Journal: Poultry Science

Article Title: Gut microbiota-derived taurolithocholic acid modulates myofiber-type switching via p38 MAPK/PGC-1α signaling underlying breed differences between Arbor Acres and Taoyuan chickens

doi: 10.1016/j.psj.2026.106914

Figure Lengend Snippet: TLCA regulates mitochondrial biogenesis and altered myofiber type composition through the p38 MAPK/PGC-1α signaling pathway. A Cell viability of cells treated with different concentrations of TLCA for 24 h (n = 10). B & F The mRNA expression of MYH1A and MYH7B (n = 6). C & G Intracellular enzymatic activities of succinate dehydrogenase (SDH) and lactate dehydrogenase (LDH), ATP content and mitochondrial DNA (mtDNA) content (n = 6). D & H The mRNA expression of HK1, GPI, PGAM1, PGK1, PYGL, PGC-1α, NRF1 and TFAM (n = 6). E The protein expression of PGC-1α, p38 MAPK and phosphorylation p38 MAPK (n = 3). I The protein expression of PGC-1α (n = 3). Data were shown as mean ± SD; *Represents significant difference when compared with 0 μM TLCA or CON group, and # represents significant difference when compared with TLCA group. *& # P < 0.05, ⁎⁎ & ## P < 0.01, ⁎⁎⁎ & ### P < 0.001.

Article Snippet: The differentiation medium containing TLCA and p38 MAPK inhibitor SB203580 (152121-47-6, MedChemExpress, Shanghai, China) was added to CPMs after 4 days of differentiation, and the cells were collected after 24 h.

Techniques: Expressing, Phospho-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 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: Precisely regulated physically-crosslinked carriers enable synergetic release of bioactive factors for MSC-mediated cartilage regeneration

doi: 10.1016/j.bioactmat.2026.01.009

Figure Lengend Snippet: Mechanisms of Cdh2 gene in chondrogenesis. (a) Relative expression of Cdh2 gene through qRT-PCR. HD: higher density; LD: lower density. (b, c) Western blotting results of N-cadherin and p38 MAPK in different groups. Cdh2 KD : Cdh2 knocked down group. (d) Immunofluorescent results of cell pellets after 3 days of co-culture. Blue: DAPI; Green: ActinGreen; Red: N-cadherin. Scale bar = 200 μm. (e, f) Relative expression of Cdh2 gene and chondrogenesis-related genes ( Sox9 , Col2a1 , Acan ) through qRT-PCR. (g) Immunofluorescent results of cell pellets after 14 days of co-culture. Blue: DAPI; Green: ActinGreen; Red: N-cadherin. Scale bar = 200 μm ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Article Snippet: After blocked with skimmed milk, the membranes were incubated with primary antibody at 4 °C (anti-N-cadherin (Abcam), anti-p38 MAPK (Proteintech)).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Co-Culture Assay

Journal: Journal of Translational Autoimmunity

Article Title: Exploring the immunomodulatory effects of environmental contaminants on autoimmune patients: An in vitro approach

doi: 10.1016/j.jtauto.2025.100341

Figure Lengend Snippet: Modulation of intracellular signaling pathways in HD, RA, and SLE cells exposed to environmental contaminants. Heatmap showing the relative expression and phosphorylation levels of key signaling proteins involved in immune regulation, inflammation, and cell survival (STAT1, STAT3, p38, AKT, and NFκB) and their phosphorylated forms in HD, RA, and SLE after exposure to PM, silica, and TCDD. Data are represented as z-score normalized values. Asterisks indicate statistically significant differences compared with the unstimulated control within each group (p < 0.05). AKT: protein kinase B; HD: healthy donors; NFκB: nuclear factor kappa-light-chain-enhancer of activated B cells; P: phosphorylated form; p38: p38 mitogen-activated protein kinase; PM: particulate matter; RA: rheumatoid arthritis; SLE: systemic lupus erythematosus; STAT: signal transducer and activator of transcription; TCDD: 2,3,7,8-tetrachlorodibenzo-p-dioxin.

Article Snippet: Membranes were stripped and re-probed for total AKT, NFκB p65, p38 MAPK, STAT1, STAT3, and β-actin (Cell Signaling Technology, Danvers, MA, USA; Santa Cruz Biotechnology, Dallas, TX, USA) as a loading control.

Techniques: Protein-Protein interactions, Expressing, Phospho-proteomics, Control