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Bioss il 1β

Assessment of the anti-inflammatory capacity of CPS gel in vitro . A Schematic of the co-culture of hydrogel with RAW 264.7. B Quantification of the relative fluorescence intensity of TNF-α. C Quantification of the relative fluorescence intensity of <t>IL-1β.</t> D Immunofluorescence image of TNF-α expression in RAW 264.7 (Scale bar = 50 μm). E Immunofluorescence image of IL-1β expression in RAW 264.7 (Scale bar = 50 μm). F-H The protein expression level of TNF-α and IL-1β was evaluated by WB and quantified by ImageJ. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Il 1β, supplied by Bioss, used in various techniques. Bioz Stars score: 96/100, based on 225 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 225 article reviews

il 1β - by Bioz Stars, 2026-03

96/100 stars

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1) Product Images from "Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment"

Article Title: Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment

Journal: Materials Today Bio

doi: 10.1016/j.mtbio.2026.102825

Figure Legend Snippet: Assessment of the anti-inflammatory capacity of CPS gel in vitro . A Schematic of the co-culture of hydrogel with RAW 264.7. B Quantification of the relative fluorescence intensity of TNF-α. C Quantification of the relative fluorescence intensity of IL-1β. D Immunofluorescence image of TNF-α expression in RAW 264.7 (Scale bar = 50 μm). E Immunofluorescence image of IL-1β expression in RAW 264.7 (Scale bar = 50 μm). F-H The protein expression level of TNF-α and IL-1β was evaluated by WB and quantified by ImageJ. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Techniques Used: In Vitro, Co-Culture Assay, Fluorescence, Immunofluorescence, Expressing

In vivo study of CPS gel for AF repair. A H&E, S&O staining sections of rat IVD at 4W and 8W post-operation (scale bar = 1 mm). B Col-1, IL-1β IHC staining sections of rat IVD at 4W and 8W post-operation (Scale bar = 50 μm). C Postoperative 4W Col-1 quantitative analysis. D Postoperative 8W Col-1 quantitative analysis. E. Postoperative 4W IL-1β quantitative analysis. F Postoperative 8W IL-1β quantitative analysis. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Figure Legend Snippet: In vivo study of CPS gel for AF repair. A H&E, S&O staining sections of rat IVD at 4W and 8W post-operation (scale bar = 1 mm). B Col-1, IL-1β IHC staining sections of rat IVD at 4W and 8W post-operation (Scale bar = 50 μm). C Postoperative 4W Col-1 quantitative analysis. D Postoperative 8W Col-1 quantitative analysis. E. Postoperative 4W IL-1β quantitative analysis. F Postoperative 8W IL-1β quantitative analysis. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Techniques Used: In Vivo, Staining, Immunohistochemistry

Image Search Results

Journal: Materials Today Bio

Article Title: Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment

doi: 10.1016/j.mtbio.2026.102825

Figure Lengend Snippet: Assessment of the anti-inflammatory capacity of CPS gel in vitro . A Schematic of the co-culture of hydrogel with RAW 264.7. B Quantification of the relative fluorescence intensity of TNF-α. C Quantification of the relative fluorescence intensity of IL-1β. D Immunofluorescence image of TNF-α expression in RAW 264.7 (Scale bar = 50 μm). E Immunofluorescence image of IL-1β expression in RAW 264.7 (Scale bar = 50 μm). F-H The protein expression level of TNF-α and IL-1β was evaluated by WB and quantified by ImageJ. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Staining was performed using IL-1β (Bioss, BS-0812R) and TNF-α (Santa, SC-52746) probes, and the staining was observed under a fluorescent inverted microscope.

Techniques: In Vitro, Co-Culture Assay, Fluorescence, Immunofluorescence, Expressing

Journal: Materials Today Bio

Article Title: Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment

doi: 10.1016/j.mtbio.2026.102825

Figure Lengend Snippet: In vivo study of CPS gel for AF repair. A H&E, S&O staining sections of rat IVD at 4W and 8W post-operation (scale bar = 1 mm). B Col-1, IL-1β IHC staining sections of rat IVD at 4W and 8W post-operation (Scale bar = 50 μm). C Postoperative 4W Col-1 quantitative analysis. D Postoperative 8W Col-1 quantitative analysis. E. Postoperative 4W IL-1β quantitative analysis. F Postoperative 8W IL-1β quantitative analysis. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Staining was performed using IL-1β (Bioss, BS-0812R) and TNF-α (Santa, SC-52746) probes, and the staining was observed under a fluorescent inverted microscope.

Techniques: In Vivo, Staining, Immunohistochemistry

Significant Ups genes in the acetabular cartilage of the rats with DDH, as determined by mRNA-seq analysis. (A) Neonatal rats were subjected to straight-leg swaddling for 10 days. A total of 4 weeks later, (a) morphology, (b) H&E staining and (c) SO/FG staining were assessed in the hip joints of the rats. (B) Immunohistochemical staining and (E) semi-quantitative analysis of COL2A1 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (C) Relative gene expression levels of COL2A1, IL-1β and IL-6 in the acetabular cartilage of the 4-week-old control rats and rats with DDH, as determined by reverse transcription-quantitative PCR. (D) Levels of IL-6 in the supernatants of acetabular cartilage from the 4-week-old rats with DDH, as determined by ELISA. (F) Significant Ups in the acetabular cartilage of rats with DDH were identified by mRNA-seq analysis with the screening criteria of log 2 FC >4 and P.adj<0.01. Principal component analysis results and a heatmap of these significant Ups are shown. (G) GO enrichment analysis of significant Ups in the acetabular cartilage of the rats with DDH. Data are presented as the mean ± SD. *** P<0.001. (C-E) Representative results of four independent experiments are shown. Ups, upregulated genes; BP, biological process; CC, cellular component; COL2A1, type II collagen; DDH, developmental dysplasia of the hip; FC, fold change; GO, Gene Ontology; H&E, hematoxylin and eosin; IHC, immunohistochemistry; IL, interleukin; IOD, integrated optical density; MF, molecular function; mRNA-seq, mRNA sequencing; SO/FG, Safranin O/Fast Green.

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: Significant Ups genes in the acetabular cartilage of the rats with DDH, as determined by mRNA-seq analysis. (A) Neonatal rats were subjected to straight-leg swaddling for 10 days. A total of 4 weeks later, (a) morphology, (b) H&E staining and (c) SO/FG staining were assessed in the hip joints of the rats. (B) Immunohistochemical staining and (E) semi-quantitative analysis of COL2A1 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (C) Relative gene expression levels of COL2A1, IL-1β and IL-6 in the acetabular cartilage of the 4-week-old control rats and rats with DDH, as determined by reverse transcription-quantitative PCR. (D) Levels of IL-6 in the supernatants of acetabular cartilage from the 4-week-old rats with DDH, as determined by ELISA. (F) Significant Ups in the acetabular cartilage of rats with DDH were identified by mRNA-seq analysis with the screening criteria of log 2 FC >4 and P.adj<0.01. Principal component analysis results and a heatmap of these significant Ups are shown. (G) GO enrichment analysis of significant Ups in the acetabular cartilage of the rats with DDH. Data are presented as the mean ± SD. *** P<0.001. (C-E) Representative results of four independent experiments are shown. Ups, upregulated genes; BP, biological process; CC, cellular component; COL2A1, type II collagen; DDH, developmental dysplasia of the hip; FC, fold change; GO, Gene Ontology; H&E, hematoxylin and eosin; IHC, immunohistochemistry; IL, interleukin; IOD, integrated optical density; MF, molecular function; mRNA-seq, mRNA sequencing; SO/FG, Safranin O/Fast Green.

Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

Techniques: Staining, Immunohistochemical staining, Control, Gene Expression, Reverse Transcription, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Immunohistochemistry, Sequencing

DUSP26 expression is upregulated in IL-1β-induced chondrocytes. (A) Schematic diagram showing the experimental protocol in vitro . Primary chondrocytes isolated from 5-day-old rats were subjected to treatment with 10 ng/ml IL-1β. The protein and mRNA expression levels of DUSP26 in chondrocytes were detected by RT-qPCR and western blotting. (B) Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were detected by RT-qPCR and western blotting. (C) Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were assessed by RT-qPCR and western blotting. Data are presented as the mean ± SD. ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. Ad-EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: DUSP26 expression is upregulated in IL-1β-induced chondrocytes. (A) Schematic diagram showing the experimental protocol in vitro . Primary chondrocytes isolated from 5-day-old rats were subjected to treatment with 10 ng/ml IL-1β. The protein and mRNA expression levels of DUSP26 in chondrocytes were detected by RT-qPCR and western blotting. (B) Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were detected by RT-qPCR and western blotting. (C) Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were assessed by RT-qPCR and western blotting. Data are presented as the mean ± SD. ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. Ad-EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

Techniques: Expressing, In Vitro, Isolation, Quantitative RT-PCR, Western Blot, Over Expression, Construct, Plasmid Preparation, Negative Control, Reverse Transcription, Real-time Polymerase Chain Reaction

DUSP26 overexpression alleviates IL-1β-induced chondrocyte injury. Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (A) Expression levels of COL2A1 and COL1A1 in the chondrocytes were detected by RT-qPCR and western blotting. (B) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (C) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were determined by ELISA. Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (D) Expression levels of COL2A1 and COL1A1 in the chondrocytes were evaluated by RT-qPCR and western blotting. (E) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (F) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were detected by ELISA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. COL1A1, type I collagen; COL2A1, type II collagen; EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: DUSP26 overexpression alleviates IL-1β-induced chondrocyte injury. Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (A) Expression levels of COL2A1 and COL1A1 in the chondrocytes were detected by RT-qPCR and western blotting. (B) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (C) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were determined by ELISA. Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (D) Expression levels of COL2A1 and COL1A1 in the chondrocytes were evaluated by RT-qPCR and western blotting. (E) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (F) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were detected by ELISA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. COL1A1, type I collagen; COL2A1, type II collagen; EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

Techniques: Over Expression, Construct, Expressing, Quantitative RT-PCR, Western Blot, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Negative Control, Reverse Transcription, Real-time Polymerase Chain Reaction

HDAC1, HDAC2 and HDAC8 are DUSP26-interacting proteins in chondrocytes. (A) IP/MS analysis in DUSP26-overexpressing chondrocytes under IL-1β stimulation. (B) Flow chart of target protein screening. (C) Immunohistochemical staining of HDAC1, HDAC2 and HDAC8 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (D) Protein expression levels of HDAC1, p-HDAC1, HDAC2, p-HDAC2, HDAC8 and p-HDAC8 in the chondrocytes by western blotting. (E) Co-IP experiments with DUSP26 protein from extracts of IL-1β-treated chondrocytes followed by western blotting with indicated antibodies. DEG, differentially expressed gene; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IB, immunoblot; IL, interleukin; IP, immunoprecipitation; LC-MS/MS, liquid chromatography-tandem MS; mRNA-seq, mRNA sequencing; MS, mass spectrometry; p-, phosphorylated.

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: HDAC1, HDAC2 and HDAC8 are DUSP26-interacting proteins in chondrocytes. (A) IP/MS analysis in DUSP26-overexpressing chondrocytes under IL-1β stimulation. (B) Flow chart of target protein screening. (C) Immunohistochemical staining of HDAC1, HDAC2 and HDAC8 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (D) Protein expression levels of HDAC1, p-HDAC1, HDAC2, p-HDAC2, HDAC8 and p-HDAC8 in the chondrocytes by western blotting. (E) Co-IP experiments with DUSP26 protein from extracts of IL-1β-treated chondrocytes followed by western blotting with indicated antibodies. DEG, differentially expressed gene; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IB, immunoblot; IL, interleukin; IP, immunoprecipitation; LC-MS/MS, liquid chromatography-tandem MS; mRNA-seq, mRNA sequencing; MS, mass spectrometry; p-, phosphorylated.

Techniques: Protein-Protein interactions, Immunohistochemical staining, Staining, Control, Expressing, Western Blot, Co-Immunoprecipitation Assay, Histone Deacetylase Assay, Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Liquid Chromatography, Sequencing, Mass Spectrometry

Inactivation of HDAC1/2/8 inhibits DUSP26 silencing-triggered cartilage degeneration. (A) Total protein and phosphorylation levels of HDAC1, HDAC2 and HDAC8 in IL-1β-treated chondrocytes determined by western blotting. (B) Relative mRNA expression levels of HDAC1, HDAC2 and HDAC8 in chondrocytes, as determined by reverse transcription-quantitative PCR. (C) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (D) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. (E) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (F) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. (B-D) Representative results of three independent experiments are shown. COL1A1, type I collagen; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IL, interleukin; NC, negative control; ns, no significance; sh, short hairpin; TSA, trichostatin A.

Journal: International Journal of Molecular Medicine

Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

doi: 10.3892/ijmm.2026.5776

Figure Lengend Snippet: Inactivation of HDAC1/2/8 inhibits DUSP26 silencing-triggered cartilage degeneration. (A) Total protein and phosphorylation levels of HDAC1, HDAC2 and HDAC8 in IL-1β-treated chondrocytes determined by western blotting. (B) Relative mRNA expression levels of HDAC1, HDAC2 and HDAC8 in chondrocytes, as determined by reverse transcription-quantitative PCR. (C) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (D) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. (E) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (F) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. (B-D) Representative results of three independent experiments are shown. COL1A1, type I collagen; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IL, interleukin; NC, negative control; ns, no significance; sh, short hairpin; TSA, trichostatin A.

Techniques: Phospho-proteomics, Western Blot, Expressing, Reverse Transcription, Real-time Polymerase Chain Reaction, Histone Deacetylase Assay, Negative Control

| In vivo anti-oxidant and anti-inflammatory effects of NTAl NPs against UC. A) H&E-stained sections of mouse colon following treatment with indicated materials. B) H&E staining histological scores. C) Typical TEM images showing the microstructures of colonic epitheliums. D-F) the expression of oxidative stress markers including MDA(D), SOD (E), and GSH-Px (F). G-J) the expression of colonic inflammatory cytokines including pro-inflammatory cytokines TNF-α (G), IL-1β (H), IL-6 (I) and anti-inflammatory cytokines IL-10 (J). All data are shown as mean ± s.d; n = 6. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001.

Journal: Materials Today Bio

Article Title: One-step green assembly of natural polyphenol-based nobiletin nanoparticles for ulcerative colitis therapy

doi: 10.1016/j.mtbio.2026.102887

Figure Lengend Snippet: | In vivo anti-oxidant and anti-inflammatory effects of NTAl NPs against UC. A) H&E-stained sections of mouse colon following treatment with indicated materials. B) H&E staining histological scores. C) Typical TEM images showing the microstructures of colonic epitheliums. D-F) the expression of oxidative stress markers including MDA(D), SOD (E), and GSH-Px (F). G-J) the expression of colonic inflammatory cytokines including pro-inflammatory cytokines TNF-α (G), IL-1β (H), IL-6 (I) and anti-inflammatory cytokines IL-10 (J). All data are shown as mean ± s.d; n = 6. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001.

Article Snippet: Commercial ELISA kits including Mouse TNF-α (EK282, Multi Sciences), Mouse IL-1β (EK201B, Multi Sciences), Mouse IL-6 (EK206, Multi Sciences), and Mouse IL-10 (EK210, Multi Sciences) were used to quantify pro-inflammatory cytokines and the anti-inflammatory cytokine according to the manufacturer's instructions.

Techniques: In Vivo, Staining, Expressing

Deletion of Usp34 accelerates cartilage destruction during TMJ OA. (A) Representative images of Safranin O/Fast Green staining of SHAM and UBR-induced TMJ OA mice. Scale bars: 100 μm for low and 50 μm for high magnification. (B and C) Quantitative analysis regarding cartilage thickness and modified Mankin score according to Safranin O/Fast Green staining. n = 6 per group. (D) Representative micro-CT images reveal the subchondral bone microstructure. Scale bars: 100 μm. (E) Quantitative analysis of subchondral bone parameters. (F and G) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, α-tubulin in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β. (H) Relative mRNA expression of MMP3, MMP13, ADAMTS4, and ADAMTS5 in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β.

Journal: JBMR Plus

Article Title: USP34 attenuates cartilage degradation in temporomandibular joint osteoarthritis by ANT1-mediated mitophagy

doi: 10.1093/jbmrpl/ziag004

Figure Lengend Snippet: Deletion of Usp34 accelerates cartilage destruction during TMJ OA. (A) Representative images of Safranin O/Fast Green staining of SHAM and UBR-induced TMJ OA mice. Scale bars: 100 μm for low and 50 μm for high magnification. (B and C) Quantitative analysis regarding cartilage thickness and modified Mankin score according to Safranin O/Fast Green staining. n = 6 per group. (D) Representative micro-CT images reveal the subchondral bone microstructure. Scale bars: 100 μm. (E) Quantitative analysis of subchondral bone parameters. (F and G) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, α-tubulin in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β. (H) Relative mRNA expression of MMP3, MMP13, ADAMTS4, and ADAMTS5 in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β.

Article Snippet: To model the inflammatory microenvironment of TMJ OA, ATDC5 cells (1 × 10 5 /well) were cultured in 24-well plates, followed by treatment with 10 ng/mL IL-1β (HY-P7073A; MedChemExpress).

Techniques: Staining, Modification, Micro-CT, Western Blot, Transfection, Expressing

USP34 deubiquitinates and stabilizes ANT1. (A) Volcano plots showing the differentially expressed proteins of USP34-deficient cells from public proteomic dataset in the National Genomics Data Center under accession numbers: OMIX007639. (B) Heatmap showing the differentially expressed protein of USP34-deficient cells from public proteomic dataset (OMIX007639). (C and D) Representative images and quantitative analysis of western blot for ANT1 and α-tubulin in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β. (E) Representative images of immunofluorescence staining of ANT1 in the TMJ cartilages of SHAM and UBR-induced TMJ OA mice. Scale bars: 50 μm. (F) Co-immunoprecipitation of USP34 with ectopically expressed ANT1 in HEK293T cells. (G) Immunoblot of ANT1-linked polyubiquitin. HEK293T cells were treated with 10 μM MG132 for 4 h after transfection with the indicated constructs. The cell lysates were subjected to immunoprecipitation with the indicated antibody. (H) Measurement of ANT1 degradation rate. HEK293T cells were transfected with the indicated constructs and treated with 10 mg/mL CHX.

Journal: JBMR Plus

Article Title: USP34 attenuates cartilage degradation in temporomandibular joint osteoarthritis by ANT1-mediated mitophagy

doi: 10.1093/jbmrpl/ziag004

Figure Lengend Snippet: USP34 deubiquitinates and stabilizes ANT1. (A) Volcano plots showing the differentially expressed proteins of USP34-deficient cells from public proteomic dataset in the National Genomics Data Center under accession numbers: OMIX007639. (B) Heatmap showing the differentially expressed protein of USP34-deficient cells from public proteomic dataset (OMIX007639). (C and D) Representative images and quantitative analysis of western blot for ANT1 and α-tubulin in ATDC5 cells transfected with Usp34 siRNA following exposure to IL-1β. (E) Representative images of immunofluorescence staining of ANT1 in the TMJ cartilages of SHAM and UBR-induced TMJ OA mice. Scale bars: 50 μm. (F) Co-immunoprecipitation of USP34 with ectopically expressed ANT1 in HEK293T cells. (G) Immunoblot of ANT1-linked polyubiquitin. HEK293T cells were treated with 10 μM MG132 for 4 h after transfection with the indicated constructs. The cell lysates were subjected to immunoprecipitation with the indicated antibody. (H) Measurement of ANT1 degradation rate. HEK293T cells were transfected with the indicated constructs and treated with 10 mg/mL CHX.

Techniques: Western Blot, Transfection, Immunofluorescence, Staining, Immunoprecipitation, Construct

ANT1 overexpression rescues mitochondrial homeostasis in USP34-deficient cells. (A and B) Representative images and quantitative analysis of western blot for LC3, Parkin, PINK1, and α-tubulin in ATDC5 cells transfected with Usp34 siRNA or Lv-ANT1 , following exposure to IL-1β. (C) Representative TEM images of ATDC5 cells transfected with Usp34 siRNA or Lv-ANT1 . Subcellular structures with discernible mitochondria (yellow arrows) and bound by a double limiting membrane are identified as putative mitophagosome structures (red arrows). Scale bars: 200 nm. (D) ATDC5 cells stained with mitotracker and lysotracker after transfection with Usp34 siRNA or Lv-ANT1 . Scale bars: 20 μm. (E) ATDC5 cells stained with Mito-SOX after transfection with Usp34 siRNA or Lv-ANT1 . Scale bars: 20 μm.

Journal: JBMR Plus

Article Title: USP34 attenuates cartilage degradation in temporomandibular joint osteoarthritis by ANT1-mediated mitophagy

doi: 10.1093/jbmrpl/ziag004

Figure Lengend Snippet: ANT1 overexpression rescues mitochondrial homeostasis in USP34-deficient cells. (A and B) Representative images and quantitative analysis of western blot for LC3, Parkin, PINK1, and α-tubulin in ATDC5 cells transfected with Usp34 siRNA or Lv-ANT1 , following exposure to IL-1β. (C) Representative TEM images of ATDC5 cells transfected with Usp34 siRNA or Lv-ANT1 . Subcellular structures with discernible mitochondria (yellow arrows) and bound by a double limiting membrane are identified as putative mitophagosome structures (red arrows). Scale bars: 200 nm. (D) ATDC5 cells stained with mitotracker and lysotracker after transfection with Usp34 siRNA or Lv-ANT1 . Scale bars: 20 μm. (E) ATDC5 cells stained with Mito-SOX after transfection with Usp34 siRNA or Lv-ANT1 . Scale bars: 20 μm.

Techniques: Over Expression, Western Blot, Transfection, Membrane, Staining

USP34 overexpression enhanced chondrocyte viability. (A and B) Representative images and quantitative analysis of western blot for LC3, Parkin, PINK1, and α-tubulin in ATDC5 cells transfected with Usp34 lentiviral activation particles ( Usp34 ac) following exposure to IL-1β. (C and D) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, and α-tubulin in ATDC5 cells transfected with Usp34 ac following exposure to IL-1β. (E and F) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, and α-tubulin in ATDC5 cells with the indicated treatment. (G) ATDC5 cells stained with Acan and Col2a1 after transfection with Usp34 ac or Lv-ANT1 . Scale bars: 50 μm. (H and I) Relative mRNA expression of Acan and Col2a1 in ATDC5 cells with the indicated treatments.

Journal: JBMR Plus

Article Title: USP34 attenuates cartilage degradation in temporomandibular joint osteoarthritis by ANT1-mediated mitophagy

doi: 10.1093/jbmrpl/ziag004

Figure Lengend Snippet: USP34 overexpression enhanced chondrocyte viability. (A and B) Representative images and quantitative analysis of western blot for LC3, Parkin, PINK1, and α-tubulin in ATDC5 cells transfected with Usp34 lentiviral activation particles ( Usp34 ac) following exposure to IL-1β. (C and D) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, and α-tubulin in ATDC5 cells transfected with Usp34 ac following exposure to IL-1β. (E and F) Representative images and quantitative analysis of western blot for MMP13, ADAMTS5, and α-tubulin in ATDC5 cells with the indicated treatment. (G) ATDC5 cells stained with Acan and Col2a1 after transfection with Usp34 ac or Lv-ANT1 . Scale bars: 50 μm. (H and I) Relative mRNA expression of Acan and Col2a1 in ATDC5 cells with the indicated treatments.

Techniques: Over Expression, Western Blot, Transfection, Activation Assay, Staining, Expressing

RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Expressing, Agarose Gel Electrophoresis, Knock-Out, Staining, Western Blot

RMST-KO reduced the inflammation during mouse skin wound healing. (A–B) QPCR assay showed the mRNA expression of TNF-α and IL-1β were significantly decreased in the RMST-KO group 21 dps. (C) Representative blot of TNF-α, IL-1β 21 dps. (D–E) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed TNF-α, IL-1β expression 21 dps. Data were shown as mean ± SD, n = 6, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: RMST-KO reduced the inflammation during mouse skin wound healing. (A–B) QPCR assay showed the mRNA expression of TNF-α and IL-1β were significantly decreased in the RMST-KO group 21 dps. (C) Representative blot of TNF-α, IL-1β 21 dps. (D–E) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed TNF-α, IL-1β expression 21 dps. Data were shown as mean ± SD, n = 6, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Expressing, Western Blot

Smad3 was a downstream molecule of lncRNA RMST. (A) The heatmap shows the upregulated long non-coding RNAs in the GSE28914 dataset. (B) The catRAPID omics v2.1 software was used to predict the proteins interacting with RMST. (C) A Venn diagram displays the intersection of the two groups of data. (D) GO and KEGG pathway analysis was performed for these 273 intersections.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: Smad3 was a downstream molecule of lncRNA RMST. (A) The heatmap shows the upregulated long non-coding RNAs in the GSE28914 dataset. (B) The catRAPID omics v2.1 software was used to predict the proteins interacting with RMST. (C) A Venn diagram displays the intersection of the two groups of data. (D) GO and KEGG pathway analysis was performed for these 273 intersections.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Software

Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Western Blot, Staining

SPH attenuates pathological changes and suppresses NLRP3 inflammasome activation in the hearts of hypertensive mice. (A, B) Masson's trichrome staining of heart (A) and aorta (B) sections, showing reduced collagen deposition (blue) with SPH treatment. Scale bars: 20 μm for heart, 50 μm (main) and 20 μm (inset) for aorta. (C) H&E staining of heart sections showing amelioration of myocardial disarray and inflammation. Scale bars: 500 μm (main) and 20 μm (inset).(D) ELISA quantification of serum IL-18 and IL-1β levels. Data are mean ± SEM. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001 vs. HBP group. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Journal: International Journal of Cardiology. Cardiovascular Risk and Prevention

Article Title: The sphingolipid metabolite sphingosine protects against hypertension by targeting metabolic-inflammatory crosstalk via the NLRP3 inflammasome

doi: 10.1016/j.ijcrp.2025.200562

Figure Lengend Snippet: SPH attenuates pathological changes and suppresses NLRP3 inflammasome activation in the hearts of hypertensive mice. (A, B) Masson's trichrome staining of heart (A) and aorta (B) sections, showing reduced collagen deposition (blue) with SPH treatment. Scale bars: 20 μm for heart, 50 μm (main) and 20 μm (inset) for aorta. (C) H&E staining of heart sections showing amelioration of myocardial disarray and inflammation. Scale bars: 500 μm (main) and 20 μm (inset).(D) ELISA quantification of serum IL-18 and IL-1β levels. Data are mean ± SEM. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001 vs. HBP group. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Article Snippet: Serum levels of interleukin-18 (IL-18) and interleukin-1β (IL-1β) were quantified using commercial enzyme-linked immunosorbent assay (ELISA) kits (IL-18: Lianke, Cat#EK218-96; IL-1β: Lianke, Cat# EK201BHS-96) according to the manufacturers' instructions.

Techniques: Activation Assay, Staining, Enzyme-linked Immunosorbent Assay

SPH mitigates Angiotensin II-induced inflammasome activation, apoptosis, and oxidative stress in HUVECs. (A, B) Representative immunofluorescence images showing increased expression of NLRP3 (red, A) and ASC (green, B) in AngII-treated cells, which is reduced by subsequent SPH treatment. Scale bar = 100 μm. (C) TUNEL assay (green) demonstrating increased apoptosis in AngII-treated cells, which is attenuated by SPH. Scale bar = 100 μm. (D, E) Biochemical assays showing that SPH or MCC950 treatment reverses the AngII-induced decrease in SOD1 activity (G).NO (H) and increase in MDA levels (D). (F, G) DCFH-DA staining showing increased intracellular ROS (green) after AngII treatment, which is suppressed by SPH or MCC950. Representative images (F) and quantification (E) are shown. (I, J) ELISA results showing that SPH or MCC950 treatment inhibits the AngII-induced secretion of IL-1β (I) and IL-18 (J). (K) Scanning electron microscopy (SEM) images showing that SPH or MCC950 treatment improves the cell surface morphology and reduces features of pyroptotic damage induced by AngII. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Journal: International Journal of Cardiology. Cardiovascular Risk and Prevention

Article Title: The sphingolipid metabolite sphingosine protects against hypertension by targeting metabolic-inflammatory crosstalk via the NLRP3 inflammasome

doi: 10.1016/j.ijcrp.2025.200562

Figure Lengend Snippet: SPH mitigates Angiotensin II-induced inflammasome activation, apoptosis, and oxidative stress in HUVECs. (A, B) Representative immunofluorescence images showing increased expression of NLRP3 (red, A) and ASC (green, B) in AngII-treated cells, which is reduced by subsequent SPH treatment. Scale bar = 100 μm. (C) TUNEL assay (green) demonstrating increased apoptosis in AngII-treated cells, which is attenuated by SPH. Scale bar = 100 μm. (D, E) Biochemical assays showing that SPH or MCC950 treatment reverses the AngII-induced decrease in SOD1 activity (G).NO (H) and increase in MDA levels (D). (F, G) DCFH-DA staining showing increased intracellular ROS (green) after AngII treatment, which is suppressed by SPH or MCC950. Representative images (F) and quantification (E) are shown. (I, J) ELISA results showing that SPH or MCC950 treatment inhibits the AngII-induced secretion of IL-1β (I) and IL-18 (J). (K) Scanning electron microscopy (SEM) images showing that SPH or MCC950 treatment improves the cell surface morphology and reduces features of pyroptotic damage induced by AngII. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Techniques: Activation Assay, Immunofluorescence, Expressing, TUNEL Assay, Activity Assay, Staining, Enzyme-linked Immunosorbent Assay, Electron Microscopy

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