anti ppar γ  (Proteintech)

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: RNA-seq identifies ABCC5 as a potential key downstream effector of PPARγ in HS. (A) Volcano plot illustrating differentially expressed genes between the WT + HS and PPARγ-OE + HS groups. (B) GO enrichment analysis of differentially expressed genes between the WT + HS and PPARγ-OE + HS groups. (C) KEGG pathway enrichment analysis of DEGs between the WT + HS and PPARγ-OE + HS groups. (D) Heatmap displaying expression changes of ABC transporter family members across the indicated groups. (E) Measurement of cellular free fatty acids and triglycerides in cells under the indicated treatments. (F) RT-qPCR analysis of PPARγ mRNA expression in PPARγ NC + HS and PPARγ OE + HS cells. (G) RT-qPCR analysis of selected ABC transporter genes (ABCC5, ABCB1A, ABCC6, TAP2, ABCA6, ABCB4, ABCC10, ABCA2, ABCG4, ABCA1, ABCA8A, ABCA9, ABCB2, ABCB7, and ABCA3) under the specified conditions. Error bars represent mean ± SD (n = 3). ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001 versus the PPARγ-NC + HS group (E–G). Statistical comparisons were performed using Student's t-test (F–G) or one-way ANOVA (E).

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: RNA Sequencing, Expressing, Quantitative RT-PCR

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: Time-dependent changes in ABCC5 expression in vivo. (A) Representative immunofluorescence images of ABCC5 (green) and DAPI (blue) in cardiac tissues from sham mice and from mice subjected to HS at the indicated time points after injury. (B) Representative immunohistochemical staining of ABCC5 in cardiac tissues from sham and HS-injured mice. (C) RT-qPCR analysis of Leptin mRNA in cardiac tissues after 2.5 h or 3 weeks of heat injury. (D) Representative immunofluorescence images of ABCC5 in cardiac sections from PPARγ-cKO mice after HS). (E–F) Representative immunofluorescence images of PPARγ and ABCC5 in cardiac sections from PPARγ-cKO mice at 3 weeks after HS). Error bars represent mean ± SD (n = 3). ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001 versus the sham group (B–C). Statistical comparisons were performed using Student's t-test (B) or one-way ANOVA (C).

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: Expressing, In Vivo, Immunofluorescence, Immunohistochemical staining, Staining, Quantitative RT-PCR

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: ABCC5 siRNA abolishes the cardioprotective effects of PPARγ overexpression against HS ​. (A) Luciferase activity in cells co-transfected with ABCC5 wild-type or mutant (Mut1/2/3) reporter plasmids and adenovirus expressing PPARγ. (B) CUT&Tag assay using a PPARγ-specific antibody to detect PPARγ binding to the ABCC5 promoter. (C) RT-qPCR analysis of ABCC5 mRNA in cells transfected with control siRNA or ABCC5 siRNA. (D – F) Cell morphology and viability in cells transfected with ABCC5 siRNA and/or PPARγ overexpression vector under HS conditions. (G – H) Apoptosis levels measured by flow cytometry in cells transfected with ABCC5 siRNA and PPARγ-OE under HS conditions. (I – J) DCFH-DA staining for ROS detection in cells transfected with ABCC5 siRNA and PPARγ-OE under HS conditions. (K – L) Mitochondrial membrane potential assessed by JC-1 fluorescence in the indicated groups. (M) Western blot analysis of PPARγ, ABCC5, ABCC1, Leptin, and β-actin (loading control) in cells treated as follows: PPARγ-NC + HS, PPARγ-OE + HS, and PPARγ-OE + ABCC5 siRNA + HS. Molecular weight markers are shown on the right. (N) Quantification of protein levels normalized to β-actin, corresponding to the blots in (M). Data are presented as mean ± SD (n = 3). ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001 versus the indicated control, PPARγ + ABCC5 group (A–B), control siRNA group (C), PPARγ-NC + HS group, PPARγ-OE + HS group, or PPARγ-OE + ABCC5 siRNA + HS group (D–L), or versus the PPARγ-NC + HS group and PPARγ-OE + HS group (M − N). Statistical comparisons were performed using one-way ANOVA.

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: Over Expression, Luciferase, Activity Assay, Transfection, Mutagenesis, Expressing, Binding Assay, Quantitative RT-PCR, Control, Plasmid Preparation, Flow Cytometry, Staining, Membrane, Fluorescence, Western Blot, Molecular Weight

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: The PPARγ/ABCC5 pathway alleviates lipid accumulation in HS-injured mice ​. (A – D) Cardiac sections from sham mice and from mice at indicated time points after HS were stained with HE (A) , PSR (B) , Masson's trichrome (C) , or Oil Red O (D) (n = 3 per group). (E) Serum levels of HDL-C and LDL-C in sham mice and in mice 3 weeks after HS (n = 6–7 per group). Error bars represent mean ± SD. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001 versus the sham group. Statistical comparisons were performed using Student's t-test.

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: Staining

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: Rosiglitazone pretreatment alleviates HS-induced myocardial injury via the PPARγ/ABCC5 pathway in HL-1 cells ​. (A – C) Cell viability and morphology in cells treated with different concentrations of rosiglitazone (5 μM, 10 μM, 20 μM, 40 μM) under HS conditions. (D – E) Apoptosis levels in cells treated with different concentrations of rosiglitazone under HS conditions. (F–I) DHE staining (F) and DCFH-DA staining (I) for ROS detection in cells treated with different concentrations of rosiglitazone under HS conditions. (J – K) Mitochondrial membrane potential assessed by JC-1 fluorescence in the indicated groups. (L) RT-qPCR analysis of PPARγ, ABCC5, Leptin, and SREBP-1c in cells treated with different concentrations of rosiglitazone under HS conditions. (M – N) Representative Western blots and quantification of PPARγ, ABCC5, ABCC1, ABCG1, ABCA1, and Leptin in cells treated with different concentrations of rosiglitazone under HS conditions. Error bars represent mean ± SD (n = 3). ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001 versus the control group or the HS group. Statistical comparisons were performed using one-way ANOVA.

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: Staining, Membrane, Fluorescence, Quantitative RT-PCR, Western Blot, Control

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: The PPARγ agonist rosiglitazone confers pharmacological protection against HS-induced myocardial dysfunction ​. (A – C) Cell viability and morphology in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. (D – E) Apoptosis levels measured by flow cytometry in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. (F) LDH release in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. (G – H) DCFH-DA staining for ROS detection in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. (I – J) Mitochondrial membrane potential assessed by JC-1 fluorescence in the indicated groups. (K) RT-qPCR analysis of PPARγ and CPT1β mRNA in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. (L) Representative Western blots and quantification of PPARγ, ABCC5, PGC-1α, and PPARγ in cells transfected with PPARγ siRNA and pretreated with rosiglitazone under HS conditions. Error bars represent mean ± SD (n = 3). ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001 versus the control group, the HS group, or the ROSI + HS group as indicated. Statistical comparisons were performed using one-way ANOVA.

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques: Transfection, Flow Cytometry, Staining, Membrane, Fluorescence, Quantitative RT-PCR, Western Blot, Control

Journal: Redox Biology

Article Title: PPARγ contributes to cardioprotection against heat stroke through ABCC5-dependent lipid metabolism

doi: 10.1016/j.redox.2026.104113

Figure Lengend Snippet: The proposed scheme describing the signaling pathway of PPARγ/ABCC5-elicted cardioprotective effect against HS.

Article Snippet: For immunofluorescence, tissues and cells were fixed in 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and blocked with 5% normal goat serum in PBS for 1 h. Sections and cells were then incubated overnight at 4 °C with primary antibodies against PPARγ (Proteintech, 66936-1-1g) and ABCC5 (Bioss, bs-1437R), followed by incubation with appropriate secondary antibodies for 1 h. Images were acquired using a fluorescence microscope (Invitrogen EVOS M5000, Thermo Fisher Scientific, Waltham, MA, USA), and fluorescence intensity was quantified with ImageJ Pro Plus software.

Techniques:

Journal: Cancer Immunology, Immunotherapy : CII

Article Title: Promoting APC function of B cells via reprogramming the fatty acid metabolism enhances anticancer immunity in metastatic ovarian cancer

doi: 10.1007/s00262-026-04387-y

Figure Lengend Snippet: The enhanced APC function of B cells by OA in vitro is achieved through H3K27ac-mediated upregulation of PPAR γ expression. A Protein expression of β -actin and H3K27ac in 3 w OvCa-bearing mouse ascitic CD19 + B cells pretreated with BMS and treated with OA was assessed by WB. β -Actin was used as the internal control to calculate the relative expression level of H3K27ac. B The enrichment percentage of H3K27ac at the PPAR γ , CD80, CD86, and CD83 promoter regions was quantified using ChIP-seq analysis. C Correlation analysis of PPAR γ and APC function-related genes (CD80, CD86, CD83, MHC II) in B cells in OvCa patients in the TCGA database (n = 426). D Analysis of protein interaction among FABP4, PPAR γ , CD80, CD86, and CD83. E The enrichment percentage of PPAR γ at the CD80, CD86, and CD83 promoter regions was quantified using ChIP-seq analysis. F Mean fluorescence intensity of CD80, CD86, and CD83 in 3 w OvCa-bearing mouse ascitic CD19 + B cells pretreated with BMS, GW9662/Trog, and treated with OA was detected by flow cytometry. AS, Ascites; Ag, Antigen; OA, oleic acid; BMS, BMS309403. Data are presented as the mean ± SD of three independent experiments. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, ns, not significant

Article Snippet: In the mechanistic study, mouse ascitic CD19 + B cells (1 × 10 6 /ml) were pretreated with fatty acid binding protein 4 gene (FABP4) inhibitor (BMS309403, MedChemExpress; Cat# HY-101903; 50 μM), PPARγ antagonist (GW9662, MedChemExpress; Cat# HY-16578; 25 μM), and PPAR γ agonist (Troglitazone, Trog, MedChemExpress; Cat# HY-50935; 10 μM) for 2h, respectively.

Techniques: In Vitro, Expressing, Control, ChIP-sequencing, Fluorescence, Flow Cytometry

Journal: Cancer Immunology, Immunotherapy : CII

Article Title: Promoting APC function of B cells via reprogramming the fatty acid metabolism enhances anticancer immunity in metastatic ovarian cancer

doi: 10.1007/s00262-026-04387-y

Figure Lengend Snippet: The mechanism diagram of combining adoptive immunotherapy with APC-function-enhanced B cells and LDC improves anticancer immunity in metastatic OvCa mice. In vitro, OA enhances the expression of CD80/CD86/CD83 of B cells through the H3K27ac-mediated upregulation of PPAR γ expression. Then, the B cells are adoptively transferred into the abdominal cavity of metastatic OvCa mice. In the abdominal cavity, LDC facilitates the APC function of the transferred B cells by causing apoptosis of cancer cells. The transferred B cells promote the activation, proliferation, and differentiation of T cells, which release higher levels of effector molecules (IL-2, GZMB, and IFN- γ , etc.), and facilitate the formation of lymphoid aggregates, finally improving anticancer immunity. LDC, low-dose chemotherapy

Article Snippet: In the mechanistic study, mouse ascitic CD19 + B cells (1 × 10 6 /ml) were pretreated with fatty acid binding protein 4 gene (FABP4) inhibitor (BMS309403, MedChemExpress; Cat# HY-101903; 50 μM), PPARγ antagonist (GW9662, MedChemExpress; Cat# HY-16578; 25 μM), and PPAR γ agonist (Troglitazone, Trog, MedChemExpress; Cat# HY-50935; 10 μM) for 2h, respectively.

Techniques: In Vitro, Expressing, Activation Assay

Journal: Journal of Advanced Research

Article Title: Hyodeoxycholic acid relieves neuropathic pain by activating farnesoid X receptor signaling

doi: 10.1016/j.jare.2025.07.017

Figure Lengend Snippet: HDCA upregulates the intestinal PPAR-γ and downregulates the MMP-9/2 expression. (A) The degree of the node between the HDCA and the intersection target. (B) Molecular docking analysis between HDCA and PPAR-γ. (C) Molecular docking analysis between HDCA and MMP-9. (D) Molecular docking analysis between HDCA and MMP-2. (E-G) Relative expression of mRNA of ppar-γ, mmp9 and mmp2 in the distal ileum. (n = 6) . (H) Representative protein immunoblots in distal ileum. (I-K) Relative expression of PPAR-γ, MMP-9, MMP-2 (n = 3–4). (L) Representative immunohistochemical staining and quantitative analysis of MMP-2+ (M), PPAR-γ+ (N) and MMP-9+ (O) cells in the distal ileum (scale bar, 100 μm, n = 6). * P < 0.05, ** P < 0.01, *** P < 0.001 by One-way ANOVA with post hoc Tukey's test (E–G, I–K, M–O). Data is presented as mean ± SEM.

Article Snippet: Tissue sections of each group were blocked with 1 % bovine serum albumin and 10 % donkey serum at room temperature for 1 h and then incubated at 4 °C overnight with primary antibodies for neuronal nuclear protein (NeuN) (1:500, Abcam, ab104224), ionized calcium-binding adapter molecule 1 (IBA-1) (1:500, Abcam, ab5076), glial fibrillary acidic protein (GFAP) (1:500, Millipore, MAB360), FXR (1:200, Proteintech, 25055–1-AP), MMP-2 (1:200, Proteintech, 10373-2-AP), MMP-9 (1:200, Proteintech, 10375-2-AP), PPAR-γ (1:200, Proteintech, 16643–1-AP), NLRP3 (1:200, Immunoway, YT5382), and cluster of differentiation 86 (CD86) (1:200, CST, #91882).

Techniques: Expressing, Western Blot, Immunohistochemical staining, Staining

Journal: Journal of Advanced Research

Article Title: Hyodeoxycholic acid relieves neuropathic pain by activating farnesoid X receptor signaling

doi: 10.1016/j.jare.2025.07.017

Figure Lengend Snippet: HDCA upregulates PPAR-γ expression and reduces MMP-9/2 expression in the spinal cord. (A–C) The relative expression of mRNA in spinal cord of ppar-γ, mmp9 and mmp2 . (n = 6) . (D–G) Representative immunoblots of proteins and relative expression of PPAR-γ, MMP-2, MMP-9 (n = 4). (H–J) Immunofluorescence staining of PPAR-γ, MMP-9, MMP-2 in spinal cord (scale, 100 μm). (n = 3). (K) Heatmap of Correlation Analysis. * P < 0.05, ** P < 0.01, *** P < 0.001 by One-way ANOVA with post hoc Tukey's test (A–D, F, G). Data is presented as mean ± SEM.

Article Snippet: Tissue sections of each group were blocked with 1 % bovine serum albumin and 10 % donkey serum at room temperature for 1 h and then incubated at 4 °C overnight with primary antibodies for neuronal nuclear protein (NeuN) (1:500, Abcam, ab104224), ionized calcium-binding adapter molecule 1 (IBA-1) (1:500, Abcam, ab5076), glial fibrillary acidic protein (GFAP) (1:500, Millipore, MAB360), FXR (1:200, Proteintech, 25055–1-AP), MMP-2 (1:200, Proteintech, 10373-2-AP), MMP-9 (1:200, Proteintech, 10375-2-AP), PPAR-γ (1:200, Proteintech, 16643–1-AP), NLRP3 (1:200, Immunoway, YT5382), and cluster of differentiation 86 (CD86) (1:200, CST, #91882).

Techniques: Expressing, Western Blot, Immunofluorescence, Staining

Journal: Journal of Advanced Research

Article Title: Hyodeoxycholic acid relieves neuropathic pain by activating farnesoid X receptor signaling

doi: 10.1016/j.jare.2025.07.017

Figure Lengend Snippet: Fxr knock down abolished the protective effect of HDCA in neuropathic pain. (A) Immunofluorescence staining showing FXR co-localization in spinal cord. (scale, 25 μm). (B) Immunofluorescence staining demonstrating MMP-2 colocalization in spinal cord. (scale, 25 μm). (C) Immunofluorescence staining showing PPAR-γ colocalization in spinal cord. (scale, 25 μm). (D) Immunofluorescence staining showing MMP-9 colocalization in spinal cord. (scale, 25 μm). (E) Immunofluorescence staining of FXR and MMP-2 colocalization in spinal cord. (scale, 25 μm). (F) Representative immunoblots of protein expression in the spinal cord from Fxr -/- mice. (G) Relative expression of PPAR-γ, MMP-2 and MMP-9 (n = 4). (H) Representative immunoblots for the proteins in spinal cord following INT-747 treatment. (I) PWT of Fxr -/- mice following HDCA or INT-747 treatment. (n = 6). (J) PWL of Fxr -/- mice following HDCA or INT-747 treatment. (n = 6). (K) Relative expression of PPAR-γ, MMP-2 and MMP-9 following INT-747 treatment. (n = 4). (L, M) Representative immunoblots for the proteins in spinal cord and relative expression of PPAR-γ, MMP-2 and MMP-9 in Fxr -/- mice following HDCA treatment. (n = 4). * P < 0.05, ** P < 0.01, ns by unpaired Student's t‐test (G, M). ns by Two-way repeated ANOVA with post hoc Bonferroni’s test (I and J), * P < 0.05, ** P < 0.01, *** P < 0.001 by One-way ANOVA with post hoc Tukey's test (K). Data are represented as mean ± SEM.

Article Snippet: Tissue sections of each group were blocked with 1 % bovine serum albumin and 10 % donkey serum at room temperature for 1 h and then incubated at 4 °C overnight with primary antibodies for neuronal nuclear protein (NeuN) (1:500, Abcam, ab104224), ionized calcium-binding adapter molecule 1 (IBA-1) (1:500, Abcam, ab5076), glial fibrillary acidic protein (GFAP) (1:500, Millipore, MAB360), FXR (1:200, Proteintech, 25055–1-AP), MMP-2 (1:200, Proteintech, 10373-2-AP), MMP-9 (1:200, Proteintech, 10375-2-AP), PPAR-γ (1:200, Proteintech, 16643–1-AP), NLRP3 (1:200, Immunoway, YT5382), and cluster of differentiation 86 (CD86) (1:200, CST, #91882).

Techniques: Knockdown, Immunofluorescence, Staining, Western Blot, Expressing