Journal: Journal of Sport and Health Science

Article Title: Weightlifting outperforms voluntary wheel running for improving adiposity and insulin sensitivity in obese mice

doi: 10.1016/j.jshs.2025.101100

Figure Lengend Snippet: Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and AS160 phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 S318, and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.

Article Snippet: Primary antibodies used for analysis were from Cell Signaling Technologies (Danvers, MA, USA) and diluted 1:1000 unless otherwise stated as follows: protein kinase B (Akt; 1:500; #4691; Cell Signaling Technologies), phospho-Akt (pAkt) S473 (1:500; #9271; Cell Signaling Technologies), Ubiquitin (#3933; Cell Signaling Technologies), microtubule-associated protein light chain 3 (LC3 II/I; #4018; Cell Signaling Technologies), cytochrome c oxidase subunit 4(COX4; #11967; Cell Signaling Technologies), Akt substrate 160 (AS160 S318; #8619; Cell Signaling Technologies), AS160 T642 (#8881; Cell Signaling Technologies), eukaryotic translation initiation factor 4E binding protein (4E-BP1; #9452; Cell Signaling Technologies), and glyceraldehyde 3 phosphate dehydrogenase (GAPDH; #2118; Cell Signaling Technologies).

Techniques: Phospho-proteomics, Injection, Western Blot, Muscles, Ubiquitin Proteomics, Staining, Binding Assay

Journal: Journal of Sport and Health Science

Article Title: Weightlifting outperforms voluntary wheel running for improving adiposity and insulin sensitivity in obese mice

doi: 10.1016/j.jshs.2025.101100

Figure Lengend Snippet: Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and AS160 phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 S318, and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.

Article Snippet: Primary antibodies used for analysis were from Cell Signaling Technologies (Danvers, MA, USA) and diluted 1:1000 unless otherwise stated as follows: protein kinase B (Akt; 1:500; #4691; Cell Signaling Technologies), phospho-Akt (pAkt) S473 (1:500; #9271; Cell Signaling Technologies), Ubiquitin (#3933; Cell Signaling Technologies), microtubule-associated protein light chain 3 (LC3 II/I; #4018; Cell Signaling Technologies), cytochrome c oxidase subunit 4(COX4; #11967; Cell Signaling Technologies), Akt substrate 160 (AS160 S318; #8619; Cell Signaling Technologies), AS160 T642 (#8881; Cell Signaling Technologies), eukaryotic translation initiation factor 4E binding protein (4E-BP1; #9452; Cell Signaling Technologies), and glyceraldehyde 3 phosphate dehydrogenase (GAPDH; #2118; Cell Signaling Technologies).

Techniques: Phospho-proteomics, Injection, Western Blot, Muscles, Ubiquitin Proteomics, Staining, Binding Assay

Journal: Bioactive Materials

Article Title: Immunomodulatory effects of biodegradable Mg–Cu–Zn alloy in esophageal cancer

doi: 10.1016/j.bioactmat.2026.02.046

Figure Lengend Snippet: Pure Mg, Mg–Cu, and Mg–Cu–Zn alloys inhibit tumor cell proliferation in immunocompetent C57BL/6 mice. (a) Representative H&E-stained tumor images showing necrosis and Ki-67 IHC staining in serial sections. Red dashed boxes indicate necrotic areas. (b) Quantification of tumor necrosis rates across groups. (c) Comparison of Ki-67 labeling index between perinecrotic and non-perinecrotic tumor cells. (d, e) Statistical analysis of Ki-67 labeling index in perinecrotic and non-perinecrotic regions across groups. (f) Representative IHC images of Ki-67 expression in viable tumor cells from perinecrotic and non-perinecrotic regions. Scale bar: 200 μm. p < 0.05 (∗), p < 0.001 (∗∗∗).

Article Snippet: Tissue sections were then incubated with primary antibodies against iNOS (22226-1-AP, ProteinTech, China), CD163 (A26411PM, Abclone, China), CD8 (SP16, Maixin, China), CD4 (SP35, Maixin, China) or Ki-67 (12202S, Cell Signaling Technology) for 12 h at 4 °C, followed by secondary antibodies (Beyotime Biotechnology, Nantong, China).

Techniques: Staining, Immunohistochemistry, Comparison, Labeling, Expressing

Journal: Bioactive Materials

Article Title: MSC-mimicking nanovesicle embedded bio-adhesive hydrogel for dual immunomodulation and osteogenesis to promote maxillofacial bone regeneration

doi: 10.1016/j.bioactmat.2026.02.032

Figure Lengend Snippet: In vivo evaluation of bone regeneration after hydrogel implantation in the mandibular bone defect mouse model. a) Schematic illustration of the mandibular bone defect mouse model. b) Micro-CT 3D reconstruction images of the mandibular bone samples at 4 and 8 weeks post-surgery. Scale bar = 1 mm. c) Semi-quantitative analysis of BV/TV, bone surface, Tb.N and Tb.sp (n = 6) in mouse mandibular bone defects implanted with different hydrogels at 8 weeks post-surgery. d) H&E staining and Masson trichrome staining of tissue sections of mandibular defects at 8 weeks post-surgery. Scale bar = 100 μm. e, f) Immunofluorescent staining images and corresponding semi-quantitative analysis of the expression levels of RUNX2 and OCN in mandibular bone defect areas at 4 and 8 weeks post-surgery (n = 3). Scale bar = 50 μm. P-values are calculated using one-way ANOVA with Tukey's test, ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, n.s. not significant ( a was created with bioRender. com).

Article Snippet: After blocking with 5% skimmed milk (diluted with TBST), the membranes were probed with the primary antibodies for CD90 (1:1000, Cat. ab92574, Abcam, UK), CD146 (1:1000, Cat. ab75769, Abcam, London, UK), CD105 (1:500, Cat. sc18838, Santa, USA), CXCR4 (1:250, Cat. 35-8800, Invitrogen, CA, USA), Na + /K + ATPase (1:1000, Cat. sc28800, Santa, USA), BMP2 (1:1000, Cat. ab284387, Abcam, UK), RUNX2 (1:1000, Cat. 12556, Cell Signaling Technology, USA) and β -actin (1:10000, Cat. T0022, Affinity, China) overnight at 4 °C, followed by bathing with horseradish peroxidase (HRP) conjugated secondary antibodies (1:5000, Cat. S0002 or Cat. S0001, Affinity, China).

Techniques: In Vivo, Micro-CT, Staining, Expressing

Journal: Bioactive Materials

Article Title: MSC-mimicking nanovesicle embedded bio-adhesive hydrogel for dual immunomodulation and osteogenesis to promote maxillofacial bone regeneration

doi: 10.1016/j.bioactmat.2026.02.032

Figure Lengend Snippet: The PEG-pp@nMSC@MT hydrogel effectively promotes BMMSCs' osteogenesis in vitro . a) Schematic illustration of co-culture BMMSCs with hydrogels. b) ALP staining of BMMSCs co-cultured with different scaffolds after 7 days. Scale bar = 500 μm. c) Semi-quantitative analysis of ALP staining (n = 3). d) ARS staining of BMMSC co-cultured with different scaffolds after 21 days. Scale bar = 500 μm. e) Semi-quantitative analysis of ARS staining (n = 3). f) mRNA expression of osteogenic genes (BMP2, OCN, and RUNX2) of BMMSCs treated with different hydrogels in the MMP condition after 5 and 10 days (n = 3). g) Western blot analysis of osteogenic protein (BMP2 and RUNX2) of BMMSCs treated with different hydrogels in the MMP condition after 7 and 14 days. P-values are calculated using one-way ANOVA with Tukey's test, ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, n.s. not significant ( a was created with bioRender. com).

Article Snippet: After blocking with 5% skimmed milk (diluted with TBST), the membranes were probed with the primary antibodies for CD90 (1:1000, Cat. ab92574, Abcam, UK), CD146 (1:1000, Cat. ab75769, Abcam, London, UK), CD105 (1:500, Cat. sc18838, Santa, USA), CXCR4 (1:250, Cat. 35-8800, Invitrogen, CA, USA), Na + /K + ATPase (1:1000, Cat. sc28800, Santa, USA), BMP2 (1:1000, Cat. ab284387, Abcam, UK), RUNX2 (1:1000, Cat. 12556, Cell Signaling Technology, USA) and β -actin (1:10000, Cat. T0022, Affinity, China) overnight at 4 °C, followed by bathing with horseradish peroxidase (HRP) conjugated secondary antibodies (1:5000, Cat. S0002 or Cat. S0001, Affinity, China).

Techniques: In Vitro, Co-Culture Assay, Staining, Cell Culture, Expressing, Western Blot

Journal: Bioactive Materials

Article Title: ADGRG1-targeted hypoxia preconditioned extracellular vesicles ameliorate intervertebral disc degeneration by delivering taurine to disrupt the oxidative stress feedback loop-driven ferroptosis in nucleus pulposus cells

doi: 10.1016/j.bioactmat.2026.02.029

Figure Lengend Snippet: Taurine activates the AMPK/NRF2 pathway by promoting the formation of the LKB1-STRAD-MO25 kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.

Article Snippet: The primary antibodies included LKB1 (sc-32245, Santa Cruz Biotechnology), MO25 (2716S, Cell Signaling Technology), and STRAD (sc-515635, Santa Cruz Biotechnology).

Techniques: Binding Assay, Liquid Chromatography with Mass Spectroscopy, Purification, SPR Assay, Mutagenesis, Immunoprecipitation, Two Tailed Test, Comparison