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APS influences MAPK signaling pathways in ATO-induced BMSCs. Cells were exposed to 0.5 μmol/L ATO, and 0.5 μmol/L ATO + APS (20, 40, 100, and 200 μg/mL) for 48 h. (A) Western blotting analysis was applied to detect protein expressions of p-Jnk and Jnk, β -actin was used as a loading control, n = 3. (B) Western blotting analysis was conducted to detect protein expressions of <t>p-p38</t> and p38, Gap was served as a loading control, n = 3. (C) Western blotting analysis was applied to detect protein expressions of p-Erk and Erk, β -actin was used as a loading control, n = 3. A two-tailed Student’s t -test was used to compare differences between two experimental groups. Error bars represent mean ± SEM. * P < 0.05, ** P < 0.01 vs control group, # P < 0.05 vs ATO group.
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APS influences MAPK signaling pathways in ATO-induced BMSCs. Cells were exposed to 0.5 μmol/L ATO, and 0.5 μmol/L ATO + APS (20, 40, 100, and 200 μg/mL) for 48 h. (A) Western blotting analysis was applied to detect protein expressions of p-Jnk and Jnk, β -actin was used as a loading control, n = 3. (B) Western blotting analysis was conducted to detect protein expressions of p-p38 and p38, Gap was served as a loading control, n = 3. (C) Western blotting analysis was applied to detect protein expressions of p-Erk and Erk, β -actin was used as a loading control, n = 3. A two-tailed Student’s t -test was used to compare differences between two experimental groups. Error bars represent mean ± SEM. * P < 0.05, ** P < 0.01 vs control group, # P < 0.05 vs ATO group.

Journal: Chinese Herbal Medicines

Article Title: Astragalus polysaccharides inhibit arsenic trioxide-induced BMSCs damage through inhibition of Jnk and p38 signaling pathways

doi: 10.1016/j.chmed.2025.03.007

Figure Lengend Snippet: APS influences MAPK signaling pathways in ATO-induced BMSCs. Cells were exposed to 0.5 μmol/L ATO, and 0.5 μmol/L ATO + APS (20, 40, 100, and 200 μg/mL) for 48 h. (A) Western blotting analysis was applied to detect protein expressions of p-Jnk and Jnk, β -actin was used as a loading control, n = 3. (B) Western blotting analysis was conducted to detect protein expressions of p-p38 and p38, Gap was served as a loading control, n = 3. (C) Western blotting analysis was applied to detect protein expressions of p-Erk and Erk, β -actin was used as a loading control, n = 3. A two-tailed Student’s t -test was used to compare differences between two experimental groups. Error bars represent mean ± SEM. * P < 0.05, ** P < 0.01 vs control group, # P < 0.05 vs ATO group.

Article Snippet: The membranes were then incubated with primary antibodies against B-cell lymphoma 2 (Bcl-2) (1:1 000, Proteintech, Chicago, USA, Cat. No. 68103-1-lg), Bcl-2-associated X protein (Bax) (1:1 000, Proteintech, Chicago, USA, Cat. No. 50599-2-lg), Caspase-3 (1:1 000, Proteintech, Chicago, USA, Cat. No. 19677-1-AP), cleaved Caspase-3 (1:2 000, Proteintech, Chicago, USA, Cat. No. 68773-1-lg), protein kinase B (Akt) (1:1 000, Cell signaling, Boston, USA, Cat. No. 9272) and phosphorylated-Akt (1:1 000, Cell signaling, Boston, USA, Cat. No. 4060), p53 (1:500, Gene Tex, California, USA, Cat. No. GTX70214), p16 (1:1 000, Proteintech, Chicago, USA, Cat. No.10883-1-AP), p38 mitogen-activated protein kinase (MAPK) (1:1 000, Proteintech, Chicago, USA, Cat. No.14064-1-AP), phosphorylated-p38 MAPK (1:1 000, Proteintech, Chicago, USA, Cat. No. 28796-1-AP), extracellular signal-regulated kinase (Erk) (1:2 000, Abcam, Cambridge, UK, Cat. No. ab184699), phosphorylated-Erk (1:2 000, Abcam, Cambridge, UK, Cat. No. ab201015), c-Jun N -terminal kinase (Jnk) (1:1 000, Proteintech, Chicago, USA, Cat. No.66210-1-lG), phosphorylated-Jnk (1:2 000, Abcam, Cambridge, UK, Cat. No. ab278538), GTPase-activating protein (Gap) (1:1 000, Abcam, Cambridge, UK, Cat. No. ab8245), and β -actin (1:1 000, Abcam, Cambridge, UK, Cat. No. ab8226) at 4 °C overnight.

Techniques: Protein-Protein interactions, Western Blot, Control, Two Tailed Test