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β actin  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc β actin
    Aa aggravated PAN‐induced podocyte injury in vitro. Control podocytes were treated with PBS. PAN‐treated podocytes received 250 μM PAN for 24 h. PAN+AA‐treated podocytes received PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. AA‐treated podocytes received AA (5 × 10 −7 M) for 24 h. (A) Representative phalloidin staining images of F‐Actin (green) and nuclei (blue), with quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Western blot analysis and quantification of nephrin protein expression in cultured podocytes ( n = 6). Data are expressed as the mean ± SD and analysed by one‐way ANOVA with Bonferroni correction. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; ns, not significant.
    β Actin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 33988 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    β actin - by Bioz Stars, 2026-10
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    1) Product Images from "Arachidonic Acid Disrupts PKM2 ‐Linked Glycolysis‐Related Metabolism and Exacerbates PAN ‐Induced Podocyte Injury"

    Article Title: Arachidonic Acid Disrupts PKM2 ‐Linked Glycolysis‐Related Metabolism and Exacerbates PAN ‐Induced Podocyte Injury

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.71404

    Aa aggravated PAN‐induced podocyte injury in vitro. Control podocytes were treated with PBS. PAN‐treated podocytes received 250 μM PAN for 24 h. PAN+AA‐treated podocytes received PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. AA‐treated podocytes received AA (5 × 10 −7 M) for 24 h. (A) Representative phalloidin staining images of F‐Actin (green) and nuclei (blue), with quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Western blot analysis and quantification of nephrin protein expression in cultured podocytes ( n = 6). Data are expressed as the mean ± SD and analysed by one‐way ANOVA with Bonferroni correction. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; ns, not significant.
    Figure Legend Snippet: Aa aggravated PAN‐induced podocyte injury in vitro. Control podocytes were treated with PBS. PAN‐treated podocytes received 250 μM PAN for 24 h. PAN+AA‐treated podocytes received PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. AA‐treated podocytes received AA (5 × 10 −7 M) for 24 h. (A) Representative phalloidin staining images of F‐Actin (green) and nuclei (blue), with quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Western blot analysis and quantification of nephrin protein expression in cultured podocytes ( n = 6). Data are expressed as the mean ± SD and analysed by one‐way ANOVA with Bonferroni correction. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; ns, not significant.

    Techniques Used: In Vitro, Control, Staining, Western Blot, Analysis, Expressing, Cell Culture

    PKM2 Activation attenuated PAN + AA‐induced podocyte injury and mitochondrial dysfunction in vitro. PAN+AA‐treated podocytes were exposed to PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. PAN+AA+TEPP‐46‐treated podocytes were exposed to TEPP‐46 (10 μM) under PAN+AA conditions. T denotes TEPP‐46 in the figure. (A) Representative phalloidin staining images of F‐Actin and quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Representative TUNEL staining images and quantification of apoptotic podocytes ( n = 3). Scale bar, 50 μm. (C, D) Representative immunofluorescence images and quantification of PKM2 and phospho‐PKM2. Nephrin is shown in red, PKM2 or phospho‐PKM2 in green, and DAPI in blue ( n = 3). Scale bar, 20 μm. (E) Western blot analysis and quantification of PKM2 protein expression ( n = 6). (F) Western blot analysis and quantification of phospho‐PKM2 (p‐PKM2) protein expression ( n = 6). (G) Western blot analysis and quantification of TOM20 protein expression ( n = 6). (H) Representative immunofluorescence images and quantification of TOM20 ( n = 3). Scale bar, 20 μm. (I) Transmission electron microscopy images and quantification of mean mitochondrial area, cristae‐damage rate and mitochondrial damage score ( n = 3). Scale bar, 2.0 μm. (J) MitoTracker staining and quantification of mitochondrial fluorescence intensity ( n = 3). Scale bar, 20 μm. (K) JC‐1 staining and quantification of mitochondrial membrane potential ( n = 3). Scale bar, 20 μm. (L) Representative DCFH‐DA staining images and quantification of ROS levels ( n = 3). Scale bar, 20 μm. (M) PK activity, lactate production, pyruvate production and ATP levels ( n = 3). Data are expressed as mean ± SD. Statistical significance was determined by unpaired Student's t ‐test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: PKM2 Activation attenuated PAN + AA‐induced podocyte injury and mitochondrial dysfunction in vitro. PAN+AA‐treated podocytes were exposed to PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. PAN+AA+TEPP‐46‐treated podocytes were exposed to TEPP‐46 (10 μM) under PAN+AA conditions. T denotes TEPP‐46 in the figure. (A) Representative phalloidin staining images of F‐Actin and quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Representative TUNEL staining images and quantification of apoptotic podocytes ( n = 3). Scale bar, 50 μm. (C, D) Representative immunofluorescence images and quantification of PKM2 and phospho‐PKM2. Nephrin is shown in red, PKM2 or phospho‐PKM2 in green, and DAPI in blue ( n = 3). Scale bar, 20 μm. (E) Western blot analysis and quantification of PKM2 protein expression ( n = 6). (F) Western blot analysis and quantification of phospho‐PKM2 (p‐PKM2) protein expression ( n = 6). (G) Western blot analysis and quantification of TOM20 protein expression ( n = 6). (H) Representative immunofluorescence images and quantification of TOM20 ( n = 3). Scale bar, 20 μm. (I) Transmission electron microscopy images and quantification of mean mitochondrial area, cristae‐damage rate and mitochondrial damage score ( n = 3). Scale bar, 2.0 μm. (J) MitoTracker staining and quantification of mitochondrial fluorescence intensity ( n = 3). Scale bar, 20 μm. (K) JC‐1 staining and quantification of mitochondrial membrane potential ( n = 3). Scale bar, 20 μm. (L) Representative DCFH‐DA staining images and quantification of ROS levels ( n = 3). Scale bar, 20 μm. (M) PK activity, lactate production, pyruvate production and ATP levels ( n = 3). Data are expressed as mean ± SD. Statistical significance was determined by unpaired Student's t ‐test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Techniques Used: Activation Assay, In Vitro, Staining, TUNEL Assay, Immunofluorescence, Western Blot, Analysis, Expressing, Transmission Assay, Electron Microscopy, Fluorescence, Membrane, Activity Assay

    Proposed working model of AA‐associated aggravation of PAN‐induced podocyte injury. Based on our previous study, AA may activate the PKA‐c‐Abl‐nephrin axis and contribute to nephrin phosphorylation and actin cytoskeletal remodelling. In the present study, PAN+AA was associated with reduced PKM2 abundance, increased PKM2 Tyr105 phosphorylation, decreased PK activity, lower pyruvate/lactate/ATP levels, mitochondrial injury, ROS accumulation and apoptosis. These cytoskeletal and metabolic stress pathways may converge to aggravate podocyte injury and proteinuria. Potential crosstalk between these pathways is proposed, but the sequence and causal relationship remain to be experimentally validated.
    Figure Legend Snippet: Proposed working model of AA‐associated aggravation of PAN‐induced podocyte injury. Based on our previous study, AA may activate the PKA‐c‐Abl‐nephrin axis and contribute to nephrin phosphorylation and actin cytoskeletal remodelling. In the present study, PAN+AA was associated with reduced PKM2 abundance, increased PKM2 Tyr105 phosphorylation, decreased PK activity, lower pyruvate/lactate/ATP levels, mitochondrial injury, ROS accumulation and apoptosis. These cytoskeletal and metabolic stress pathways may converge to aggravate podocyte injury and proteinuria. Potential crosstalk between these pathways is proposed, but the sequence and causal relationship remain to be experimentally validated.

    Techniques Used: Phospho-proteomics, Cytoskeletal, Activity Assay, Sequencing

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    Article Title: Extracellular biogenic nanoscale mitochondria reprogram the wound microenvironment via ROS scavenging independent of cellular uptake
    Article Snippet: Equal amounts of protein samples were separated by SDS-PAGE and transferred onto PVDF membranes (Millipore). .. After blocking with 5% non-fat milk, membranes were incubated overnight at 4 °C with the following primary antibodies: anti-PINK1 (CST, Cat# 6946), anti-NIX (CST, Cat# 12396), anti-TOM20 (CST, Cat# 42406), anti-USP30 (Proteintech, Cat# 15402-1-AP), Total OXPHOS Rodent WB Antibody Cocktail (Abcam, Cat# ab110413), anti-phospho-AKT (Ser473) (CST, Cat# 4060), and anti-β-actin (CST, Cat# 4967). .. After incubation with appropriate HRP-conjugated secondary antibodies, signals were developed using an enhanced chemiluminescence (ECL) kit (Thermo Fisher, Cat#34580) and imaged with a chemiluminescence detection system (Tanon).

    Article Title: TGIF2-mediated HMGB3 overexpression promotes esophageal squamous cell carcinoma proliferation and metastasis through TLR3/TGF-β signaling
    Article Snippet: Next, proteins were transferred to nitrocellulose membranes (Millipore; Temecula, California, USA). .. Afterward, before incubation with primary antibodies overnight at 4 °C, membranes were blocked with 5% non-fat milk at 37 °C for 1 h. Subsequently, membranes were treated with horseradish peroxidase-conjugated secondary antibodies against rabbit or mouse IgG (Abcam, Massachusetts, USA, 1:5000) at 37 °C for 1 h. The following primary antibodies were used to assess the expression of proteins: anti-β-actin (#3700; Cell Signaling Technology, Massachusetts, USA, 1:5000), anti-TGIF2 (#ab190152; Abcam, 1:1000), anti-p-TGIF2 and TGIF2 (#sc-390870; Santa Cruz, CA, USA), anti-HMGB3 (#ab75782; Abcam, 1:1000), anti-TLR3 (#ab62566; Abcam, 1:1000), anti-TGF-β (#ab215715; Abcam , 1:1000), anti-SMAD2/3 (#8685; Cell Signaling Technology, 1:1000), anti-SMAD2 (#5339; Cell Signaling Technology, 1:1000), anti-p-SMAD2 (#3108; Cell Signaling Technology, 1:1000), anti-SMAD3 (#9523; Cell Signaling Technology, 1:1000), anti-p-SMAD3 (#9520; Cell Signaling Technology, 1:1000), anti-extracellular signal-regulated kinase 1/2 (ERK1/2) (#4695; Cell Signaling Technology, 1:1000), anti-p-ERK1/2 (#4370; Cell Signaling Technology, 1:1000), anti-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kB) P65 (#8242S; Cell Signaling Technology, 1:1000), and anti-His-tag (#66005-1-Ig; protein-tech, 1:1000). .. Protein bands were quantified using ImageJ densitometry software, with β-actin serving as the loading control for normalization of target protein expression levels.

    Blocking Assay:

    Article Title: Extracellular biogenic nanoscale mitochondria reprogram the wound microenvironment via ROS scavenging independent of cellular uptake
    Article Snippet: Equal amounts of protein samples were separated by SDS-PAGE and transferred onto PVDF membranes (Millipore). .. After blocking with 5% non-fat milk, membranes were incubated overnight at 4 °C with the following primary antibodies: anti-PINK1 (CST, Cat# 6946), anti-NIX (CST, Cat# 12396), anti-TOM20 (CST, Cat# 42406), anti-USP30 (Proteintech, Cat# 15402-1-AP), Total OXPHOS Rodent WB Antibody Cocktail (Abcam, Cat# ab110413), anti-phospho-AKT (Ser473) (CST, Cat# 4060), and anti-β-actin (CST, Cat# 4967). .. After incubation with appropriate HRP-conjugated secondary antibodies, signals were developed using an enhanced chemiluminescence (ECL) kit (Thermo Fisher, Cat#34580) and imaged with a chemiluminescence detection system (Tanon).

    Western Blot:

    Article Title: Extracellular biogenic nanoscale mitochondria reprogram the wound microenvironment via ROS scavenging independent of cellular uptake
    Article Snippet: Equal amounts of protein samples were separated by SDS-PAGE and transferred onto PVDF membranes (Millipore). .. After blocking with 5% non-fat milk, membranes were incubated overnight at 4 °C with the following primary antibodies: anti-PINK1 (CST, Cat# 6946), anti-NIX (CST, Cat# 12396), anti-TOM20 (CST, Cat# 42406), anti-USP30 (Proteintech, Cat# 15402-1-AP), Total OXPHOS Rodent WB Antibody Cocktail (Abcam, Cat# ab110413), anti-phospho-AKT (Ser473) (CST, Cat# 4060), and anti-β-actin (CST, Cat# 4967). .. After incubation with appropriate HRP-conjugated secondary antibodies, signals were developed using an enhanced chemiluminescence (ECL) kit (Thermo Fisher, Cat#34580) and imaged with a chemiluminescence detection system (Tanon).

    Expressing:

    Article Title: TGIF2-mediated HMGB3 overexpression promotes esophageal squamous cell carcinoma proliferation and metastasis through TLR3/TGF-β signaling
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    Cell-Signaling:

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    Ubiquitin Proteomics:

    Article Title: Omaveloxolone functions as a molecular crowbar-like degrader of STING to alleviate aging-related inflammation
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    Recurrent sleep restriction decreases levels of the ZO-1 protein in the cerebral cortex during aging. A Representative blots of each protein in the cortex using <t>β-actin</t> as a load control. B Normalized levels expressed as relative fold change of the ZO-1 and C occludin proteins. D Representative blots of each protein in the hippocampus using β-actin as a load control. E Normalized levels expressed as relative fold change of the ZO-1 and F occludin proteins. Data are presented as mean ± SEM. Two-way ANOVA, followed by Tukey’s test for multiple comparisons ( n = 4 per group, in duplicate). * p < 0.05, ** p < 0.001, *** p < 0.0001
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    Recurrent sleep restriction decreases levels of the ZO-1 protein in the cerebral cortex during aging. A Representative blots of each protein in the cortex using <t>β-actin</t> as a load control. B Normalized levels expressed as relative fold change of the ZO-1 and C occludin proteins. D Representative blots of each protein in the hippocampus using β-actin as a load control. E Normalized levels expressed as relative fold change of the ZO-1 and F occludin proteins. Data are presented as mean ± SEM. Two-way ANOVA, followed by Tukey’s test for multiple comparisons ( n = 4 per group, in duplicate). * p < 0.05, ** p < 0.001, *** p < 0.0001
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    Recurrent sleep restriction decreases levels of the ZO-1 protein in the cerebral cortex during aging. A Representative blots of each protein in the cortex using <t>β-actin</t> as a load control. B Normalized levels expressed as relative fold change of the ZO-1 and C occludin proteins. D Representative blots of each protein in the hippocampus using β-actin as a load control. E Normalized levels expressed as relative fold change of the ZO-1 and F occludin proteins. Data are presented as mean ± SEM. Two-way ANOVA, followed by Tukey’s test for multiple comparisons ( n = 4 per group, in duplicate). * p < 0.05, ** p < 0.001, *** p < 0.0001
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    Image Search Results


    Aa aggravated PAN‐induced podocyte injury in vitro. Control podocytes were treated with PBS. PAN‐treated podocytes received 250 μM PAN for 24 h. PAN+AA‐treated podocytes received PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. AA‐treated podocytes received AA (5 × 10 −7 M) for 24 h. (A) Representative phalloidin staining images of F‐Actin (green) and nuclei (blue), with quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Western blot analysis and quantification of nephrin protein expression in cultured podocytes ( n = 6). Data are expressed as the mean ± SD and analysed by one‐way ANOVA with Bonferroni correction. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; ns, not significant.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Arachidonic Acid Disrupts PKM2 ‐Linked Glycolysis‐Related Metabolism and Exacerbates PAN ‐Induced Podocyte Injury

    doi: 10.1111/jcmm.71404

    Figure Lengend Snippet: Aa aggravated PAN‐induced podocyte injury in vitro. Control podocytes were treated with PBS. PAN‐treated podocytes received 250 μM PAN for 24 h. PAN+AA‐treated podocytes received PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. AA‐treated podocytes received AA (5 × 10 −7 M) for 24 h. (A) Representative phalloidin staining images of F‐Actin (green) and nuclei (blue), with quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Western blot analysis and quantification of nephrin protein expression in cultured podocytes ( n = 6). Data are expressed as the mean ± SD and analysed by one‐way ANOVA with Bonferroni correction. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; ns, not significant.

    Article Snippet: Membranes were incubated overnight at 4°C with primary antibodies against β‐actin (1:2000, Sigma‐Aldrich, MO, USA), nephrin (1:500, PROGEN), PKM1 (1:1000, Abcam), PKM2 (1:1000, Proteintech), phospho‐PKM2 (Tyr105 1:1000, Proteintech), β‐actin (1:1000, CST), and TOMM20 (1:1000, CST).

    Techniques: In Vitro, Control, Staining, Western Blot, Analysis, Expressing, Cell Culture

    PKM2 Activation attenuated PAN + AA‐induced podocyte injury and mitochondrial dysfunction in vitro. PAN+AA‐treated podocytes were exposed to PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. PAN+AA+TEPP‐46‐treated podocytes were exposed to TEPP‐46 (10 μM) under PAN+AA conditions. T denotes TEPP‐46 in the figure. (A) Representative phalloidin staining images of F‐Actin and quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Representative TUNEL staining images and quantification of apoptotic podocytes ( n = 3). Scale bar, 50 μm. (C, D) Representative immunofluorescence images and quantification of PKM2 and phospho‐PKM2. Nephrin is shown in red, PKM2 or phospho‐PKM2 in green, and DAPI in blue ( n = 3). Scale bar, 20 μm. (E) Western blot analysis and quantification of PKM2 protein expression ( n = 6). (F) Western blot analysis and quantification of phospho‐PKM2 (p‐PKM2) protein expression ( n = 6). (G) Western blot analysis and quantification of TOM20 protein expression ( n = 6). (H) Representative immunofluorescence images and quantification of TOM20 ( n = 3). Scale bar, 20 μm. (I) Transmission electron microscopy images and quantification of mean mitochondrial area, cristae‐damage rate and mitochondrial damage score ( n = 3). Scale bar, 2.0 μm. (J) MitoTracker staining and quantification of mitochondrial fluorescence intensity ( n = 3). Scale bar, 20 μm. (K) JC‐1 staining and quantification of mitochondrial membrane potential ( n = 3). Scale bar, 20 μm. (L) Representative DCFH‐DA staining images and quantification of ROS levels ( n = 3). Scale bar, 20 μm. (M) PK activity, lactate production, pyruvate production and ATP levels ( n = 3). Data are expressed as mean ± SD. Statistical significance was determined by unpaired Student's t ‐test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Arachidonic Acid Disrupts PKM2 ‐Linked Glycolysis‐Related Metabolism and Exacerbates PAN ‐Induced Podocyte Injury

    doi: 10.1111/jcmm.71404

    Figure Lengend Snippet: PKM2 Activation attenuated PAN + AA‐induced podocyte injury and mitochondrial dysfunction in vitro. PAN+AA‐treated podocytes were exposed to PAN (250 μM) and AA (5 × 10 −7 M) for 24 h. PAN+AA+TEPP‐46‐treated podocytes were exposed to TEPP‐46 (10 μM) under PAN+AA conditions. T denotes TEPP‐46 in the figure. (A) Representative phalloidin staining images of F‐Actin and quantification of F‐Actin mean intensity per cell ( n = 3). Scale bar, 20 μm. (B) Representative TUNEL staining images and quantification of apoptotic podocytes ( n = 3). Scale bar, 50 μm. (C, D) Representative immunofluorescence images and quantification of PKM2 and phospho‐PKM2. Nephrin is shown in red, PKM2 or phospho‐PKM2 in green, and DAPI in blue ( n = 3). Scale bar, 20 μm. (E) Western blot analysis and quantification of PKM2 protein expression ( n = 6). (F) Western blot analysis and quantification of phospho‐PKM2 (p‐PKM2) protein expression ( n = 6). (G) Western blot analysis and quantification of TOM20 protein expression ( n = 6). (H) Representative immunofluorescence images and quantification of TOM20 ( n = 3). Scale bar, 20 μm. (I) Transmission electron microscopy images and quantification of mean mitochondrial area, cristae‐damage rate and mitochondrial damage score ( n = 3). Scale bar, 2.0 μm. (J) MitoTracker staining and quantification of mitochondrial fluorescence intensity ( n = 3). Scale bar, 20 μm. (K) JC‐1 staining and quantification of mitochondrial membrane potential ( n = 3). Scale bar, 20 μm. (L) Representative DCFH‐DA staining images and quantification of ROS levels ( n = 3). Scale bar, 20 μm. (M) PK activity, lactate production, pyruvate production and ATP levels ( n = 3). Data are expressed as mean ± SD. Statistical significance was determined by unpaired Student's t ‐test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Membranes were incubated overnight at 4°C with primary antibodies against β‐actin (1:2000, Sigma‐Aldrich, MO, USA), nephrin (1:500, PROGEN), PKM1 (1:1000, Abcam), PKM2 (1:1000, Proteintech), phospho‐PKM2 (Tyr105 1:1000, Proteintech), β‐actin (1:1000, CST), and TOMM20 (1:1000, CST).

    Techniques: Activation Assay, In Vitro, Staining, TUNEL Assay, Immunofluorescence, Western Blot, Analysis, Expressing, Transmission Assay, Electron Microscopy, Fluorescence, Membrane, Activity Assay

    Proposed working model of AA‐associated aggravation of PAN‐induced podocyte injury. Based on our previous study, AA may activate the PKA‐c‐Abl‐nephrin axis and contribute to nephrin phosphorylation and actin cytoskeletal remodelling. In the present study, PAN+AA was associated with reduced PKM2 abundance, increased PKM2 Tyr105 phosphorylation, decreased PK activity, lower pyruvate/lactate/ATP levels, mitochondrial injury, ROS accumulation and apoptosis. These cytoskeletal and metabolic stress pathways may converge to aggravate podocyte injury and proteinuria. Potential crosstalk between these pathways is proposed, but the sequence and causal relationship remain to be experimentally validated.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Arachidonic Acid Disrupts PKM2 ‐Linked Glycolysis‐Related Metabolism and Exacerbates PAN ‐Induced Podocyte Injury

    doi: 10.1111/jcmm.71404

    Figure Lengend Snippet: Proposed working model of AA‐associated aggravation of PAN‐induced podocyte injury. Based on our previous study, AA may activate the PKA‐c‐Abl‐nephrin axis and contribute to nephrin phosphorylation and actin cytoskeletal remodelling. In the present study, PAN+AA was associated with reduced PKM2 abundance, increased PKM2 Tyr105 phosphorylation, decreased PK activity, lower pyruvate/lactate/ATP levels, mitochondrial injury, ROS accumulation and apoptosis. These cytoskeletal and metabolic stress pathways may converge to aggravate podocyte injury and proteinuria. Potential crosstalk between these pathways is proposed, but the sequence and causal relationship remain to be experimentally validated.

    Article Snippet: Membranes were incubated overnight at 4°C with primary antibodies against β‐actin (1:2000, Sigma‐Aldrich, MO, USA), nephrin (1:500, PROGEN), PKM1 (1:1000, Abcam), PKM2 (1:1000, Proteintech), phospho‐PKM2 (Tyr105 1:1000, Proteintech), β‐actin (1:1000, CST), and TOMM20 (1:1000, CST).

    Techniques: Phospho-proteomics, Cytoskeletal, Activity Assay, Sequencing

    Recurrent sleep restriction decreases levels of the ZO-1 protein in the cerebral cortex during aging. A Representative blots of each protein in the cortex using β-actin as a load control. B Normalized levels expressed as relative fold change of the ZO-1 and C occludin proteins. D Representative blots of each protein in the hippocampus using β-actin as a load control. E Normalized levels expressed as relative fold change of the ZO-1 and F occludin proteins. Data are presented as mean ± SEM. Two-way ANOVA, followed by Tukey’s test for multiple comparisons ( n = 4 per group, in duplicate). * p < 0.05, ** p < 0.001, *** p < 0.0001

    Journal: Neurochemical Research

    Article Title: Recurrent Sleep Restriction During Aging Induces Early Recognition Memory Impairment, Neuroinflammation, and Blood–Brain Barrier Dysfunction in Female Wistar Rats

    doi: 10.1007/s11064-026-04909-1

    Figure Lengend Snippet: Recurrent sleep restriction decreases levels of the ZO-1 protein in the cerebral cortex during aging. A Representative blots of each protein in the cortex using β-actin as a load control. B Normalized levels expressed as relative fold change of the ZO-1 and C occludin proteins. D Representative blots of each protein in the hippocampus using β-actin as a load control. E Normalized levels expressed as relative fold change of the ZO-1 and F occludin proteins. Data are presented as mean ± SEM. Two-way ANOVA, followed by Tukey’s test for multiple comparisons ( n = 4 per group, in duplicate). * p < 0.05, ** p < 0.001, *** p < 0.0001

    Article Snippet: Membranes were then incubated overnight at 4 °C with the following primary antibodies: ZO-1 (Invitrogen, Cat. No. 40–2200, 1:500), occludin (Invitrogen, Cat. No. 40–4700, 1:500), and β-actin (Santa Cruz Biotechnology, Cat. No. sc-69879, 1:2500).

    Techniques: Control