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CA induced breast cancer cell apoptosis via <t>p38</t> and JNK phosphorylation and regulated glucose metabolism. (A) T‐47D and MCF‐7 cells were treated with 25 μM and 20 μM CA for 6, 12, and 24 h, respectively. Cancer cell apoptosis was detected by flow cytometry using annexin V‐FITC/PI (B) Potential targets of CA. (C) Protein expression levels of p‐JNK, <t>p‐p38,</t> Bax, Bcl‐2, and PARP were measured by western blotting. Data presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.
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CA induced breast cancer cell apoptosis via <t>p38</t> and JNK phosphorylation and regulated glucose metabolism. (A) T‐47D and MCF‐7 cells were treated with 25 μM and 20 μM CA for 6, 12, and 24 h, respectively. Cancer cell apoptosis was detected by flow cytometry using annexin V‐FITC/PI (B) Potential targets of CA. (C) Protein expression levels of p‐JNK, <t>p‐p38,</t> Bax, Bcl‐2, and PARP were measured by western blotting. Data presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.
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CA induced breast cancer cell apoptosis via p38 and JNK phosphorylation and regulated glucose metabolism. (A) T‐47D and MCF‐7 cells were treated with 25 μM and 20 μM CA for 6, 12, and 24 h, respectively. Cancer cell apoptosis was detected by flow cytometry using annexin V‐FITC/PI (B) Potential targets of CA. (C) Protein expression levels of p‐JNK, p‐p38, Bax, Bcl‐2, and PARP were measured by western blotting. Data presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.

Journal: Cancer Medicine

Article Title: Carnosic Acid Mediates Production of Reactive Oxygen Species to Regulate Mitogen‐Activated Protein Kinase Pathway Phosphorylation and Induce Apoptosis in Human Breast Cancer Cells

doi: 10.1002/cam4.71446

Figure Lengend Snippet: CA induced breast cancer cell apoptosis via p38 and JNK phosphorylation and regulated glucose metabolism. (A) T‐47D and MCF‐7 cells were treated with 25 μM and 20 μM CA for 6, 12, and 24 h, respectively. Cancer cell apoptosis was detected by flow cytometry using annexin V‐FITC/PI (B) Potential targets of CA. (C) Protein expression levels of p‐JNK, p‐p38, Bax, Bcl‐2, and PARP were measured by western blotting. Data presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.

Article Snippet: The following antibodies were also used: rabbit monoclonal phospho (p)‐JNK, p‐p38 (Cell Signaling Technology, 9926 T), rabbit polyclonal β‐actin (Proteintech, 20,536–1‐AP), Bax (Proteintech, 50,599‐2‐Ig), Bcl‐2 (Proteintech, 12,789‐1‐AP), and poly‐ADP ribose polymerase (PARP, Cell Signaling Technology, 9542).

Techniques: Phospho-proteomics, Flow Cytometry, Expressing, Western Blot

SP600125 and BMS582949 were used to inhibit CA‐induced JNK and p38 phosphorylation. (A) T‐47D and (B) MCF‐7 cells were pre‐treated with SP600125 and BMS582949 for 2 h, followed by treatment with CA at 25 μM and 20 μM, respectively. Protein expression levels of p‐JNK, p‐p38, Bax, Bcl‐2, and PARP were measured by western blotting. (C) and (D) Relative cell viability was evaluated by MTT assays. Data are presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.

Journal: Cancer Medicine

Article Title: Carnosic Acid Mediates Production of Reactive Oxygen Species to Regulate Mitogen‐Activated Protein Kinase Pathway Phosphorylation and Induce Apoptosis in Human Breast Cancer Cells

doi: 10.1002/cam4.71446

Figure Lengend Snippet: SP600125 and BMS582949 were used to inhibit CA‐induced JNK and p38 phosphorylation. (A) T‐47D and (B) MCF‐7 cells were pre‐treated with SP600125 and BMS582949 for 2 h, followed by treatment with CA at 25 μM and 20 μM, respectively. Protein expression levels of p‐JNK, p‐p38, Bax, Bcl‐2, and PARP were measured by western blotting. (C) and (D) Relative cell viability was evaluated by MTT assays. Data are presented as mean ± SD of three independent experiments. * p < 0.05, ** p < 0.01 versus NC group.

Article Snippet: The following antibodies were also used: rabbit monoclonal phospho (p)‐JNK, p‐p38 (Cell Signaling Technology, 9926 T), rabbit polyclonal β‐actin (Proteintech, 20,536–1‐AP), Bax (Proteintech, 50,599‐2‐Ig), Bcl‐2 (Proteintech, 12,789‐1‐AP), and poly‐ADP ribose polymerase (PARP, Cell Signaling Technology, 9542).

Techniques: Phospho-proteomics, Expressing, Western Blot