Journal: Translational Oncology

Article Title: Zeaxanthin targets TOP2A to regulate autophagy and suppress lung cancer progression via the MAPK/ERK pathway

doi: 10.1016/j.tranon.2025.102658

Figure Lengend Snippet: Zea modulates MAPK/ERK signaling to inhibit LC progression. A: Analysis of gene expression differences pre- and post-Zea treatment; B: Heat map analysis of TOP 50 DEGs; C: GO functional enrichment of differentially expressed genes; D: KEGG pathway enrichment of differentially expressed genes; E: WB analysis of MAPK/ERK pathway proteins. A549 cells: NC, Zea, Zea + Ro 67–7476. F: Cell viability measured by CCK-8; G: Cell proliferation assessed by colony formation; H: Cell migration analyzed by Transwell; I: Cell apoptosis detected by flow cytometry; J: WB of autophagy-related proteins; K: IF analysis of autophagosomes and lysosomes, with LC3 for autophagosomes and LAMP1 for lysosomes. ** P < 0.01, *** P < 0.001. The data is presented as mean ± standard deviation, and inter-group comparisons are conducted using ANOVA and Tukey’s post hoc test.

Article Snippet: We also wondered whether the impact of Zea on LC cells was associated with the MAPK/ERK signaling, so we treated A549 cells with Zea and subsequently added MAPK/ERK pathway activator Ro 67–7476 (MCE, USA) to activate this pathway.

Techniques: Gene Expression, Functional Assay, CCK-8 Assay, Migration, Flow Cytometry, Standard Deviation

Journal: Translational Oncology

Article Title: Zeaxanthin targets TOP2A to regulate autophagy and suppress lung cancer progression via the MAPK/ERK pathway

doi: 10.1016/j.tranon.2025.102658

Figure Lengend Snippet: Zea targets TOP2A to enhance autophagy via the MAPK/ERK pathway and impedes LC progression. A549 cells: oe-NC, oe-TOP2A, A: TOP2A mRNA level detected by qRT-PCR A549 cells: oe-NC, oe-TOP2A, oe-NC + Zea, oe-TOP2A + Zea. B: WB analysis of TOP2A, MAPK/ERK pathway proteins (p-ERK1/2, ERK1/2, p-MEK, MEK), and autophagy-related proteins (LC3-I, LC3-II, Beclin 1); C: IF detection of autophagosome and lysosome formation; D: CCK-8 assay of cell viability; E: Colony formation assay of cell proliferation; F: Transwell assay of cell migration; G: Flow cytometry analysis of cell apoptosis. ** P < 0.01, *** P < 0.001. The data is presented as mean ± standard deviation, and inter-group comparisons are conducted using ANOVA and Tukey’s post hoc test.

Article Snippet: We also wondered whether the impact of Zea on LC cells was associated with the MAPK/ERK signaling, so we treated A549 cells with Zea and subsequently added MAPK/ERK pathway activator Ro 67–7476 (MCE, USA) to activate this pathway.

Techniques: Quantitative RT-PCR, CCK-8 Assay, Colony Assay, Transwell Assay, Migration, Flow Cytometry, Standard Deviation

Journal: Translational Oncology

Article Title: Zeaxanthin targets TOP2A to regulate autophagy and suppress lung cancer progression via the MAPK/ERK pathway

doi: 10.1016/j.tranon.2025.102658

Figure Lengend Snippet: In vivo evidence that Zea targets TOP2A to influence the MAPK/ERK pathway and autophagy to mitigate LC progression. Animal groups: oe-NC, oe-TOP2A, oe-NC + Zea, oe-TOP2A + Zea. A: Tumor images from the mouse model; B: Weight of mouse tumor tissues; C: Volume of mouse tumor tissues; D: HE staining images of mouse tumor tissues; E: IHC detection of TOP2A and KI67 expression levels in tumor tissues; F: WB analysis of MAPK/ERK pathway proteins (p-ERK1/2, ERK1/2, p-MEK, MEK) and autophagy-related proteins (LC3-I, LC3-II, Beclin 1); G: IF detection of autophagosome and lysosome colocalization. *** P < 0.001. The data is presented as mean ± standard deviation, and inter-group comparisons are conducted using ANOVA and Tukey’s post hoc test.

Article Snippet: We also wondered whether the impact of Zea on LC cells was associated with the MAPK/ERK signaling, so we treated A549 cells with Zea and subsequently added MAPK/ERK pathway activator Ro 67–7476 (MCE, USA) to activate this pathway.

Techniques: In Vivo, Staining, Expressing, Standard Deviation

Journal: Scientific Reports

Article Title: PTPRK promotes resiniferatoxin-induced postherpetic neuralgia via activating DUSP1/p38 MAPK signaling pathway in dorsal root ganglia

doi: 10.1038/s41598-025-24233-y

Figure Lengend Snippet: PTPRK activated the DUSP1/p38 MAPK signaling pathway in PHN. A , Western blot was performed to analyze the protein levels of DUSP1, p-p38 MAPK, and p38 MAPK in DRG tissues of each group; B , The protein levels of PTPRK, DUSP1, p-p38 MAPK, and p38 MAPK in Lv-NC and Lv-PTPRK groups were detected via Western blot. ( N = 5).

Article Snippet: Conversely, to activate the p38 MAPK pathway, rats were injected with anisomycin (2.5 mg/kg; HY-18982; purity: 99.82%; MedChem Express), a known inducer of p38 phosphorylation , once daily for 7 days.

Techniques: Western Blot

Journal: Scientific Reports

Article Title: PTPRK promotes resiniferatoxin-induced postherpetic neuralgia via activating DUSP1/p38 MAPK signaling pathway in dorsal root ganglia

doi: 10.1038/s41598-025-24233-y

Figure Lengend Snippet: p38 MAPK signaling pathway activation promoted mechanical allodynia and inflammation in rat DRG tissues. A , Paw withdrawal thresholds and B , paw withdrawal latency in each group were quantified; ELISA was performed to assess the concentrations of C , TNF-α, D , IL-1β, and E , IL-4 in DRG tissues of each group; RT-qPCR was performed to analyze the mRNA levels of F , TNF-α, G , IL-1β, H , IL-4, I , BDNF, J , Nav1.3, K , Nav1.7, and L , TRPV1 in DRG tissues of each group. ( N = 5; ** p < 0.01 vs. the RTX-PHN + Lv-shNC group; # p < 0.05, ## p < 0.01 vs. the RTX-PHN + Lv-shPTPRK group).

Article Snippet: Conversely, to activate the p38 MAPK pathway, rats were injected with anisomycin (2.5 mg/kg; HY-18982; purity: 99.82%; MedChem Express), a known inducer of p38 phosphorylation , once daily for 7 days.

Techniques: Activation Assay, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR

Journal: Scientific Reports

Article Title: PTPRK promotes resiniferatoxin-induced postherpetic neuralgia via activating DUSP1/p38 MAPK signaling pathway in dorsal root ganglia

doi: 10.1038/s41598-025-24233-y

Figure Lengend Snippet: PTPRK overexpression promoted inflammation via activating DUSP1/p38 MAPK signaling pathway in rat DRG cells. A , PTPRK expression was analyzed by RT-qPCR after empty and PTPRK overexpression vectors transfection; B , The protein levels of PTPRK, DUSP1, p-p38 MAPK, and p38 MAPK in each group were detected though Western blot; ELISA was performed to assess the concentrations of C , TNF-α, D , IL-1β, and E , IL-4 in DRG cells of each group; RT-qPCR was performed to analyze the mRNA levels of F , TNF-α, G , IL-1β, H , IL-4, I , BDNF, J , Nav1.3, K , Nav1.7, and L , TRPV1 in DRG cells of each group. ( N = 3; ** p < 0.01 vs. the vector group; ## p < 0.01 vs. the PTPRK group).

Article Snippet: Conversely, to activate the p38 MAPK pathway, rats were injected with anisomycin (2.5 mg/kg; HY-18982; purity: 99.82%; MedChem Express), a known inducer of p38 phosphorylation , once daily for 7 days.

Techniques: Over Expression, Expressing, Quantitative RT-PCR, Transfection, Western Blot, Enzyme-linked Immunosorbent Assay, Plasmid Preparation