Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: p-PI3K Rabbit Ab , Abmart , P76365R4 , 1: 1500.

Techniques: Expressing

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: p-PI3K Rabbit Ab , Abmart , P76365R4 , 1: 1500.

Techniques: Activity Assay

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: Membranes were blocked with 5 % BSA at 37°C for 2 h and incubated overnight at 4°C with the following primary antibodies: ITGAV Rabbit Ab, PLC Rabbit Ab, p-PLC Rabbit Ab, p-p65 Rabbit Ab, and Bcl2 Rabbit Ab were purchased from Bioss (Beijing, China); FAK Rabbit Ab, p-FAK Rabbit Ab, ERK Rabbit Ab, p-ERK Rabbit Ab, JNK Rabbit Ab, p-JNK Rabbit Ab, p38 MAPK Rabbit Ab, p-p38 MAPK Rabbit Ab, PI3K Rabbit Ab, p-PI3K Rabbit Ab, AKT Rabbit Ab, p-AKT Rabbit Ab, PKC Rabbit Ab, p-PKC Rabbit Ab, Bax Rabbit Ab, and Caspase 3 Rabbit Ab were purchased from Abmart (Shanghai, China); p65 Rabbit Ab (Proteintech, Wuhan, China).

Techniques: Expressing

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: Membranes were blocked with 5 % BSA at 37°C for 2 h and incubated overnight at 4°C with the following primary antibodies: ITGAV Rabbit Ab, PLC Rabbit Ab, p-PLC Rabbit Ab, p-p65 Rabbit Ab, and Bcl2 Rabbit Ab were purchased from Bioss (Beijing, China); FAK Rabbit Ab, p-FAK Rabbit Ab, ERK Rabbit Ab, p-ERK Rabbit Ab, JNK Rabbit Ab, p-JNK Rabbit Ab, p38 MAPK Rabbit Ab, p-p38 MAPK Rabbit Ab, PI3K Rabbit Ab, p-PI3K Rabbit Ab, AKT Rabbit Ab, p-AKT Rabbit Ab, PKC Rabbit Ab, p-PKC Rabbit Ab, Bax Rabbit Ab, and Caspase 3 Rabbit Ab were purchased from Abmart (Shanghai, China); p65 Rabbit Ab (Proteintech, Wuhan, China).

Techniques: Activity Assay

Journal: Journal of Ovarian Research

Article Title: Gut microbiota-derived Tryptophanol driven by N-Carbamylglutamate alleviates premature ovarian failure through inhibiting oxidative stress

doi: 10.1186/s13048-026-02152-4

Figure Lengend Snippet: Tryptophanol treatment alleviated POF symptoms by inhibiting PI3K/AKT and MAPK pathways. A Experimental scheme. B Estrus status of mice ( n = 8). C Body weights of mice ( n = 8). D Ovary weights of mice ( n = 8). E Representative Ovary from the Control, the POF and the NCG groups mice with H&E and IHC staining. H&E scale bar = 200 μm; IHC scale bar = 100 μm. F Quantification of primordial, primary, secondary, antral follicles, corpora lutea and corpora atretica per ovary. n = 3 ovaries per each condition. Levels of FSH ( G ), LH ( H ), E 2 ( I ) in mouse serum ( n = 6). Levels of ROS ( J ), MDA ( K ), SOD ( L ), GSH-Px ( M ) in mouse ovaries ( n = 3–4). N Western blotting ( a ) and quantitative ( b ) analysis of proteins ( n = 3). O Litter sizes of mice ( n = 3). Data presented as the mean ± SD, statistical significance was determined using one-way or two-way ANOVA. * p < 0.05, ** p < 0.01. *** p < 0.001. Different lowercase letters indicate significant differences ( p < 0.05)

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA; Sigma) for 1 h at room temperature, followed by overnight incubation at 4 °C with the primary antibodies: rabbit Cleaved caspase 3 (MCE, HY- P80623 , 1:800), rabbit BAX (Bioworld, BS61098, 1:800), rabbit BCL2 (Bioworld, BS1511, 1:800), rabbit ERK1/2 (Bioworld, BS90472, 1:1,000), rabbit p-ERK1/2 (Bioworld, BS4621P, 1:1,000), rabbit p38 (Bioworld, BS4635, 1:1,000), rabbit p-p38 (Bioworld, BS4766, 1:1,000), rabbit PI3K (MCE, HY- P80867 , 1:1,000); rabbit p-PI3K (MCE, HY- P80846 , 1:1,000), rabbit AKT (Bioworld, MB3288 1:1,000); rabbit p-AKT (Bioworld, BS4007 1:1,000); rabbit IL-6 (Abclonal, A0286, 1:800), rabbit IL-1β (MCE, HY- P80720 , 1:1,000), rabbit Occludin (Abclonal, A2601, 1:1,000); rabbit ZO-1 (Bioworld, BS71522, 1:1,000); rabbit GPX4 (MCE, HY- P80450 , 1:1,000); mouse GAPDH (Bioworld, MB001, 1:1,000); rabbit SOD2 (Bioworld, BS6734, 1:1,000).

Techniques: Control, Immunohistochemistry, Western Blot

Journal: Journal of Ovarian Research

Article Title: Gut microbiota-derived Tryptophanol driven by N-Carbamylglutamate alleviates premature ovarian failure through inhibiting oxidative stress

doi: 10.1186/s13048-026-02152-4

Figure Lengend Snippet: Tryptophanol treatment alleviated POF by inhibiting PI3K/AKT and MAPK pathways in vitro . A Experimental scheme. B Different concentrations of Cy on GCs viability was assessed by CCK8 assay. C and E Different concentrations of Trp on GCs viability was assessed by CCK8 assay. D The effect of Trp on GCs cell viability following Cy treatment. The control and treatment groups were stained with DCFH-DA, the cells were washed and examined by fluorescence microscopy. Scale bar = 50 μm. F The fluorescence intensity of ROS in mouse GCs. G The level of MDA in mouse GCs. H Flow cytometry apoptosis analysis graph and cell death rate in different groups. The level of SOD ( I ), GSH-Px ( J ), and E 2 ( K ) in mouse GCs. ( L ) Western blotting ( a ) and quantitative ( b ) analysis of proteins ( n = 3). All values are presented as the mean ± SD ( n = 3). Different lowercase letters indicate significant differences compared to the control group ( p < 0.05)

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA; Sigma) for 1 h at room temperature, followed by overnight incubation at 4 °C with the primary antibodies: rabbit Cleaved caspase 3 (MCE, HY- P80623 , 1:800), rabbit BAX (Bioworld, BS61098, 1:800), rabbit BCL2 (Bioworld, BS1511, 1:800), rabbit ERK1/2 (Bioworld, BS90472, 1:1,000), rabbit p-ERK1/2 (Bioworld, BS4621P, 1:1,000), rabbit p38 (Bioworld, BS4635, 1:1,000), rabbit p-p38 (Bioworld, BS4766, 1:1,000), rabbit PI3K (MCE, HY- P80867 , 1:1,000); rabbit p-PI3K (MCE, HY- P80846 , 1:1,000), rabbit AKT (Bioworld, MB3288 1:1,000); rabbit p-AKT (Bioworld, BS4007 1:1,000); rabbit IL-6 (Abclonal, A0286, 1:800), rabbit IL-1β (MCE, HY- P80720 , 1:1,000), rabbit Occludin (Abclonal, A2601, 1:1,000); rabbit ZO-1 (Bioworld, BS71522, 1:1,000); rabbit GPX4 (MCE, HY- P80450 , 1:1,000); mouse GAPDH (Bioworld, MB001, 1:1,000); rabbit SOD2 (Bioworld, BS6734, 1:1,000).

Techniques: In Vitro, CCK-8 Assay, Control, Staining, Fluorescence, Microscopy, Flow Cytometry, Western Blot

Journal: Poultry Science

Article Title: PKA and PKC signaling pathways mediate vitamin D₃-regulated intestinal phosphorus absorption in broiler chickens

doi: 10.1016/j.psj.2026.106762

Figure Lengend Snippet: Effects of dietary vitamin D 3 supplementation on jejunal phosphorylation levels of PKA, PKC, PI3K, p38MAPK, and ERK in broiler chickens (19 d) (Experiment 1). The control and vitamin D 3 diets contained 0 and 1000 IU/kg vitamin D 3 , respectively. (a) p-PKA/t-PKA; (b) p-PKC/t-PKC; (c) p-PI3K/t-PI3K; (d) p-p38MAPK/t-p38MAPK; (e) p-ERK/t-ERK. Protein abundance values are means ± SD of four replicates per treatment (1 broiler per replicate) (n = 4). Values with different letters differ between treatments ( P < 0.05).

Article Snippet: PVDF membranes were incubated with primary antibodies against NaPi-IIb (1:1000, A9460; ABclonal, Wuhan, China), phosphorylated PKA (p-PKA; 1:1000, 5661S), phosphorylated PI3K (p-PI3K; 1:1000, 4228), phosphorylated ERK (p-ERK; 1:1000, 9101S), phosphorylated p38MAPK (p-p38MAPK; 1:1000, 9216S), total PKA (t-PKA; 1:1000, 5842S) (Cell Signaling Technology, Boston, USA), total PI3K (t-PI3K; 1:10000, 60225-1-Ig), total ERK (t-ERK; 1:8000, 11257-1-AP-50), total p38MAPK(t-p38MAPK; 1:1000, 14064-1-AP), total PKC (t-PKC; 1:1000, 21991-1-AP), phosphorylated PKC (p-PKC; 1:5000, 29123-1-AP), and GAPDH (1:10000, 60004-1-Ig) (Proteintech, Wuhan, China).

Techniques: Phospho-proteomics, Control, Quantitative Proteomics

Journal: Poultry Science

Article Title: PKA and PKC signaling pathways mediate vitamin D₃-regulated intestinal phosphorus absorption in broiler chickens

doi: 10.1016/j.psj.2026.106762

Figure Lengend Snippet: Effects of the PKA inhibitor H-89 on jejunal phosphorylation levels of PKC, PI3K, p38MAPK, and ERK in broiler chickens (10–15 d) (Experiment 2). (a) p-PKC/t-PKC; (b) p-PI3K/t-PI3K; (c) p-p38MAPK/t-p38MAPK; (d) p-ERK/t-ERK. Protein abundance values are means ± SD of four replicates per treatment (1 broiler per replicate) (n = 4). Values with different letters differ between treatments ( P < 0.05).

Article Snippet: PVDF membranes were incubated with primary antibodies against NaPi-IIb (1:1000, A9460; ABclonal, Wuhan, China), phosphorylated PKA (p-PKA; 1:1000, 5661S), phosphorylated PI3K (p-PI3K; 1:1000, 4228), phosphorylated ERK (p-ERK; 1:1000, 9101S), phosphorylated p38MAPK (p-p38MAPK; 1:1000, 9216S), total PKA (t-PKA; 1:1000, 5842S) (Cell Signaling Technology, Boston, USA), total PI3K (t-PI3K; 1:10000, 60225-1-Ig), total ERK (t-ERK; 1:8000, 11257-1-AP-50), total p38MAPK(t-p38MAPK; 1:1000, 14064-1-AP), total PKC (t-PKC; 1:1000, 21991-1-AP), phosphorylated PKC (p-PKC; 1:5000, 29123-1-AP), and GAPDH (1:10000, 60004-1-Ig) (Proteintech, Wuhan, China).

Techniques: Phospho-proteomics, Quantitative Proteomics

Journal: Poultry Science

Article Title: PKA and PKC signaling pathways mediate vitamin D₃-regulated intestinal phosphorus absorption in broiler chickens

doi: 10.1016/j.psj.2026.106762

Figure Lengend Snippet: Effects of the PKC inhibitor staurosporine on duodenal phosphorylation levels of PKA, PI3K, p38MAPK, and ERK in broiler chickens (13 d) (Experiment 3). (a) p-PKA/t-PKA; (b) p-PI3K/t-PI3K; (c) p-p38MAPK/t-p38MAPK; (d) p-ERK/t-ERK. Protein abundance values are means ± SD of four replicates per treatment (1 broiler per replicate) (n = 4). Values with different letters differ between treatments ( P < 0.05).

Article Snippet: PVDF membranes were incubated with primary antibodies against NaPi-IIb (1:1000, A9460; ABclonal, Wuhan, China), phosphorylated PKA (p-PKA; 1:1000, 5661S), phosphorylated PI3K (p-PI3K; 1:1000, 4228), phosphorylated ERK (p-ERK; 1:1000, 9101S), phosphorylated p38MAPK (p-p38MAPK; 1:1000, 9216S), total PKA (t-PKA; 1:1000, 5842S) (Cell Signaling Technology, Boston, USA), total PI3K (t-PI3K; 1:10000, 60225-1-Ig), total ERK (t-ERK; 1:8000, 11257-1-AP-50), total p38MAPK(t-p38MAPK; 1:1000, 14064-1-AP), total PKC (t-PKC; 1:1000, 21991-1-AP), phosphorylated PKC (p-PKC; 1:5000, 29123-1-AP), and GAPDH (1:10000, 60004-1-Ig) (Proteintech, Wuhan, China).

Techniques: Phospho-proteomics, Quantitative Proteomics

Journal: Bioactive Materials

Article Title: Integrated cryopreservation-thawing-transplantation platform for neural stem cell-based spinal cord injury repair

doi: 10.1016/j.bioactmat.2026.01.024

Figure Lengend Snippet: Mechanisms of NSC Differentiation into Neurons Promoted by Composite In Vitro. A) Schematic of the interactive system with NSCs and the composites. B) Representative confocal images of NSCs treated with distinct groups for 72 h. NSCs were stained with Tuj-1 (red), GFAP (green), and DAPI (blue). Scale bar: 50 μm. C-D) Quantitative analysis of Tuj-1 (C) and GFAP (D) fluorescence intensity in each group (n = 4). E) Western blot bands of Tuj-1 and GFAP protein expression in NSCs treated with separate groups. F-G) Quantitative analysis of Tuj-1/GAPDH (F) and GFAP/GAPDH (G) ratios in each group (n = 3). H) Volcano plots of DEGs in the hUCMSC-Exo + PM vs. control. DEGs are defined as |log2FC| ≥ 1 with q < 0.05. I-J) GO and KEGG pathway enrichment analysis of DEGs in NSCs after intervention with hUCMSC-Exo + PM. K) Heatmap showing the expression levels of significantly altered genes in the hUCMSC-Exo + PM and Control. L) GSEA showing pathways significantly positively correlated with DEGs in the hUCMSC-Exo + PM group. Enrichment scores (ES), P values, and false discovery rates (FDR) values are indicated for each pathway. M) Western blot bands of p-CaMK II, CaMK II, p-CREB, CREB, p-PI3K, PI3K, p-AKT, and AKT protein expression in NSCs treated with distinct groups. N) Quantitative analysis of p-CaMK II/CaMK II, p-CREB/CREB, p-PI3K/PI3K, and p-AKT/AKT ratios (n = 3). All data are presented as the mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001.

Article Snippet: The primary antibodies used in this research are listed below: CD68 (Abcam, Cambridge, UK), CD206 (Abcam, Cambridge, UK), GFAP (Bioss, Beijing, China), iNOS (Abcam, Cambridge, UK), Tuj-1 (Abcam, Cambridge, UK), NF-200 (Invitrogen, CA, USA), MBP (Abcam, Cambridge, UK), HIF-1α (Abcam, Cambridge, UK), VEGFA (Abcam, Cambridge, UK), P-CaMKII (Abcam, Cambridge, UK), CaMKII (Abcam, Cambridge, UK), P-CREB (Cell Signaling Technology, USA), CREB (Cell Signaling Technology, USA), P-PI3K (Cell Signaling Technology, USA), PI3K (Cell Signaling Technology, USA), P-AKT (Cell Signaling Technology, USA), AKT (Cell Signaling Technology, USA), Cleaved-Caspase3 (Cell Signaling Technology, USA), Bcl-2 (Cell Signaling Technology, USA), Bax (Cell Signaling Technology, USA), GAPDH (Proteintech, IL, USA).

Techniques: In Vitro, Staining, Fluorescence, Western Blot, Expressing, Control

Journal: Frontiers in Pharmacology

Article Title: Bruceine D attenuates prostate cancer growth and motility by suppressing PI3K/AKT signaling and downregulating CXCL16: implications for skeletal metastasis in orthopedic oncology

doi: 10.3389/fphar.2026.1819854

Figure Lengend Snippet: BD inhibits migration and motility of prostate cancer cells. (A–D) Distribution of prostate cancer cell lines (PC-3 and C4-2b) after passage through the chamber following 24-h treatment with varying doses of BD. (E,F) Wound-healing analysis of PC-3 and C4-2B cells 24 h after BD treatment, performed by the scratch assay. (G-L) Western blot analysis of P-PI3K and P-AKT expression in PC-3 and C4-2b cells after 24-h BD treatment. Data are presented as mean ± standard deviation from three independent experiments. One-way ANOVA was used to compare each group with the control. * p < 0.05, ** p < 0.01, and *** p < 0.001 denote statistical significance.

Article Snippet: The membranes were blocked with 5% non-fat milk in TBST, followed by overnight incubation at 4 °C with primary antibodies at manufacturer-recommended dilutions: PI3K (AF5112, Affinity Biosciences), phospho-PI3K (AF6241, Affinity Biosciences), AKT (AF6261, Affinity Biosciences), phospho-AKT (AF3263, Affinity Biosciences), PCNA (10205-2-AP, Proteintech), MMP9 (10375-2-AP, Proteintech), CXCL16 (60123-1-Ig, Proteintech), BAX (AF0120, Affinity Biosciences), BCL2 (AF6139, Affinity Biosciences), GAPDH (AF7021, Affinity Biosciences), and Tubulin (AF7011, Affinity Biosciences).

Techniques: Migration, Wound Healing Assay, Western Blot, Expressing, Standard Deviation, Control

Journal: Frontiers in Pharmacology

Article Title: Bruceine D attenuates prostate cancer growth and motility by suppressing PI3K/AKT signaling and downregulating CXCL16: implications for skeletal metastasis in orthopedic oncology

doi: 10.3389/fphar.2026.1819854

Figure Lengend Snippet: Effects of BD on the PI3K/AKT pathway and the CXCL16 chemokine. (A,B,D) Bar plots, volcano plots, and heatmaps depict differentially expressed genes in PC-3 cells treated with BD for 24 h (n = 3). (C) GSEA enrichment plot for the PI3K/AKT pathway gene set. (E) GO enrichment analysis of biological processes (BP), cellular components (CC), and molecular functions (MF). (F,G) Molecular docking models of ligand BD with the protein receptors PIK3AP1, PIK3C2B, PIK3CB, PIK3R2, AKT1, and CXCL16.Statistical significance was determined by one-way analysis of variance and is indicated as * p < 0.05, ** p < 0.01, and *** p < 0.001 versus the control.

Article Snippet: The membranes were blocked with 5% non-fat milk in TBST, followed by overnight incubation at 4 °C with primary antibodies at manufacturer-recommended dilutions: PI3K (AF5112, Affinity Biosciences), phospho-PI3K (AF6241, Affinity Biosciences), AKT (AF6261, Affinity Biosciences), phospho-AKT (AF3263, Affinity Biosciences), PCNA (10205-2-AP, Proteintech), MMP9 (10375-2-AP, Proteintech), CXCL16 (60123-1-Ig, Proteintech), BAX (AF0120, Affinity Biosciences), BCL2 (AF6139, Affinity Biosciences), GAPDH (AF7021, Affinity Biosciences), and Tubulin (AF7011, Affinity Biosciences).

Techniques: Control

Journal: Frontiers in Pharmacology

Article Title: Bruceine D attenuates prostate cancer growth and motility by suppressing PI3K/AKT signaling and downregulating CXCL16: implications for skeletal metastasis in orthopedic oncology

doi: 10.3389/fphar.2026.1819854

Figure Lengend Snippet: BD suppresses PI3K/AKT, CXCL16, and MMP9.

Article Snippet: The membranes were blocked with 5% non-fat milk in TBST, followed by overnight incubation at 4 °C with primary antibodies at manufacturer-recommended dilutions: PI3K (AF5112, Affinity Biosciences), phospho-PI3K (AF6241, Affinity Biosciences), AKT (AF6261, Affinity Biosciences), phospho-AKT (AF3263, Affinity Biosciences), PCNA (10205-2-AP, Proteintech), MMP9 (10375-2-AP, Proteintech), CXCL16 (60123-1-Ig, Proteintech), BAX (AF0120, Affinity Biosciences), BCL2 (AF6139, Affinity Biosciences), GAPDH (AF7021, Affinity Biosciences), and Tubulin (AF7011, Affinity Biosciences).

Techniques: