleton"

    Article Title: GDAP1 loss of function inhibits the mitochondrial pyruvate dehydrogenase complex by altering the actin cytoskeleton

    Journal: bioRxiv

    doi: 10.1101/2021.03.04.433895

    (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and GDH levels. HK, Hexokinase; G6PD, glucose-6-phosphate dehydrogenase; GAPDH, Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.
    Figure Legend Snippet: (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and GDH levels. HK, Hexokinase; G6PD, glucose-6-phosphate dehydrogenase; GAPDH, Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.

    Techniques Used: Western Blot, Expressing, Luminescence Assay, Confocal Microscopy, Staining

    (a) Immunoblot of whole cell lysates from Ctrl and GDAP1 KD cells against Hexokinase 1 (HK1), HK2, Glucose-6-phosphate dehydrogenase (G6PD), Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), Pyruvate kinase M1/2 (PKM1/2), Pyruvate dehydrogenase (PDH), Lactate Dehydrogenase A (LDHA), Glutamate dehydrogenase (GDH). Sizes are indicated and actin served as loading control. n=3-7
    Figure Legend Snippet: (a) Immunoblot of whole cell lysates from Ctrl and GDAP1 KD cells against Hexokinase 1 (HK1), HK2, Glucose-6-phosphate dehydrogenase (G6PD), Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), Pyruvate kinase M1/2 (PKM1/2), Pyruvate dehydrogenase (PDH), Lactate Dehydrogenase A (LDHA), Glutamate dehydrogenase (GDH). Sizes are indicated and actin served as loading control. n=3-7

    Techniques Used: Western Blot

    gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc gdh
    ATM inhibition stimulated SIRT3 activity in DLBCL. ( A ) Expression of SIRT3 targets in DLBCL cell lines inhibited for ATM expression compared to non-target controls. Expression of these targets in ABC DLBCL cell lines (HLY AND SUDHL2) and GCB cell line (SUDHL6) is depicted and quantitated normalized expression is provided below. Protein expression was quantitated using Image J software. Protein expression in shATM-DLBCL cell lines is expressed as relative percentage expression compared to non-target control. Protein abundance data shown here is a representative from triplicate experiments that were initiated from independent cell cultures. ( B ) Effects of SIRT3 on <t>GDH</t> acetylation in ATM-WT and ATM deficient DLBCL cell line HLY. Western blotting was performed using AcK and GDH antibodies on immunoprecipitated (IP) GDH. Protein expression was quantitated using Image J software. Percentage of GDH acetylation normalized to total GDH expression is depicted. VDAC was used as input control loading. The images are representative of two independent experiments. All western blots were run under same experimental conditions. (C) GDH activity assay in GM control cells and DLBCL cell lines expressing nt-shRNA and ATM-shRNA, experiments were repeated three times and data are expressed as mean + SD, asterisks define significant difference *p < 0.05. ( D ) Percentage acetylation <t>of</t> <t>SOD2</t> as determined by Ack-68-SOD2 antibody in ATM CRISPR knock out (CKO) DLBCL cells compared to WT-ATM. The percentage decrease in acetylated SOD2 expression in ATM-CKO cells was estimated by normalizing the acetylated expression levels to total SOD2 levels in both wild type-ATM and ATM deficient DLBCL groups. The images are representative of two independent experiments. All western blots were run under same experimental conditions. ( E ) Representative density blots of FACs analysis showing percentage ROS accumulation in DLBCL transduced with GFP tagged lentiviral particles expressing nt-shRNA and ATM-shRNA. Experiment was repeated n = 3, data are expressed as mean + SD, asterisks define significant difference p < 0.05.
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "SIRT3, a metabolic target linked to ataxia-telangiectasia mutated (ATM) gene deficiency in diffuse large B-cell lymphoma"

    Article Title: SIRT3, a metabolic target linked to ataxia-telangiectasia mutated (ATM) gene deficiency in diffuse large B-cell lymphoma

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-78193-6

    ATM inhibition stimulated SIRT3 activity in DLBCL. ( A ) Expression of SIRT3 targets in DLBCL cell lines inhibited for ATM expression compared to non-target controls. Expression of these targets in ABC DLBCL cell lines (HLY AND SUDHL2) and GCB cell line (SUDHL6) is depicted and quantitated normalized expression is provided below. Protein expression was quantitated using Image J software. Protein expression in shATM-DLBCL cell lines is expressed as relative percentage expression compared to non-target control. Protein abundance data shown here is a representative from triplicate experiments that were initiated from independent cell cultures. ( B ) Effects of SIRT3 on GDH acetylation in ATM-WT and ATM deficient DLBCL cell line HLY. Western blotting was performed using AcK and GDH antibodies on immunoprecipitated (IP) GDH. Protein expression was quantitated using Image J software. Percentage of GDH acetylation normalized to total GDH expression is depicted. VDAC was used as input control loading. The images are representative of two independent experiments. All western blots were run under same experimental conditions. (C) GDH activity assay in GM control cells and DLBCL cell lines expressing nt-shRNA and ATM-shRNA, experiments were repeated three times and data are expressed as mean + SD, asterisks define significant difference *p < 0.05. ( D ) Percentage acetylation of SOD2 as determined by Ack-68-SOD2 antibody in ATM CRISPR knock out (CKO) DLBCL cells compared to WT-ATM. The percentage decrease in acetylated SOD2 expression in ATM-CKO cells was estimated by normalizing the acetylated expression levels to total SOD2 levels in both wild type-ATM and ATM deficient DLBCL groups. The images are representative of two independent experiments. All western blots were run under same experimental conditions. ( E ) Representative density blots of FACs analysis showing percentage ROS accumulation in DLBCL transduced with GFP tagged lentiviral particles expressing nt-shRNA and ATM-shRNA. Experiment was repeated n = 3, data are expressed as mean + SD, asterisks define significant difference p < 0.05.
    Figure Legend Snippet: ATM inhibition stimulated SIRT3 activity in DLBCL. ( A ) Expression of SIRT3 targets in DLBCL cell lines inhibited for ATM expression compared to non-target controls. Expression of these targets in ABC DLBCL cell lines (HLY AND SUDHL2) and GCB cell line (SUDHL6) is depicted and quantitated normalized expression is provided below. Protein expression was quantitated using Image J software. Protein expression in shATM-DLBCL cell lines is expressed as relative percentage expression compared to non-target control. Protein abundance data shown here is a representative from triplicate experiments that were initiated from independent cell cultures. ( B ) Effects of SIRT3 on GDH acetylation in ATM-WT and ATM deficient DLBCL cell line HLY. Western blotting was performed using AcK and GDH antibodies on immunoprecipitated (IP) GDH. Protein expression was quantitated using Image J software. Percentage of GDH acetylation normalized to total GDH expression is depicted. VDAC was used as input control loading. The images are representative of two independent experiments. All western blots were run under same experimental conditions. (C) GDH activity assay in GM control cells and DLBCL cell lines expressing nt-shRNA and ATM-shRNA, experiments were repeated three times and data are expressed as mean + SD, asterisks define significant difference *p < 0.05. ( D ) Percentage acetylation of SOD2 as determined by Ack-68-SOD2 antibody in ATM CRISPR knock out (CKO) DLBCL cells compared to WT-ATM. The percentage decrease in acetylated SOD2 expression in ATM-CKO cells was estimated by normalizing the acetylated expression levels to total SOD2 levels in both wild type-ATM and ATM deficient DLBCL groups. The images are representative of two independent experiments. All western blots were run under same experimental conditions. ( E ) Representative density blots of FACs analysis showing percentage ROS accumulation in DLBCL transduced with GFP tagged lentiviral particles expressing nt-shRNA and ATM-shRNA. Experiment was repeated n = 3, data are expressed as mean + SD, asterisks define significant difference p < 0.05.

    Techniques Used: Inhibition, Activity Assay, Expressing, Software, Western Blot, Immunoprecipitation, shRNA, CRISPR, Knock-Out, Transduction

    rabbit gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit gdh
    Acetylation of <t>GDH</t> ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), <t>and</t> <t>ADP/ATP</t> translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.
    Rabbit Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Rescue of myocardial energetic dysfunction in diabetes through the correction of mitochondrial hyperacetylation by honokiol"

    Article Title: Rescue of myocardial energetic dysfunction in diabetes through the correction of mitochondrial hyperacetylation by honokiol

    Journal: JCI Insight

    doi: 10.1172/jci.insight.140326

    Acetylation of GDH ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), and ADP/ATP translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.
    Figure Legend Snippet: Acetylation of GDH ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), and ADP/ATP translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.

    Techniques Used:

    rabbit glutamate dehydrogenase gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit glutamate dehydrogenase gdh
    Rabbit Glutamate Dehydrogenase Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit glutamate dehydrogenase gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit glutamate dehydrogenase gdh
    Rabbit Glutamate Dehydrogenase Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    total gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total gdh
    Total Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit glutamate dehydrogenase gdh  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit glutamate dehydrogenase gdh
    Rabbit Glutamate Dehydrogenase Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti gdh antibody
    Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic <t>enzymes</t> <t>(LCAD,</t> <t>GDH,</t> AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.
    Rabbit Anti Gdh Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
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    Acetylation of <t>GDH</t> ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), <t>and</t> <t>ADP/ATP</t> translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.
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    Image Search Results


    Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic enzymes (LCAD, GDH, AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.

    Journal: European Journal of Histochemistry : EJH

    Article Title: Resveratrol mediates mitochondrial function through the sirtuin 3 pathway to improve abnormal metabolic remodeling in atrial fibrillation

    doi: 10.4081/ejh.2024.4004

    Figure Lengend Snippet: Resveratrol regulates the acetylation of metabolic enzymes through a SIRT3-dependent pathway during AF. A ) The mRNA expression level of SIRT3 in HL-1 cells was detected by RT-qPCR. B,C ) Western blot analysis was used to detect the protein expression level of SIRT3 in HL-1 cells and analyze its gray value. D,G ) Western blotting was used to detect the acetylated protein level and gray value analysis of key metabolic enzymes (LCAD, GDH, AceCS2) in HL-1 cells; * p <0.05, ** p <0.01, *** p <0.001; n=3.

    Article Snippet: The membrane was blocked with Tween-Tris buffered brine (TTBS) containing 5% skim milk at room temperature for 2 h and then incubated with the following primary antibodies: SIRT3 (C73E3) rabbit mAb (2627, Cell Signaling Technology, Danvers, MA, USA), rabbit anti-LCAD antibody (2980, Cell Signaling Technology), rabbit anti-GDH antibody (12793, Cell Signaling Technology), rabbit anti-ACE2 antibody (92485, Cell Signaling Technology), and GAPDH (4970, Cell Signaling Technology).

    Techniques: Expressing, Quantitative RT-PCR, Western Blot

    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Journal: Cell Proliferation

    Article Title: Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation

    doi: 10.1111/cpr.13324

    Figure Lengend Snippet: Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Article Snippet: Primary antibodies employed in this study included β‐actin (1:1000, CW0096A, CWBIO), ALP (1:500, sc‐79840, Santa Cruz Biotechnology), Runx2 (1:1000, #12556, Cell Signalling), BMP2 (1:1000, ab14933, Abcam), TFAM (1:1000, sc‐376,672, Santa Cruz Biotechnology), total OXPHOS cocktail (1:1000, ab110413, Abcam), Glut1 (1:1000, er1510‐11, Huabio), GDH (1:1000, 12793S, Cell Signalling), and CPT1A (1:1000, 12252S, Cell Signalling).

    Techniques: Expressing, Activity Assay, Western Blot, ECAR Assay

    Acetylation of GDH ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), and ADP/ATP translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.

    Journal: JCI Insight

    Article Title: Rescue of myocardial energetic dysfunction in diabetes through the correction of mitochondrial hyperacetylation by honokiol

    doi: 10.1172/jci.insight.140326

    Figure Lengend Snippet: Acetylation of GDH ( A ), hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit α (HADHA) ( B ), and ADP/ATP translocase 1 (ANT1) ( C ) in SSM mitochondria. * P < 0.05 vs. control, # P < 0.05 vs. diabetic untreated, analyzed using a 2-way ANOVA with Holm-Sidak’s post hoc correction. See for example blots. GDH, glutamate dehydrogenase, T2D, type 2 diabetes; SSM, subsarcolemmal.

    Article Snippet: Protein expression was analyzed using the following primary antibodies: rabbit acetyl-lysine, rabbit GDH (12793 Cell Signaling), rabbit ADP/ATP translocase (ANT1, custom made by Eurogentec), and rabbit hydroxyacyl-CoA dehydrogenase (HADHA) from Protein-Tech (10758-1-AP).

    Techniques: