p38 mapk inhibitors  (Baines Food Consultancy)

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: Hepatic Oncology

Article Title: RTA‑408 induces p38‑dependent apoptosis and suppresses cell viability in hepatocellular carcinoma cells

doi: 10.1080/20450923.2026.2659967

Figure Lengend Snippet: RTA-408 activates p38–NRF2 signaling and promotes LC3B accumulation in hepatocellular carcinoma cells. HepG2 and PP5 cells were treated with RTA-408 (0, 200, 400, or 600 nM) for 24 h, and protein expression was analyzed by western blotting. Representative immunoblots show phosphorylated p38 (p-p38), total p38, phosphorylated ERK1/2 (p-ERK), total ERK1/2, phosphorylated JNK (p-JNK), total JNK, NRF2, LC3B, p62, cleaved caspase-3 (c-cas3), and β-actin. Densitometric analyses of p-p38/p38, p-ERK/ERK, and p-JNK/JNK, as well as NRF2, LC3B, p62, and c-cas3 normalized to β-actin, are shown in the accompanying bar graphs. RTA-408 increased p38 phosphorylation and NRF2 expression in both cell lines and was accompanied by marked accumulation of LC3B and p62, while ERK and JNK responses differed between HepG2 and PP5 cells. Cleaved caspase-3 increased at higher concentrations of RTA-408. β-Actin was used as a loading control. Data are presented as mean ± SEM from three independent experiments ( n = 3). *P < 0.05 and **P < 0.01 versus control.

Article Snippet: RTA-408 (omaveloxolone) (MCE; 1474034-05-3; USA) and the p38 MAPK inhibitor, SB203580 (MCE; 152121-47-6; USA), were dissolved in dimethyl sulfoxide (DMSO) to prepare stock solutions (10 mM for RTA-408 and 10 mM for SB203580), which were stored at − 20 °C according to the manufacturer’s instructions.

Techniques: Expressing, Western Blot, Phospho-proteomics, Control

Journal: Hepatic Oncology

Article Title: RTA‑408 induces p38‑dependent apoptosis and suppresses cell viability in hepatocellular carcinoma cells

doi: 10.1080/20450923.2026.2659967

Figure Lengend Snippet: p38 inhibition attenuates RTA-408-induced p38 signaling, LC3B/p62 accumulation, and apoptotic protein activation in hepatocellular carcinoma cells. HepG2 and PP5 cells were treated for 24 h with vehicle control (Con), RTA-408 (400 nM) alone, or RTA-408 (400 nM) plus SB203580 (10 μM). Protein expression was analyzed by western blotting. Representative immunoblots show phosphorylated p38 (p-p38), total p38, NRF2, LC3B, p62, cleaved caspase-3 (c-cas3), and β-actin. Densitometric analyses of p-p38/p38, as well as NRF2, LC3B, p62, and c-cas3 normalized to β-actin, are shown in the accompanying bar graphs. In both HepG2 and PP5 cells, RTA-408 increased p38 phosphorylation, NRF2 expression, LC3B accumulation, p62 accumulation, and cleaved caspase-3 levels, whereas co-treatment with SB203580 markedly attenuated these RTA-408-induced effects without altering total p38 expression. These findings indicate that p38 activity contributes to RTA-408-induced stress signaling, LC3B/p62-associated responses, and apoptotic protein activation in hepatocellular carcinoma cells. Data are presented as mean ± SEM from three independent experiments ( n = 3). *P < 0.05 and **P < 0.01 versus control; #P < 0.05 and ##P < 0.01 versus RTA-408 alone.

Article Snippet: RTA-408 (omaveloxolone) (MCE; 1474034-05-3; USA) and the p38 MAPK inhibitor, SB203580 (MCE; 152121-47-6; USA), were dissolved in dimethyl sulfoxide (DMSO) to prepare stock solutions (10 mM for RTA-408 and 10 mM for SB203580), which were stored at − 20 °C according to the manufacturer’s instructions.

Techniques: Inhibition, Activation Assay, Control, Expressing, Western Blot, Phospho-proteomics, Activity Assay

Journal: Hepatic Oncology

Article Title: RTA‑408 induces p38‑dependent apoptosis and suppresses cell viability in hepatocellular carcinoma cells

doi: 10.1080/20450923.2026.2659967

Figure Lengend Snippet: Pharmacological inhibition of p38 MAPK partially restores cell viability and attenuates RTA-408-induced apoptosis in hepatocellular carcinoma cells. (A) HepG2 and PP5 cells were treated for 24 h with vehicle control (Con), RTA-408 (400 nM) alone, or RTA-408 (400 nM) plus SB203580 (10 μM), and cell viability was assessed by the MTT assay. Bar graphs show the percentage of viable cells relative to the control group. (B) Under the same treatment conditions, apoptosis was evaluated by Annexin V/7-AAD flow cytometry. Representative dot plots show the distribution of viable (Annexin V − /7-AAD − ), early apoptotic (Annexin V + /7-AAD − ), late apoptotic (Annexin V + /7-AAD + ), and necrotic (Annexin V − /7-AAD + ) cell populations. The accompanying bar graphs summarize total apoptosis (early + late apoptosis). In both cell lines, RTA-408 reduced cell viability and increased apoptosis, whereas co-treatment with SB203580 partially reversed the loss of viability and attenuated the pro-apoptotic effect of RTA-408. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical significance was determined by one-way analysis of variance with appropriate post hoc testing. *P < 0.05, **P < 0.01, and ***P < 0.001 versus control; ##P < 0.01 versus RTA-408 alone.

Article Snippet: RTA-408 (omaveloxolone) (MCE; 1474034-05-3; USA) and the p38 MAPK inhibitor, SB203580 (MCE; 152121-47-6; USA), were dissolved in dimethyl sulfoxide (DMSO) to prepare stock solutions (10 mM for RTA-408 and 10 mM for SB203580), which were stored at − 20 °C according to the manufacturer’s instructions.

Techniques: Inhibition, Control, MTT Assay, Flow Cytometry

Journal: JBMR Plus

Article Title: Osteocytes regulate osteoprotegerin expression via the p38-MAPK-CREB pathway in rheumatoid arthritis

doi: 10.1093/jbmrpl/ziag023

Figure Lengend Snippet: TNF-α-induced changes in Wnt/β-catenin-related transcripts and activation of the p38-MAPK-CREB signaling pathway in osteocytes. (A) Dot plots showing relative mRNA levels of Ctnnb1 (β-catenin), Lef1 , and Axin2 in MLO-Y4 cells treated with or without TNF-α ( n = 3). (B) Representative immunoblotting images showing phosphorylated p38 MAPK (p-p38), total p38, phosphorylated CREB (p-CREB), total CREB, phosphorylated JNK (p-JNK), total JNK, phosphorylated ERK (p-ERK), total ERK, and β-actin in MLO-Y4 cells following TNF-α treatment. Data in (A) are shown as individual values with the mean ± SD and were analyzed by the two-sided Student’s t -test. (C) Representative immunoblot of OPG in TNF-α-stimulated MLO-Y4 cells treated with a p38 inhibitor or a CREB inhibitor. Cells were stimulated with TNF-α in the presence or absence of SB203580 (p38 inhibitor) or 666-15 (CREB inhibitor), and total cell lysates were subjected to immunoblotting for OPG. β-actin serves as the loading control. Numeric values shown beneath each band represent the relative expression levels of OPG/β-actin for the corresponding lane. (D) ChIP-PCR demonstrating enrichment of the OPG promoter in anti-CREB immunoprecipitates from MLO-Y4 cells with or without TNF-α stimulation, with densitometric quantification of the ChIP-PCR bands; input DNA served as the internal control, normal IgG as the negative control, and anti-histone H3 as the positive control.

Article Snippet: For inhibitor experiments, the p38 MAPK inhibitor SB203580 (Selleck Chemicals) was used at a concentration of 30 μM, and the CREB inhibitor 666-15 (Selleck Chemicals) was used at a concentration of 0.1 μM.

Techniques: Activation Assay, Western Blot, Control, Expressing, Negative Control, Positive Control

Journal: The FASEB Journal

Article Title: ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway

doi: 10.1096/fj.202600272R

Figure Lengend Snippet: Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

Article Snippet: To examine the inflammatory signaling pathways involved in LPS‐mediated cytokine production, signaling inhibitors targeting p38 MAPK (SB239063; MedChemExpress, Monmouth Junction NJ, USA), NF‐κB (APDC; Merck KGaA), MEK1/2 (U0126; MedChemExpress), phosphatidyl inositol‐3 kinase (PI3K; Wortmannin; Merck KGaA), and c‐Jun N‐terminal kinase (JNK; SP600125; Merck KGaA) were administered 30 min prior to LPS treatment.

Techniques: Protein-Protein interactions, Western Blot, Control

Journal: The FASEB Journal

Article Title: ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway

doi: 10.1096/fj.202600272R

Figure Lengend Snippet: Effect of 13‐HODE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 13‐HODE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

Article Snippet: To examine the inflammatory signaling pathways involved in LPS‐mediated cytokine production, signaling inhibitors targeting p38 MAPK (SB239063; MedChemExpress, Monmouth Junction NJ, USA), NF‐κB (APDC; Merck KGaA), MEK1/2 (U0126; MedChemExpress), phosphatidyl inositol‐3 kinase (PI3K; Wortmannin; Merck KGaA), and c‐Jun N‐terminal kinase (JNK; SP600125; Merck KGaA) were administered 30 min prior to LPS treatment.

Techniques: Protein-Protein interactions, Western Blot, Control