pparα  (Proteintech)

Journal: Journal of Inflammation Research

Article Title: HMGCS2 Palmitoylation Promotes Diabetes-Induced Erectile Dysfunction Through PPARα-Mediated Macrophage Extracellular Trap Formation

doi: 10.2147/JIR.S623377

Figure Lengend Snippet: HG and PA treatments induce high expression of HMGCS2 and MET formation in macrophages. ( A and B ) Volcano and heatmap diagrams depicting the DEGs in corpus cavernosum between DMED rats and controls. ( C ) Heatmap visualizing the top 20 up- and downregulated DEGs in DMED, respectively. ( D and E ) Biological processes and KEGG pathways enriched by the DEGs. ( F ) Visualization of PPAR signaling pathway enriched by the DEGs. ( G ) qRT-PCR for detecting the mRNA expression of HMGCS2 in control RAW264.7 macrophages and those with treatments of 25 mmol/L HG and 60 μM PA for 48 h. ( H ) Representative Western blot of HMGCS2, PAD4, ME, and MPO in control and HG- and PA-induced RAW264.7 macrophages. ( I-L ) Quantification of the expression levels of HMGCS2, PAD4, ME, and MPO in control and HG- and PA-induced RAW264.7 macrophages. ***, P<0.001; ****, P<0.0001 derived from Student’s t test.

Article Snippet: Primary antibodies included: HMGCS2 (ab305,227; Abcam, USA), peptidyl arginine deiminase 4 (PAD4; 17,373-1-AP; Proteintech, China), macrophage elastase (ME; 22,989-1-AP; Proteintech), MPO (22,225-1-AP; Proteintech), GAPDH (T0004; Affinity, USA), β-Tubulin (66,240-1-Ig; Proteintech), and PPARα (66,826-1-Ig; Proteintech).

Techniques: Expressing, Quantitative RT-PCR, Control, Western Blot, Derivative Assay

Journal: Journal of Inflammation Research

Article Title: HMGCS2 Palmitoylation Promotes Diabetes-Induced Erectile Dysfunction Through PPARα-Mediated Macrophage Extracellular Trap Formation

doi: 10.2147/JIR.S623377

Figure Lengend Snippet: Pharmacological suppression of protein palmitoylation downregulates HMGCS2 palmitoylation and expression and hinders MET formation in HG- and PA-induced macrophages. ( A ) ABE assay for measuring HMGCS2 palmitoylation in control macrophages, HG- and PA-induced macrophages, and HG- and PA-induced macrophages with CMA treatment, in the presence or absence of HAM. ( B ) Co-IP assay for detecting the interaction of HMGCS2 with PPARα in control macrophages, HG- and PA-induced macrophages, and HG- and PA-induced macrophages with CMA treatment. ( C ) qRT-PCR for measuring the mRNA level of HMGCS2 in control macrophages, HG- and PA-induced macrophages, and HG- and PA-induced macrophages with CMA treatment. ( D ) Representative Western blot of HMGCS2, PAD4, ME, and MPO in control macrophages, HG- and PA-induced macrophages, and HG- and PA-induced macrophages with CMA treatment. ( E–H ) Quantification of the protein expression levels of HMGCS2, PAD4, ME, and MPO in the above macrophages. **, P<0.01; ***, P<0.001; ****, P<0.0001 derived from one-way ANOVA followed by Tukey’s post hoc test.

Article Snippet: Primary antibodies included: HMGCS2 (ab305,227; Abcam, USA), peptidyl arginine deiminase 4 (PAD4; 17,373-1-AP; Proteintech, China), macrophage elastase (ME; 22,989-1-AP; Proteintech), MPO (22,225-1-AP; Proteintech), GAPDH (T0004; Affinity, USA), β-Tubulin (66,240-1-Ig; Proteintech), and PPARα (66,826-1-Ig; Proteintech).

Techniques: Expressing, Control, Co-Immunoprecipitation Assay, Quantitative RT-PCR, Western Blot, Derivative Assay

Journal: Journal of Inflammation Research

Article Title: HMGCS2 Palmitoylation Promotes Diabetes-Induced Erectile Dysfunction Through PPARα-Mediated Macrophage Extracellular Trap Formation

doi: 10.2147/JIR.S623377

Figure Lengend Snippet: Palmitoylation inhibitor CMA reduces HMGCS2 palmitoylation and expression and hinders MET formation in corpus cavernosum of DMED model rats. ( A ) Detection of PA level in peripheral blood from control rats, DMED model rats, and DMED model rats with CMA administration. ( B ) ABE assay for measuring HMGCS2 palmitoylation in corpus cavernosum from control rats, DMED model rats, and DMED model rats with CMA administration, in the presence or absence of HAM. ( C ) Co-IP assay for detecting the interaction of HMGCS2 with PPARα in corpus cavernosum from control rats, DMED model rats, and DMED model rats with CMA administration. ( D ) qRT-PCR for measuring the mRNA level of HMGCS2 in corpus cavernosum from control rats, DMED model rats, and DMED model rats with CMA administration. ( E ) Representative Western blot of HMGCS2, PAD4, ME, and MPO in corpus cavernosum from control rats, DMED model rats, and DMED model rats with CMA administration. ( F–I ) Quantification of the protein expression levels of HMGCS2, PAD4, ME, and MPO in corpus cavernosum from control rats, DMED model rats, and DMED model rats with CMA administration. *, P<0.05; **, P<0.01; ***, P<0.001; ****, P<0.0001 derived from one-way ANOVA followed by Tukey’s post hoc test.

Article Snippet: Primary antibodies included: HMGCS2 (ab305,227; Abcam, USA), peptidyl arginine deiminase 4 (PAD4; 17,373-1-AP; Proteintech, China), macrophage elastase (ME; 22,989-1-AP; Proteintech), MPO (22,225-1-AP; Proteintech), GAPDH (T0004; Affinity, USA), β-Tubulin (66,240-1-Ig; Proteintech), and PPARα (66,826-1-Ig; Proteintech).

Techniques: Expressing, Control, Co-Immunoprecipitation Assay, Quantitative RT-PCR, Western Blot, Derivative Assay

Journal: Frontiers in Genetics

Article Title: HOTAIR regulates osteogenic–adipogenic differentiation imbalance through the miR-217/DKK1-mediated Wnt/β-catenin pathway in SONFH-BMSCs

doi: 10.3389/fgene.2026.1917162

Figure Lengend Snippet: Primers for qRT-PCR analyses.

Article Snippet: The membranes were blocked with 5% non-fat milk in Tris-buffered saline with 0.1% Tween-20 (TBST) for 1 h at room temperature and then incubated overnight at 4 °C with primary antibodies targeting Osterix (Boster, Cat. No. M02077, 1:1,000), BMP2 (Boster, Cat. No. BM4960, 1:1,000), RUNX2 (Boster, Cat. No. BM4700, 1:1,000), PPARγ (Boster, Cat. No. M00449-2, 1:1,000), C/EBPα (Boster, Cat. No. A00386-1, 1:1,000), Adipsin (Boster, Cat. No. M01134, 1:1,000), DKK1 (Boster, Cat. No. A09360-1, 1:1,000), OCT4 (Abmart, Cat. No. T55781 , 1:10,000), β-catenin (Abmart, Cat. No. M24002 , 1:10,000), and β-actin (Boster, Cat. No. BM3873, 1:10,000).

Techniques: Sequencing

Journal: Frontiers in Genetics

Article Title: HOTAIR regulates osteogenic–adipogenic differentiation imbalance through the miR-217/DKK1-mediated Wnt/β-catenin pathway in SONFH-BMSCs

doi: 10.3389/fgene.2026.1917162

Figure Lengend Snippet: HOTAIR silencing inhibits adipogenic differentiation of SONFH-BMSCs in vitro . (A) Oil Red O staining of FNF-derived control BMSCs (NC), untreated SONFH-BMSCs, SONFH si-NC, and SONFH si-HOTAIR groups at days 7 and 14. (B) Quantitative analysis of Oil Red O staining at days 7 and 14. (C) qRT-PCR analysis of PPARγ, C/EBPα, and Adipsin mRNA levels. Expression was normalized to GAPDH and is shown compared with untreated SONFH-BMSCs and si-NC controls. (D) Western blot analysis of PPARγ, C/EBPα, and Adipsin. Data are presented as mean ± SD from three independent biological replicates using BMSCs from independent donors, with three technical replicates per experiment. (*P < 0.05; **P < 0.01; ***P < 0.001).

Article Snippet: The membranes were blocked with 5% non-fat milk in Tris-buffered saline with 0.1% Tween-20 (TBST) for 1 h at room temperature and then incubated overnight at 4 °C with primary antibodies targeting Osterix (Boster, Cat. No. M02077, 1:1,000), BMP2 (Boster, Cat. No. BM4960, 1:1,000), RUNX2 (Boster, Cat. No. BM4700, 1:1,000), PPARγ (Boster, Cat. No. M00449-2, 1:1,000), C/EBPα (Boster, Cat. No. A00386-1, 1:1,000), Adipsin (Boster, Cat. No. M01134, 1:1,000), DKK1 (Boster, Cat. No. A09360-1, 1:1,000), OCT4 (Abmart, Cat. No. T55781 , 1:10,000), β-catenin (Abmart, Cat. No. M24002 , 1:10,000), and β-actin (Boster, Cat. No. BM3873, 1:10,000).

Techniques: In Vitro, Staining, Derivative Assay, Control, Analysis, Quantitative RT-PCR, Expressing, Western Blot

Journal: International Journal of Molecular Sciences

Article Title: MicroRNA-34a Promotes Hepatic Lipid Accumulation Through RXRα Suppression and Is Reversed by 9- cis -Retinoic Acid in Steatotic Hepatocytes

doi: 10.3390/ijms27156609

Figure Lengend Snippet: Proposed model of the miR-34a–RXRα regulatory axis in MASLD and its modulation by 9- cis -retinoic acid: schematic illustration summarizing the proposed findings of this study. Under steatotic conditions, FFA-induced upregulation of miR-34a is proposed to suppress RXRα expression, thereby promoting enhanced de novo lipogene-sis (FASN and SCD1), increased fatty acid uptake (CD36 and FABP4), and reduced PPARα-mediated fatty acid β-oxidation. These coordinated molecular alterations are accompanied by increased intracellular lipid accumula-tion and contribute to the development of MASLD. Conversely, activation of RXR-associated signaling by 9- cis -retinoic acid is proposed to attenuate these alterations by suppressing lipogenesis and fatty acid uptake while promoting fatty acid oxidation, thereby reducing hepatic lipid accumulation. Because 9- cis -retinoic acid is a pan-RXR agonist capable of activating multiple RXR-dependent signaling pathways, the proposed mechanism should be regarded as a working model that requires receptor-specific mechanistic validation. In the schematic, arrows indicate positive regulation or the direction of change, whereas T-shaped lines indicate negative regu-lation or inhibition.

Article Snippet: The membranes were blocked with 5% non-fat milk in Tris-buffered saline containing 0.1% Tween-20 (TBST) for 1 h at room temperature and then incubated overnight at 4 °C with primary antibodies against RXRα (Cat. No. A15242, ABclonal, Wuhan, China), SIRT1 (Cat. No. A11267, ABclonal), α-tubulin (Cat. No. AC012, ABclonal), CD36 (Cat. No. A1470, ABclonal), FABP4 (Cat. No. A0232, ABclonal), SCD1 (Cat. No. A26246, ABclonal), PPARα (Cat. No. A18252, ABclonal), FASN (Cat. No. A21182 , ABclonal), and GAPDH (Cat. No. AC033, ABclonal).

Techniques: Expressing, Activation Assay, Protein-Protein interactions, Biomarker Discovery, Inhibition

Journal: BMC Medicine

Article Title: Therapeutic activation of PPARα contributes to NOTCH1 inhibition in T-cell acute lymphoblastic leukemia

doi: 10.1186/s12916-026-05045-x

Figure Lengend Snippet: Chiglitazar activates PPARα and exerts cytotoxic effects on T-ALL cell lines in vitro. ( A ) Western blot analysis showing that chiglitazar treatment dose-dependently enhances PPARα protein expression in Jurkat and Molt4 cells, without significantly affecting PPARγ levels. ( B - C ) CCK-8 assay ( B ) and trypan blue staining ( C ) showing the viability and proliferation of Jurkat and Molt4 cells treated with increasing concentrations of chiglitazar at 24, 48, and 72 h, indicating dose- and time-dependent inhibition. ( D ) EdU incorporation assays confirming significantly reduced cell proliferation in Jurkat and Molt4 cells following 24 h of chiglitazar treatment. ( E ) Flow cytometry analysis of the cell cycle revealing that chiglitazar treatment for 24 h induces G0/G1 phase arrest in T-ALL cells. ( F ) Colony formation assays showing a significant reduction in the colony-forming ability of Jurkat and Molt4 cells treated with indicated concentrations of chiglitazar and cultured for 14 days. (G-H) Flow cytometry analysis using Annexin V/PI staining demonstrates that chiglitazar treatment for 24 h induces apoptosis in Jurkat and Molt4 cells in a dose-dependent manner. Data are presented as mean ± SD (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001)

Article Snippet: The following primary antibodies were used: PPARα (Abcam); PPARγ (ABclonal); GAPDH (HUABIO); NOTCH1 (Abcam); NICD (Cell Signaling Technology); RPBJK (Abcam); Hes1 (Cell Signaling Technology); Hey1 (ABclonal); Bcl-2 (Cell Signaling Technology); Bcl-XL (Cell Signaling Technology); C-Myc (Cell Signaling Technology); STAT3 (Cell Signaling Technology); p-STAT3 (Cell Signaling Technology); Lamin B1 (Cell Signaling Technology); β-Tubulin (Proteintech).

Techniques: In Vitro, Western Blot, Analysis, Expressing, CCK-8 Assay, Staining, Inhibition, EdU Assay, Flow Cytometry, Colony Assay, Cell Culture