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Schematic illustration of Gel BC@ZnO synthesis and the proposed bioelectric <t>signal-Piezo1-Ca</t> 2+ -efferocytosis mechanism for diabetic bone repair.
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All the primers listed in this study.
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Screening-identified asiatic acid inhibits FBP1 and promotes wound healing. (A) The relative FBP1 activity after the candidate compounds (50 μM) treatment using the FBP1 activity assay kit. (B) The chemical structure of AA. (C) Molecular docking structural model depicting asiatic acid-FBP1 binding interactions at the catalytic pocket (D) The effect of AA and AMP (0.01–100 μM) on FBP1 activity was detected by FBP1 activity assay kit. (E) CETSA analysis demonstrated enhanced FBP1 thermostability in asiatic acid-treated HaCaT cells. (F) Scratch wound healing assay demonstrated the migration changes after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (G) HaCaT cells exposed to asiatic acid (0.2–200 μM) for 24 h underwent MTT assay to quantify dose-dependent viability effects. (H) Clonal numbers after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (I) Transwell assay assessing invasion of HaCaT cells stimulated with MGO and overexpressing FBP1 after the introduction of AA. (J, K) Observation of HaCaT cells proliferation following AA administration using <t>Ki67</t> staining (Scale bar = 100 μm). (L) Phalloidin staining after AA introduction in HaCaT cells stimulated with MGO and overexpressing FBP1. Data represent mean ± SEM from three independent replicates. * P < 0.05, ** P < 0.01, *** P < 0.001 vs Ctrl group. ^ P < 0.05, ^^ P < 0.01 vs OE group. & P < 0.05, && P < 0.01 vs NC group. # P < 0.05, ## P < 0.01 vs MGO group.
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Osteogenic differentiation-promoting effect of DBM-DMSN@TPTD composite scaffold on BMSCs. ( A ) ALP staining of BMSCs after 7 days of culture. ( B ) Immunofluorescence staining of <t>RUNX2</t> in BMSCs. ( C ) Immunofluorescence staining of OCN in BMSCs. ( D ) Quantitative analysis of RUNX2 mean fluorescence intensity. ( E ) Quantitative analysis of OCN mean fluorescence intensity. Data are presented as mean ± SD ( n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Tukey’s multiple comparisons post hoc test. ns, no significant difference; * p < 0.05; ** p < 0.01; *** p < 0.001.
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Osteogenic differentiation-promoting effect of DBM-DMSN@TPTD composite scaffold on BMSCs. ( A ) ALP staining of BMSCs after 7 days of culture. ( B ) Immunofluorescence staining of <t>RUNX2</t> in BMSCs. ( C ) Immunofluorescence staining of OCN in BMSCs. ( D ) Quantitative analysis of RUNX2 mean fluorescence intensity. ( E ) Quantitative analysis of OCN mean fluorescence intensity. Data are presented as mean ± SD ( n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Tukey’s multiple comparisons post hoc test. ns, no significant difference; * p < 0.05; ** p < 0.01; *** p < 0.001.
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Image Search Results


Schematic illustration of Gel BC@ZnO synthesis and the proposed bioelectric signal-Piezo1-Ca 2+ -efferocytosis mechanism for diabetic bone repair.

Journal: Bioactive Materials

Article Title: Bioelectric signals promote diabetic bone regeneration through Piezo1-mediated activation of the efferocytic immune microenvironment

doi: 10.1016/j.bioactmat.2026.05.037

Figure Lengend Snippet: Schematic illustration of Gel BC@ZnO synthesis and the proposed bioelectric signal-Piezo1-Ca 2+ -efferocytosis mechanism for diabetic bone repair.

Article Snippet: Cells were permeabilized with 0.5% Triton X-100, blocked with 5% BSA, and incubated overnight at 4 °C with anti-Piezo1 primary antibody (Abclonal; 1:100) in immunostaining dilution buffer (Beyotime Biotechnology, China).

Techniques:

Ultrasound-triggered Gel BC@ZnO promotes Piezo1 activation and macrophage efferocytosis. A) Piezo1 immunofluorescence staining. B) Representative flow-cytometry plots showing CFSE signal in gated macrophages after co-culture with CFSE-labeled apoptotic Jurkat cells. Before co-culture, camptothecin-induced Jurkat cells were quality-checked by Annexin V/7-AAD staining to ensure an apoptosis-enriched target-cell population and minimize necrotic/debris contamination. C) Fluorescence images showing intracellular CFSE signals in macrophages. D) Quantification of Piezo1 immunofluorescence. E) Quantification of CFSE-positive macrophages by flow cytometry. F) Percentage of efferocytic macrophages, defined as F4/80+CFSE + events among total F4/80+ macrophages after exclusion of debris, doublets, and F4/80-negative free apoptotic cells/debris. G) Quantification of intracellular CFSE fluorescence intensity. Data are presented as mean ± SD; error bars indicate SD. Statistical comparisons were performed using one-way ANOVA followed by Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3.

Journal: Bioactive Materials

Article Title: Bioelectric signals promote diabetic bone regeneration through Piezo1-mediated activation of the efferocytic immune microenvironment

doi: 10.1016/j.bioactmat.2026.05.037

Figure Lengend Snippet: Ultrasound-triggered Gel BC@ZnO promotes Piezo1 activation and macrophage efferocytosis. A) Piezo1 immunofluorescence staining. B) Representative flow-cytometry plots showing CFSE signal in gated macrophages after co-culture with CFSE-labeled apoptotic Jurkat cells. Before co-culture, camptothecin-induced Jurkat cells were quality-checked by Annexin V/7-AAD staining to ensure an apoptosis-enriched target-cell population and minimize necrotic/debris contamination. C) Fluorescence images showing intracellular CFSE signals in macrophages. D) Quantification of Piezo1 immunofluorescence. E) Quantification of CFSE-positive macrophages by flow cytometry. F) Percentage of efferocytic macrophages, defined as F4/80+CFSE + events among total F4/80+ macrophages after exclusion of debris, doublets, and F4/80-negative free apoptotic cells/debris. G) Quantification of intracellular CFSE fluorescence intensity. Data are presented as mean ± SD; error bars indicate SD. Statistical comparisons were performed using one-way ANOVA followed by Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3.

Article Snippet: Cells were permeabilized with 0.5% Triton X-100, blocked with 5% BSA, and incubated overnight at 4 °C with anti-Piezo1 primary antibody (Abclonal; 1:100) in immunostaining dilution buffer (Beyotime Biotechnology, China).

Techniques: Activation Assay, Immunofluorescence, Staining, Flow Cytometry, Co-Culture Assay, Labeling, Fluorescence, Comparison

Gel BC@ZnO + US induces Piezo1-dependent Ca 2+ influx and macrophage immunomodulation in vitro. A, B) Representative flow-cytometry plots and quantification of FITC-Ca 2+ -positive macrophages. C, D) Representative fluorescence images and MFI quantification of intracellular Ca 2+ in macrophages. E, F) Representative flow-cytometry plots and quantification of FITC-Ca 2+ -positive osteoblastic cells. G, H) Representative fluorescence images and MFI quantification of intracellular Ca 2+ in osteoblastic cells. I) Flow-cytometry analysis of macrophage polarization based on CD206 and CD86 expression. J, K) Representative flow-cytometry histograms and quantification of intracellular ROS. GsMTx4 was used as a Piezo1 inhibitor. Data are presented as mean ± SD; error bars indicate SD. Statistical significance was determined by one-way ANOVA with Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3. Scale bars: 100 μm in C and 150 μm in G.

Journal: Bioactive Materials

Article Title: Bioelectric signals promote diabetic bone regeneration through Piezo1-mediated activation of the efferocytic immune microenvironment

doi: 10.1016/j.bioactmat.2026.05.037

Figure Lengend Snippet: Gel BC@ZnO + US induces Piezo1-dependent Ca 2+ influx and macrophage immunomodulation in vitro. A, B) Representative flow-cytometry plots and quantification of FITC-Ca 2+ -positive macrophages. C, D) Representative fluorescence images and MFI quantification of intracellular Ca 2+ in macrophages. E, F) Representative flow-cytometry plots and quantification of FITC-Ca 2+ -positive osteoblastic cells. G, H) Representative fluorescence images and MFI quantification of intracellular Ca 2+ in osteoblastic cells. I) Flow-cytometry analysis of macrophage polarization based on CD206 and CD86 expression. J, K) Representative flow-cytometry histograms and quantification of intracellular ROS. GsMTx4 was used as a Piezo1 inhibitor. Data are presented as mean ± SD; error bars indicate SD. Statistical significance was determined by one-way ANOVA with Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3. Scale bars: 100 μm in C and 150 μm in G.

Article Snippet: Cells were permeabilized with 0.5% Triton X-100, blocked with 5% BSA, and incubated overnight at 4 °C with anti-Piezo1 primary antibody (Abclonal; 1:100) in immunostaining dilution buffer (Beyotime Biotechnology, China).

Techniques: In Vitro, Flow Cytometry, Fluorescence, Expressing, Comparison

Gel BC@ZnO + US accelerates diabetic bone-defect repair in vivo. A) Micro-CT images showing new bone formation in diabetic rat femoral condyle defects 8 weeks after surgery. B) Quantitative micro-CT analysis of regenerated bone. C) H&E and Masson's trichrome staining after 8 weeks. D) Piezo1 immunofluorescence staining in the defect area. E) Semi-quantitative analysis of Piezo1-positive area. Data are presented as mean ± SD; error bars indicate SD. Statistical comparisons were performed using one-way ANOVA followed by Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3.

Journal: Bioactive Materials

Article Title: Bioelectric signals promote diabetic bone regeneration through Piezo1-mediated activation of the efferocytic immune microenvironment

doi: 10.1016/j.bioactmat.2026.05.037

Figure Lengend Snippet: Gel BC@ZnO + US accelerates diabetic bone-defect repair in vivo. A) Micro-CT images showing new bone formation in diabetic rat femoral condyle defects 8 weeks after surgery. B) Quantitative micro-CT analysis of regenerated bone. C) H&E and Masson's trichrome staining after 8 weeks. D) Piezo1 immunofluorescence staining in the defect area. E) Semi-quantitative analysis of Piezo1-positive area. Data are presented as mean ± SD; error bars indicate SD. Statistical comparisons were performed using one-way ANOVA followed by Tukey's multiple-comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001, n = 3.

Article Snippet: Cells were permeabilized with 0.5% Triton X-100, blocked with 5% BSA, and incubated overnight at 4 °C with anti-Piezo1 primary antibody (Abclonal; 1:100) in immunostaining dilution buffer (Beyotime Biotechnology, China).

Techniques: In Vivo, Micro-CT, Staining, Immunofluorescence, Comparison

All the primers listed in this study.

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: All the primers listed in this study.

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques: Sequencing

Quantitative analysis of collagen abundance in the calipash and muscle. ( A , B ) Representative Masson’s trichrome-stained sections utilized for collagen quantification in calipash ( A ) and muscle ( B ). ( A1 – A3 ) The first/second/third microscopic field in calipash; ( B1 – B3 ) The first/second/third microscopic field in muscle. The microscopic images are representative fields from the same individual and were used for visualization only. ( C ) Quantitative comparison of the collagen area fraction between the calipash and muscle tissues. Data are presented as mean ± SD ( n = 3) calculated from three independent microscopic fields. * p < 0.05 indicates significant differences.

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: Quantitative analysis of collagen abundance in the calipash and muscle. ( A , B ) Representative Masson’s trichrome-stained sections utilized for collagen quantification in calipash ( A ) and muscle ( B ). ( A1 – A3 ) The first/second/third microscopic field in calipash; ( B1 – B3 ) The first/second/third microscopic field in muscle. The microscopic images are representative fields from the same individual and were used for visualization only. ( C ) Quantitative comparison of the collagen area fraction between the calipash and muscle tissues. Data are presented as mean ± SD ( n = 3) calculated from three independent microscopic fields. * p < 0.05 indicates significant differences.

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques: Analysis, Staining, Comparison

Comparative Picro Sirius Red staining of collagen subtype composition and spatial organization. ( A1 – A4 ) Representative brightfield microscopy images of the calipash acquired at increasing magnification. Scale bars: 200 μm ( A1 ), 100 μm ( A2 ), 50 μm ( A3 ) and 20 μm ( A4 ). ( B1 – B4 ) Representative polarized light microscopy images of the calipash acquired at increasing magnification. Scale bars: 200 μm ( B1 ), 100 μm ( B2 ), 50 μm ( B3 ) and 20 μm ( B4 ). ( C1 – C4 ) Representative brightfield microscopy images of muscle acquired at increasing magnification. Scale bars: 200 μm ( C1 ), 100 μm ( C2 ), 50 μm ( C3 ) and 20 μm ( C4 ). ( D1 – D4 ) Representative polarized light microscopy images of muscle acquired at increasing magnification. Scale bars: 200 μm ( D1 ), 100 μm ( D2 ), 50 μm ( D3 ) and 20 μm ( D4 ). Yellow-orange birefringence indicates densely packed type I collagen, while green birefringence is indicative of type III collagen-rich regions. Scale bars are as indicated in the respective images.

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: Comparative Picro Sirius Red staining of collagen subtype composition and spatial organization. ( A1 – A4 ) Representative brightfield microscopy images of the calipash acquired at increasing magnification. Scale bars: 200 μm ( A1 ), 100 μm ( A2 ), 50 μm ( A3 ) and 20 μm ( A4 ). ( B1 – B4 ) Representative polarized light microscopy images of the calipash acquired at increasing magnification. Scale bars: 200 μm ( B1 ), 100 μm ( B2 ), 50 μm ( B3 ) and 20 μm ( B4 ). ( C1 – C4 ) Representative brightfield microscopy images of muscle acquired at increasing magnification. Scale bars: 200 μm ( C1 ), 100 μm ( C2 ), 50 μm ( C3 ) and 20 μm ( C4 ). ( D1 – D4 ) Representative polarized light microscopy images of muscle acquired at increasing magnification. Scale bars: 200 μm ( D1 ), 100 μm ( D2 ), 50 μm ( D3 ) and 20 μm ( D4 ). Yellow-orange birefringence indicates densely packed type I collagen, while green birefringence is indicative of type III collagen-rich regions. Scale bars are as indicated in the respective images.

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques: Staining, Brightfield, Microscopy, Light Microscopy

Comparative immunofluorescence localization of COL1A1 in calipash ( A1 – A3 ) and muscle ( B1 – B3 ) tissues. ( A1 ) Representative immunofluorescence image showing the spatial distribution of COL1A1 (green) in calipash at low magnification; scale bar, 200 μm. ( A2 ) Higher-magnification image of a representative field of view in calipash; scale bar, 50 μm. ( A3 ) Higher-magnification image of a second, independent field of view in calipash; scale bar, 50 μm. ( B1 ) Spatial distribution of COL1A1 (red) in muscle tissue at low magnification; scale bar, 200 μm. ( B2 ) Higher-magnification image of a representative field of view in muscle; scale bar, 50 μm. ( B3 ) Higher-magnification image of a second, independent field of view in muscle; scale bar, 50 μm. Nuclei were counterstained with DAPI (blue). Scale bars are as indicated in the respective images.

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: Comparative immunofluorescence localization of COL1A1 in calipash ( A1 – A3 ) and muscle ( B1 – B3 ) tissues. ( A1 ) Representative immunofluorescence image showing the spatial distribution of COL1A1 (green) in calipash at low magnification; scale bar, 200 μm. ( A2 ) Higher-magnification image of a representative field of view in calipash; scale bar, 50 μm. ( A3 ) Higher-magnification image of a second, independent field of view in calipash; scale bar, 50 μm. ( B1 ) Spatial distribution of COL1A1 (red) in muscle tissue at low magnification; scale bar, 200 μm. ( B2 ) Higher-magnification image of a representative field of view in muscle; scale bar, 50 μm. ( B3 ) Higher-magnification image of a second, independent field of view in muscle; scale bar, 50 μm. Nuclei were counterstained with DAPI (blue). Scale bars are as indicated in the respective images.

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques: Immunofluorescence, Tissue

Collagen gene expression profiling, transcriptional validation, and protein-level confirmation in calipash and muscle of P. sinensis . ( A ) Volcano plot of collagen-related DEGs. Each point represents a gene, with significantly upregulated (green) and downregulated (orange) genes in calipash defined by |log 2 fold change| ≥ 1 and FDR < 0.05. The x -axis represents log 2 fold change, and the y -axis represents log 10 adjusted p value. Collagen-related genes are highlighted, including col1a1 , col1a2 , col3a1 , col6a1 , col6a2 , col4a6 , col4a5 , col5a3 , col7a1 , col12a1 , col16a1 , and col17a1 . ( B ) Targeted qPCR validation of col1a1 and col1a2 expression in calipash and muscle. Data are presented as mean ± SD ( n = 3). Asterisks indicate significant differences between calipash and muscle ( p < 0.05). ( C ) Western blot analysis of COL1A1 protein in calipash and muscle. β-actin was used as the loading control.

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: Collagen gene expression profiling, transcriptional validation, and protein-level confirmation in calipash and muscle of P. sinensis . ( A ) Volcano plot of collagen-related DEGs. Each point represents a gene, with significantly upregulated (green) and downregulated (orange) genes in calipash defined by |log 2 fold change| ≥ 1 and FDR < 0.05. The x -axis represents log 2 fold change, and the y -axis represents log 10 adjusted p value. Collagen-related genes are highlighted, including col1a1 , col1a2 , col3a1 , col6a1 , col6a2 , col4a6 , col4a5 , col5a3 , col7a1 , col12a1 , col16a1 , and col17a1 . ( B ) Targeted qPCR validation of col1a1 and col1a2 expression in calipash and muscle. Data are presented as mean ± SD ( n = 3). Asterisks indicate significant differences between calipash and muscle ( p < 0.05). ( C ) Western blot analysis of COL1A1 protein in calipash and muscle. β-actin was used as the loading control.

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques: Gene Expression, Profiling, Biomarker Discovery, Expressing, Western Blot, Analysis, Control

DEGs related to collagen in the muscle and calipash of P. sinensis .

Journal: Animals : an Open Access Journal from MDPI

Article Title: Integrated Histological and Transcriptomic Analyses Reveal Distinct Structural and Molecular Features of the Calipash and Muscle in the Chinese Soft-Shelled Turtle ( Pelodiscus sinensis )

doi: 10.3390/ani16182960

Figure Lengend Snippet: DEGs related to collagen in the muscle and calipash of P. sinensis .

Article Snippet: After blocking with 10% goat serum (Boster Biological Technology Co., Ltd., Wuhan, China) for 30 min, the sections were incubated with a rabbit anti-COL1A1 primary antibody (ABclonal Biotechnology Co., Ltd., Wuhan, China; 1:200 dilution) overnight at 4 °C.

Techniques:

ECH alleviates cisplatin-induced renal injury and inflammation in vivo. ( A ) Serum BUN levels in each group. ( B ) Serum creatinine levels of each group. ( C ) Serum KIM-1 levels detected by ELISA. ( D ) Serum NGAL levels detected by ELISA. ( E ) Representative H&E, PAS and KIM-1 immunohistochemical staining images of kidney tissues and quantitative analysis. ( F ) Western blot analysis and quantitative analysis of KIM-1 and NGAL protein in kidney tissues. ( G – J ) Relative mRNA levels of IL-1β, MCP-1, TNF-α and IL-6 in kidney tissues. ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01 vs. cisplatin group. n = 3 mice per group.

Journal: Biomedicines

Article Title: Echinacoside Alleviates Cisplatin-Induced Acute Kidney Injury by Regulating Bap1 to Inhibit Ferroptosis

doi: 10.3390/biomedicines14092127

Figure Lengend Snippet: ECH alleviates cisplatin-induced renal injury and inflammation in vivo. ( A ) Serum BUN levels in each group. ( B ) Serum creatinine levels of each group. ( C ) Serum KIM-1 levels detected by ELISA. ( D ) Serum NGAL levels detected by ELISA. ( E ) Representative H&E, PAS and KIM-1 immunohistochemical staining images of kidney tissues and quantitative analysis. ( F ) Western blot analysis and quantitative analysis of KIM-1 and NGAL protein in kidney tissues. ( G – J ) Relative mRNA levels of IL-1β, MCP-1, TNF-α and IL-6 in kidney tissues. ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01 vs. cisplatin group. n = 3 mice per group.

Article Snippet: After membrane blocking, primary antibodies targeting KIM-1 (A24493, ABclonal, Wuhan, China), NGAL (A2092, ABclonal, Wuhan, China), GPX4 (A27995, ABclonal, Wuhan, China), Slc7a11 (A25302, ABclonal, Wuhan, China), Bap1 (A6533SP, ABclonal, Wuhan, China) and the internal reference GAPDH (A19056, ABclonal, Wuhan, China) were incubated overnight at 4 °C, followed by incubation with corresponding secondary antibodies.

Techniques: In Vivo, Enzyme-linked Immunosorbent Assay, Immunohistochemical staining, Staining, Analysis, Western Blot, Control

ECH relieves cisplatin-induced cell damage in vitro. ( A ) HK-2 cell viability treated after treatment with different concentrations of ECH. ( B ) HK-2 cell viability under cisplatin stimulation with gradient ECH intervention. ( C ) Representative PI staining images of HK-2 cells and quantitative analysis. ( D ) Western blot and quantitative analysis of KIM-1 and NGAL proteins in HK-2 cells. ( E – H ) Relative mRNA levels of IL-1β, MCP-1, TNF-α and IL-6 in HK-2 cells. ns, no significancant; * p < 0.05, ** p < 0.01 vs. control group; # p < 0.05 vs. cisplatin group.

Journal: Biomedicines

Article Title: Echinacoside Alleviates Cisplatin-Induced Acute Kidney Injury by Regulating Bap1 to Inhibit Ferroptosis

doi: 10.3390/biomedicines14092127

Figure Lengend Snippet: ECH relieves cisplatin-induced cell damage in vitro. ( A ) HK-2 cell viability treated after treatment with different concentrations of ECH. ( B ) HK-2 cell viability under cisplatin stimulation with gradient ECH intervention. ( C ) Representative PI staining images of HK-2 cells and quantitative analysis. ( D ) Western blot and quantitative analysis of KIM-1 and NGAL proteins in HK-2 cells. ( E – H ) Relative mRNA levels of IL-1β, MCP-1, TNF-α and IL-6 in HK-2 cells. ns, no significancant; * p < 0.05, ** p < 0.01 vs. control group; # p < 0.05 vs. cisplatin group.

Article Snippet: After membrane blocking, primary antibodies targeting KIM-1 (A24493, ABclonal, Wuhan, China), NGAL (A2092, ABclonal, Wuhan, China), GPX4 (A27995, ABclonal, Wuhan, China), Slc7a11 (A25302, ABclonal, Wuhan, China), Bap1 (A6533SP, ABclonal, Wuhan, China) and the internal reference GAPDH (A19056, ABclonal, Wuhan, China) were incubated overnight at 4 °C, followed by incubation with corresponding secondary antibodies.

Techniques: In Vitro, Staining, Analysis, Western Blot, Control

Screening-identified asiatic acid inhibits FBP1 and promotes wound healing. (A) The relative FBP1 activity after the candidate compounds (50 μM) treatment using the FBP1 activity assay kit. (B) The chemical structure of AA. (C) Molecular docking structural model depicting asiatic acid-FBP1 binding interactions at the catalytic pocket (D) The effect of AA and AMP (0.01–100 μM) on FBP1 activity was detected by FBP1 activity assay kit. (E) CETSA analysis demonstrated enhanced FBP1 thermostability in asiatic acid-treated HaCaT cells. (F) Scratch wound healing assay demonstrated the migration changes after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (G) HaCaT cells exposed to asiatic acid (0.2–200 μM) for 24 h underwent MTT assay to quantify dose-dependent viability effects. (H) Clonal numbers after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (I) Transwell assay assessing invasion of HaCaT cells stimulated with MGO and overexpressing FBP1 after the introduction of AA. (J, K) Observation of HaCaT cells proliferation following AA administration using Ki67 staining (Scale bar = 100 μm). (L) Phalloidin staining after AA introduction in HaCaT cells stimulated with MGO and overexpressing FBP1. Data represent mean ± SEM from three independent replicates. * P < 0.05, ** P < 0.01, *** P < 0.001 vs Ctrl group. ^ P < 0.05, ^^ P < 0.01 vs OE group. & P < 0.05, && P < 0.01 vs NC group. # P < 0.05, ## P < 0.01 vs MGO group.

Journal: Journal of Advanced Research

Article Title: Discovery of FBP1 as novel therapeutic target and asiatic acid-hydrogen sulfide donors accelerate diabetic wound healing

doi: 10.1016/j.jare.2025.12.003

Figure Lengend Snippet: Screening-identified asiatic acid inhibits FBP1 and promotes wound healing. (A) The relative FBP1 activity after the candidate compounds (50 μM) treatment using the FBP1 activity assay kit. (B) The chemical structure of AA. (C) Molecular docking structural model depicting asiatic acid-FBP1 binding interactions at the catalytic pocket (D) The effect of AA and AMP (0.01–100 μM) on FBP1 activity was detected by FBP1 activity assay kit. (E) CETSA analysis demonstrated enhanced FBP1 thermostability in asiatic acid-treated HaCaT cells. (F) Scratch wound healing assay demonstrated the migration changes after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (G) HaCaT cells exposed to asiatic acid (0.2–200 μM) for 24 h underwent MTT assay to quantify dose-dependent viability effects. (H) Clonal numbers after AA administration in HaCaT cells stimulated with MGO and overexpressing FBP1. (I) Transwell assay assessing invasion of HaCaT cells stimulated with MGO and overexpressing FBP1 after the introduction of AA. (J, K) Observation of HaCaT cells proliferation following AA administration using Ki67 staining (Scale bar = 100 μm). (L) Phalloidin staining after AA introduction in HaCaT cells stimulated with MGO and overexpressing FBP1. Data represent mean ± SEM from three independent replicates. * P < 0.05, ** P < 0.01, *** P < 0.001 vs Ctrl group. ^ P < 0.05, ^^ P < 0.01 vs OE group. & P < 0.05, && P < 0.01 vs NC group. # P < 0.05, ## P < 0.01 vs MGO group.

Article Snippet: For immunostaining, primary antibody targeting Ki67 (ABclonal, Wuhan, China) was applied and incubated overnight at 4 °C.

Techniques: Activity Assay, Binding Assay, Wound Healing Assay, Migration, MTT Assay, Transwell Assay, Staining

Osteogenic differentiation-promoting effect of DBM-DMSN@TPTD composite scaffold on BMSCs. ( A ) ALP staining of BMSCs after 7 days of culture. ( B ) Immunofluorescence staining of RUNX2 in BMSCs. ( C ) Immunofluorescence staining of OCN in BMSCs. ( D ) Quantitative analysis of RUNX2 mean fluorescence intensity. ( E ) Quantitative analysis of OCN mean fluorescence intensity. Data are presented as mean ± SD ( n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Tukey’s multiple comparisons post hoc test. ns, no significant difference; * p < 0.05; ** p < 0.01; *** p < 0.001.

Journal: Pharmaceutics

Article Title: Dendritic Mesoporous Silica-Modified Decellularized Bone Matrix Scaffold for Sustained Teriparatide Delivery in Bone Defect Repair: Characterization, Drug Release, and In Vitro Biological Performance

doi: 10.3390/pharmaceutics18091067

Figure Lengend Snippet: Osteogenic differentiation-promoting effect of DBM-DMSN@TPTD composite scaffold on BMSCs. ( A ) ALP staining of BMSCs after 7 days of culture. ( B ) Immunofluorescence staining of RUNX2 in BMSCs. ( C ) Immunofluorescence staining of OCN in BMSCs. ( D ) Quantitative analysis of RUNX2 mean fluorescence intensity. ( E ) Quantitative analysis of OCN mean fluorescence intensity. Data are presented as mean ± SD ( n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Tukey’s multiple comparisons post hoc test. ns, no significant difference; * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: Subsequently, the cells were blocked with 5% bovine serum albumin (BSA, Sigma-Aldrich, St. Louis, MO, USA) at 37 °C for 30 min. Primary antibodies against RUNX2 (ABclonal Technology Co., Ltd., Wuhan, Hubei, China) and OCN (ABclonal Technology Co., Ltd., Wuhan, Hubei, China) were added and incubated overnight at 4 °C in a humidified chamber.

Techniques: Staining, Immunofluorescence, Analysis, Fluorescence