phosphorylated p38mapk  (Cell Signaling Technology Inc)

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: Anti-Cancer Drugs

Article Title: Hematopoietic progenitor kinase 1 inhibitor BGB-15025 induces apoptosis in acute myeloid leukemia cells through the cell cycle pathway and mitogen-activated protein kinase/extracellular signal-regulated kinase pathway signaling axis

doi: 10.1097/CAD.0000000000001794

Figure Lengend Snippet: BGB-15025 inhibits the cell cycle and the MAPK/ERK signaling pathway in AML cells. (a) KEGG analysis revealed that differentially expressed genes were significantly enriched in relevant signaling pathways. (b) GSEA of differentially expressed genes in the treated group, compared with the control group, indicated a predominant enrichment in cell cycle-related pathways. (c) Two AML cell lines (KG1A and THP-1) were exposed to different concentrations of BGB-15025, and the expression levels of CCND1 , CDK4 , and P21 genes were quantified using qRT-PCR. (d) Various concentrations of BGB-15025 were administered to two AML cell lines (KG1A and THP-1), followed by the detection of cyclin D1, CDK4, and P21 protein expressions via Western blot analysis. (f) Different concentrations of BGB-15025 were administered to two AML cell lines, KG1A and THP-1. The expression levels of ERK, p-ERK, P38, and p-P38 proteins were assessed using Western blot analysis. Data presented are derived from at least three independent experiments. Statistical significance was determined as follows: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 when compared with the control group. (e and g) The effect of HPK1 knockdown on the expression of the above-mentioned proteins was assessed in AML (THP-1) cells. AML, acute myeloid leukemia; GSEA, Gene Set Enrichment Analysis; HPK1, hematopoietic progenitor kinase 1; KEGG, Kyoto Encyclopedia of Genes and Genomes; MAPK/ERK, mitogen-activated protein kinase/extracellular signal-regulated kinase; qRT-PCR, quantitative real-time PCR.

Article Snippet: Membranes were subsequently incubated overnight at 4 °C with specific primary antibodies: β-actin (#4970; 1 : 1000), HPK1 (#46510; 1 : 1000), cyclin D1 (#55506; 1 : 1000), P21 (#2947; 1 : 1000), ERK (#4696; 1 : 1000), phosphorylated ERK (p-ERK, #4370; 1 : 1000), P38 MAPK (#8690; 1 : 1000), and phosphorylated P38 MAPK (p-P38, #9211; 1 : 1000) (all from Cell Signaling Technology, Danvers, Massachusetts, USA).

Techniques: Protein-Protein interactions, Control, Expressing, Quantitative RT-PCR, Western Blot, Derivative Assay, Knockdown, Real-time Polymerase Chain Reaction

Journal: JID Innovations

Article Title: High-salt diet aggravates skin inflammation of psoriasis-like mouse model with CCL20‒CCR6 axis further activation

doi: 10.1016/j.xjidi.2026.100451

Figure Lengend Snippet: Increasing sodium concentration upregulates Ccl20 expression in KCs through the JNK/p38–SGK1 pathway. ( a ) qPCR analysis of selected chemokines, cytokines, and Sgk1 in KCs (n = 5 for each group). (b) Immunoblot analysis of p38, phosphorylated p38, JNK, and phosphorylated JNK in KCs for different time (0 min, 30 min, 60 min), and tubulin was used as control. The relative densitometry of all bands (arbitrary unit) was normalized to the level of 0 min (n = 3 for each group). (c) qPCR analysis of Ccl20 and Sgk1 RNA expression in KCs treated with pharmacological inhibitors (n = 3 for each group). Data are shown as mean ± SEM. For a, P -values were determined by 2-tailed Student’s t -test. For c, P -values were determined by 1-way ANOVA. ∗∗ P < .01, ∗∗∗ P < .01, and ∗∗∗∗ P < .0001. KC, keratinocyte; min, minute.

Article Snippet: JNK Rabbit mAb (Cell Signaling Technology, catalog number 5292), phosphorylated JNK Rabbit mAb (Cell Signaling Technology, catalog number 4668), p38 Rabbit mAb (Cell Signaling Technology, catalog number 8690), phosphorylated p38 Rabbit mAb (Cell Signaling Technology, catalog number 4511), mouse anti-Alpha Tubulin mAb (Proteintech, catalog number HRP-66031) were used as primary antibodies, and goat antirabbit antibody (Abcam, catalog number ab6721) was used as secondary antibody.

Techniques: Concentration Assay, Expressing, Western Blot, Control, RNA Expression

Journal: The American Journal of Pathology

Article Title: Mechanistic Insights into Glucocorticoid-Induced Ocular Hypertension Using Differences in Mouse Strain Responsiveness

doi: 10.1016/j.ajpath.2025.11.009

Figure Lengend Snippet: Identification of putative molecular mechanisms involved in GC-induced ocular hypertension response. A: Left: Hub-and-spoke diagram of the upstream regulators SMARCA4 and myocardin-related transcription factor (MRTFA), with its target genes differentially expressed within the data set. Right: Quantification of protein levels of SMARCA4 and MRTFA in trabecular meshwork (TM) tissues of C57BL/6J mouse treated with dexamethasone (DEX) or vehicle (Veh); unpaired two-tailed t -test was used. B: Left: Diagram illustrating the P38 mitogen-activated protein kinase (MAPK) upstream regulator and its target genes. Right: Phosphorylation level of P38 MAPK against total P38 MAPK in TM tissues of DEX-treated C57BL/6J mice compared with vehicle; unpaired two-tailed t -test was used. C: Left: Causal network analysis revealed down-regulation of Notch signaling in response to DEX treatment in responders, thereby driving the immunomodulatory effect. Right: Levels of cleaved Notch were reduced in DEX-treated TM rim tissues compared with vehicle. Unpaired two-tailed t -test was used. Each n represents a sample from an individual mouse containing pooled TM tissue from left and right eyes. Data are represented as means ± SEM ( A – C ). n = 4 per group ( A – C ). ∗ P < 0.05. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; NS, not significant.

Article Snippet: Phosphorylated P38 MAPK antibody , 4511P , 1:1000 , Cell Signaling Technology.

Techniques: Two Tailed Test, Phospho-proteomics