antibody against ho 1  (Santa Cruz Biotechnology)

Journal: Current Therapeutic Research, Clinical and Experimental

Article Title: The Berberine Derivative BBR684 Inhibits VDAC Oligomerization to Suppress Ferroptosis in Acute Kidney Injury

doi: 10.1016/j.curtheres.2026.100825

Figure Lengend Snippet: BBR684 attenuates Erastin-induced ferroptosis in HK-2 cells by suppressing lipid peroxidation and activating the antioxidant response. (A) Flow cytometric analysis of lipid peroxidation using the C11-BODIPY probe in HK-2 cells treated as indicated for 12 hours. Data are presented as mean fluorescence intensity (MFI). (B) Intracellular Fe²⁺ levels measured by a ferrous iron colorimetric assay. (C, D) Levels of malondialdehyde (MDA, C) and reduced glutathione (GSH, D) in cell lysates. (E, F) Representative immunofluorescence images (E) and quantification (F) of 4-hydroxynonenal (4-HNE) adducts (red) in HK-2 cells. Nuclei were counterstained with DAPI (blue). Scale bar, 50 µm. (G) Western blot analysis of key ferroptosis-related proteins: glutathione peroxidase 4 (GPX4), heme oxygenase-1 (HO-1), and nuclear factor erythroid 2–related factor 2 (NRF2). β-actin served as the loading control. Data are from 3 independent biological replicates (n = 3) and presented as mean ± SEM. Significance was determined by one-way ANOVA followed by Tukey's HSD post hoc test. * P < 0.05, ** P < 0.01, *** P < 0.001; n.s., not significant.

Article Snippet: Antibodies against GPX4 (Catalog #3F5G5), HO-1 (Catalog #10701-1-AP), NRF2 (Catalog #16396-1-AP), VDAC (Catalog #10866-1-AP), Cleaved Caspase-3 (Catalog #68773-1-Ig), and CD45 (Catalog #98035-1-RR) were purchased from Proteintech.

Techniques: Fluorescence, Colorimetric Assay, Immunofluorescence, Western Blot, Control

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: Stimulus‐responsive expression of HO1 and CD47 in transduced HEK‐293T cells under xenogeneic and inflammatory stimuli. (A) Schematic diagram of the dual‐promoter expression construct: HO1 cDNA under the human HO1 promoter and CD47 cDNA under the pig EF1α promoter. (B) Western blot analysis of HO1 and CD47 protein expression in HEK‐293T cells transduced with the construct in (A) and treated with control medium, human serum, or PMA. (C) qPCR showing time‐dependent mRNA expression levels of HO1 and CD47 in HEK‐293T cells transduced with the construct in (A) and subjected to the same treatments. HO1 exhibited strong inducibility, while CD47 , already expressed at high baseline levels, was further upregulated following stimulation. Data are presented as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). HO1, heme oxygenase‐1; PMA, phorbol 12‐myristate 13‐acetate.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: Expressing, Construct, Western Blot, Transduction, Control

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: CRISPR/Cas9‐mediated knock‐in of HO1/CD47 expression cassette into pig CMAH locus and functional evaluation of knock‐in cell clones. (A) Knock‐in strategy and PCR‐based genotyping scheme for integrating the HO1/CD47 expression cassette into exon 4 of the pig CMAH locus using CRISPR/Cas9‐mediated homology‐directed repair. The diagram illustrates the structure of the inserted cassette and the location of PCR primer pairs (HO1‐F/CD47‐R and CMAH‐F/HO1‐R) used for genotyping. (B) PCR‐based genotyping analysis of donor cell clones confirmed the targeted integration of the HO1/CD47 expression cassette into the CMAH locus. The presence of the cassette was verified by amplification of its internal region (HO1‐F/CD47‐R), and site‐specific integration at the 5′ junction with the CMAH gene was confirmed using the CMAH‐F/HO1‐R primer pair. Multiple clones showed positive bands for both primer sets. The expected amplicon sizes were 1763 bp (HO1‐F/CD47‐R) and 949 bp (CMAH‐F/HO1‐R). (C) Analysis of cytotoxicity in GTKO/CMAH‐KO/HO1/CD47 knock‐in fibroblast clones following exposure to 10% human serum. Data are presented as mean ± SD ( n = 3 biological replicates). * p < 0.05, ** p < 0.01, *** p < 0.001. CMAHKO, CMAH knockout; GTKO , GGTA1 ‐knockout; HO1, heme oxygenase‐1; SD, standard deviation.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: CRISPR, Knock-In, Expressing, Functional Assay, Clone Assay, Amplification, Knock-Out, Standard Deviation

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: Generation and genotyping of a GTKO/CMAH‐KI (HO1/CD47)/+ cloned piglet. (A) Image of the cloned piglet produced using knock‐in clone #229. (B) PCR analysis confirming HO1/CD47 knock‐in and GGTA 1‐knockout. Primer information is detailed in Section and Figure . Lanes 1 and 4 show GGTA1 ‐knockout. Lanes 2 and 5 indicate the presence of the HO1/CD47 cassette. Lanes 3 and 6 show the 5′ junction between the CMAH locus and the HO1/CD47 cassette. HO1, heme oxygenase‐1.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: Clone Assay, Produced, Knock-In, Knock-Out

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: Western blot analysis of HO1 and CD47 expression in tissues of GTKO/CMAH‐KI (HO1/CD47)/+ cloned piglet. Protein lysates were prepared from six tissues (heart, liver, lung, spleen, kidney, and aorta) of GTKO/ CMAH/HO1/CD47/+ cloned pigs and analyzed using Western blotting. HO1 expression (top panel) was predominantly detected in the liver, lung, and spleen, whereas CD47 (middle panel) was strongly expressed across all tissues. Vinculin was used as the loading control (bottom panel). HO1, heme oxygenase‐1.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: Western Blot, Expressing, Clone Assay, Control

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: Flow cytometric analysis of human CD47 expression in pEFs and PBMCs from GTKO and GTKO/CMAH‐KI (HO1/CD47)/+ pigs. (A) Knock‐in pigs showed a substantial increase in CD47 + pEFs compared with those in GTKO pigs. (B) Both monocytes and lymphocytes from knock‐in pigs exhibited a marked increase in CD47 + cells compared with those in GTKO pigs. CD47 was stained with APC‐conjugated anti‐human CD47 antibody. Monocytes and lymphocytes were gated based on FSC/SSC profiles. HO1, heme oxygenase‐1; PBMCs, peripheral blood mononuclear cells; PEFs, pig ear fibroblasts.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: Expressing, Knock-In, Staining

Journal: Xenotransplantation

Article Title: CMAH‐Targeted Knock‐In of Inducible Heme Oxygenase‐1 and Constitutive CD47 in GGTA1‐Knockout Pigs for Xenotransplantation

doi: 10.1111/xen.70124

Figure Lengend Snippet: Immunohistochemical detection of HO1 protein in tissues from GTKO control and GTKO/CMAH‐KI (HO1/CD47)/+ pigs. Tissue sections from the heart, liver, lungs, and spleen were analyzed using immunohistochemistry to assess HO1 protein expression. The upper row shows sections from knock‐in pigs, while the lower row shows the corresponding tissues from GTKO control pigs. Positive HO1 staining (brown) was observed in the liver and lungs of transgenic pigs, consistent with inflammation‐inducible promoter activity, whereas no signal was detected in the heart and spleen or any tissue from GTKO controls. Tissues were obtained from the neonatal knock‐in piglet (#2) that died at 3 days of age; therefore, the data represent a single biological specimen. All sections were counterstained with hematoxylin. Scale bar, 50 µm; magnification, 40×. HO1, heme oxygenase‐1.

Article Snippet: Thereafter, the sections were incubated overnight at 4°C with a primary antibody against HO‐1 (sc‐136960; Santa Cruz Biotechnology) at a 1:200 dilution.

Techniques: Immunohistochemical staining, Control, Immunohistochemistry, Expressing, Knock-In, Staining, Transgenic Assay, Activity Assay

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: AKK alleviates ABX/LPS-induced pathological remodeling and inflammation in murine intestine via inhibition of the p38α MAPK pathway. (A) Schematic of the experimental design, illustrating the timeline of ABX/LPS challenge and the interventions with AKK or the p38α MAPK inhibitor (SB203580). (B) Body weight changes of mice in different treatment groups. (C) Disease activity index. The data points represent the daily measurements. To make the graph clear, the data at key time points are shown in the figure. (D) Representative images showing: (i) The gross appearance of the colon and cecum; (ii) H&E-stained sections of the ileum; and (iii) H&E-stained sections of the colon. (E) Quantitative analysis of colon length. (F) Histopathological colitis scores. (G–I) Morphometric analysis of the ileum, including villus height, crypt depth, and the villus height-to-crypt depth ratio (VCR). n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus NC group; * p < 0.05, ** p > p < 0.01, *** p < 0.001, **** p < 0.0001 versus NS + ABX/LPS group, + p < 0.05, ++ p < 0.01, +++ p < 0.01, +++ p < 0.001, +++p < 0.0001 versus the AKK-treated group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Inhibition, Activity Assay, Staining

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: AKK directly inhibits phosphorylation and activation of p38α MAPK in human colonic epithelial cells. In the LPS-induced injury model of Ncm460 cells: (A) Identification of the optimal concentration and treatment time for AKK via CCK-8 assay. (B) AKK reverses the LPS-induced suppression of cell viability. Data are normalized to the control group (set as 1.0). (C) Representative western blot images of p38α MAPK and phosphorylated p38α MAPK (p-p38α MAPK). Blots for p38α MAPK and p-p38α MAPK were obtained from the same membrane. (D) Quantitative analysis of total p-p38α MAPK protein expression levels. n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus p38KD group. * p < 0.05, ** p > p < 0.01, *** p < 0.001, **** p < 0.0001 versus LPS group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Phospho-proteomics, Activation Assay, Concentration Assay, CCK-8 Assay, Control, Western Blot, Membrane, Expressing

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: Inhibition of p38α MAPK alleviates oxidative stress in human colonic epithelial cells by activating the Nrf2 pathway. In the LPS-induced injury model of Ncm460 cells: (A,B) Representative flow cytometry scatter plots and quantitative analysis of intracellular ROS levels. (C) Levels of cellular oxidative stress markers (GSH, SOD, MDA). (D) Representative western blot images of Nrf2 and its downstream targets HO-1 and NQO1. The representative western blot images presented here are accompanied by the corresponding internal control detected on the same membrane. (E–G) Quantitative analysis of protein and mRNA expression levels of Nrf2 (E) , HO-1 (F) , and NQO1 (G) . n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus p38KD group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 versus LPS group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Inhibition, Flow Cytometry, Western Blot, Control, Membrane, Expressing

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: AKK enhances migration and tight junction integrity in human colonic epithelial cells in a p38α MAPK-dependent manner. In the LPS-induced injury model of Ncm460 cells: (A) Representative images and quantitative analysis of wound closure rate in the scratch assay. (B) Representative western blot images of tight junction proteins. The representative western blot images presented here are accompanied by the corresponding internal control detected on the same membrane. (C–E) Quantitative analysis of protein and mRNA expression levels of ZO-1 (C) , Occludin (D) , and Claudin-1 (E) . n = 6 independent biological replicates. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus p38KD group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 versus LPS group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Migration, Wound Healing Assay, Western Blot, Control, Membrane, Expressing

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: Akk restores the intestinal barrier by upregulating MUC2 and tight junction expression in a p38α MAPK-dependent manner. (A) Modulation of the mucus barrier by Akk and the p38α MAPK inhibitor (SB203580): representative IHC images of MUC2 and quantitative analysis. (B) Representative western blot images of tight junction proteins across groups. The representative western blot images presented here are accompanied by the corresponding internal control detected on the same membrane. (C–E) Quantitative analysis of protein and mRNA expression levels of ZO-1 (C) , occludin (D) , and claudin-1 (E) . (F,G) Serum levels of intestinal barrier damage markers, DAO activity, and D-LA concentration. n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus NC group; * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 versus NS + ABX/LPS group, + p < 0.05, ++ p < 0.01, +++ p < 0.01, +++ p < 0.001, +++ p < 0.0001 versus the AKK-treated group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Expressing, Western Blot, Control, Membrane, Activity Assay, Concentration Assay

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: AKK alleviates intestinal oxidative stress by activating the Nrf2 signaling pathway through inhibition of p38α MAPK. (A) Levels of oxidative stress markers in colonic tissue: GSH, SOD, and MDA (B) Representative western blot images of Nrf2 and its downstream targets, HO-1 and NQO1. The representative western blot images presented here are accompanied by the corresponding internal control detected on the same membrane. n = 6 independent biological replicates. (C–E) Quantitative analysis of protein and mRNA expression levels of Nrf2 (C) , HO-1 (D) , and NQO1 (E) . n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus NC group; * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 versus NS + ABX/LPS group, + p < 0.05, ++ p < 0.01, +++ p < 0.01, +++ p < 0.001, +++ p < 0.0001 versus the A-treated group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Inhibition, Western Blot, Control, Membrane, Expressing

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: Molecular docking predicts direct binding of AKK to p38α MAPK and validation in a murine model. Exploratory molecular docking results demonstrating strong binding between AKK and p38α MAPK: (A) Detailed view of the binding mode, with a binding free energy of −7.0 kcal·mol −1 ; (B) 3D representation of binding site interactions (yellow dashed lines indicate hydrogen bonds); (C) Schematic 3D structure of the complex; (D) 2D diagram of binding site interactions. (E) Top ten ranked binding conformations from docking screening. (F–I) Experimental validation in an ABX/LPS-induced mouse intestinal injury model: (F) Representative western blot images of p38α MAPK and p-p38α MAPK in colonic tissue; Blots for p38α MAPK and p-p38α MAPK were obtained from the same membrane. (G) p38α MAPK mRNA expression levels in the colon; (H) p-p38α MAPK/p38α MAPK ratio; (I) Total p-p38α MAPK protein levels. n = 6 independent biological replicates. All data are presented as mean ± SEM. # p < 0.05, ### p < 0.001, #### p < 0.0001 versus NC group; * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 versus NS + ABX/LPS group, + p < 0.05, ++ p < 0.01, +++ < 0.01, +++ p < 0.001, +++ p < 0.0001 versus the AKK-treated group.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques: Binding Assay, Biomarker Discovery, Western Blot, Membrane, Expressing

Journal: Frontiers in Microbiology

Article Title: Akkermansia muciniphila alleviates antibiotic- and LPS-induced oxidative stress via the p38α MAPK–Nrf2 signaling axis

doi: 10.3389/fmicb.2026.1753421

Figure Lengend Snippet: A schematic model illustrating the role of the AKK-p38α MAPK-Nrf2 axis and microbial regulation in restoring intestinal homeostasis.

Article Snippet: Antibodies against p-p38α MAPK (#4511), HO-1(#43966), NQO-1(#3187) were purchased from Cell Signaling Technology (Danvers, MA, United States).

Techniques:

Journal: Journal of Cachexia, Sarcopenia and Muscle

Article Title: Calprotectin Is a Circulating Biomarker and Potential Therapeutic Target for Sarcopenia in Chronic Obstructive Pulmonary Disease

doi: 10.1002/jcsm.70196

Figure Lengend Snippet: Paquinimod attenuates the inflammatory response and oxidative stress in the cigarette smoke‐exposed mouse model. (A) The mRNA levels of inflammatory factors (TNF‐α, IL‐6, IL‐8, CXCL1, and IL1β) in skeletal muscle measured by qPCR. (B) TNF‐α and IL‐6 levels in different groups measured by ELISAs. (C) Levels of GSH, MDA, SOD2, and T‐AOC in the mouse Gast muscle. (D) Western blot analysis of the levels of antioxidant markers (Nrf2 and HO‐1) in each group of mice. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: The primary antibodies used were a rabbit polyclonal antibody against GAPDH (1:1000; Cell Signalling Technology, 5174), a mouse monoclonal antibody against atrogin‐1 (1:1000; Santa Cruz Biotechnology, sc‐166 806), a mouse monoclonal antibody against MuRF1 (1:1000; Santa Cruz Biotechnology, sc‐398 608), a rabbit monoclonal antibody against Nrf2 (1:1000; Cell Signalling Technology, 12721), and a rabbit monoclonal antibody against HO‐1 (1:1000; Cell Signalling Technology, 26416).

Techniques: Western Blot

Journal: Phytotherapy Research

Article Title: Lithospermic Acid Improves Doxorubicin‐Induced Cardiomyopathy Through Sirtuin‐3‐Mediated Deacetylation of p53

doi: 10.1002/ptr.70188

Figure Lengend Snippet: Lithospermic acid (LA) ameliorates doxorubicin (Dox)‐induced apoptosis and oxidative damage in human cardiomyocytes. (A) Schematic diagram illustrating the differentiation protocol for human embryonic stem cell (hESC)‐derived cardiomyocytes (hESC‐CMs) in chemically defined medium. (B) The expression of caspase 3, BAX, and BCL2 protein. (C) Mitochondrial membrane potential was measured using JC‐1 fluorescent probe. (D) The expression of gp91 phox , p67 phox , P‐p47 phox and p47 phox protein. (E) The reactive oxygen species (ROS) level determined by DCFH‐DA staining. (F) The mitochondrial superoxide formation examined by MitoSOX Red and Mito‐Tracker staining. (G) The expression of NFR2 in cytoplasm and nucleus of hESC‐CMs. H, The expression of HO‐1 and NQO‐1 protein. The experiments were conducted after 24‐h treatment with Dox (2 μM) in combination with vehicle (Veh) or LA (20 μM). n = 6 in B, D, H, n = 7 in C, E, F, n = 8 in G, n = 6 in H.

Article Snippet: Antibodies against HO‐1 (ER1802‐73), NQO‐1 (ET1702‐50), and NRF2 (HA721432) were acquired from HuaBio. (Hangzhou, China).

Techniques: Derivative Assay, Expressing, Membrane, Staining

Journal: Phytotherapy Research

Article Title: Lithospermic Acid Improves Doxorubicin‐Induced Cardiomyopathy Through Sirtuin‐3‐Mediated Deacetylation of p53

doi: 10.1002/ptr.70188

Figure Lengend Snippet: Lithospermic acid (LA) improves doxorubicin (Dox)‐induced oxidative stress damage in mouse cardiomyocytes. (A and B) The reactive oxygen species (ROS) level determined by DCFH‐DA probe. (C and D) The mitochondrial superoxide formation examined by MitoSOX Red and Mito‐Tracker probe. (E) The levels of malondialdehyde (MDA). (F–H) The expression of gp91 phox , p67 phox , P‐p47 phox and p47 phox protein. (I and J) The expression of NFR2 in cytoplasm and nucleus of HL‐1 cells. (K and L) The expression of HO‐1 and NQO‐1 protein. (M) The expression of Ho‐1 and Nqo‐1 mRNA. The experiments were made after 24‐h treatment with Dox (1 μM) in combination with vehicle (Veh) or LA (20 μM). n = 8 in A‐D, n = 6 in E–H, n = 3 in I and J, n = 6 in K–M. Data represent the mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001. Two‐way ANOVA was used.

Article Snippet: Antibodies against HO‐1 (ER1802‐73), NQO‐1 (ET1702‐50), and NRF2 (HA721432) were acquired from HuaBio. (Hangzhou, China).

Techniques: Expressing

Journal: Phytotherapy Research

Article Title: Lithospermic Acid Improves Doxorubicin‐Induced Cardiomyopathy Through Sirtuin‐3‐Mediated Deacetylation of p53

doi: 10.1002/ptr.70188

Figure Lengend Snippet: Lithospermic acid (LA) prevents doxorubicin (Dox)‐induced cardiac apoptosis and oxidative damage in mice. (A and B) The expression of caspase 3, BAX, and BCL2 protein. (C) Representative images of immunohistochemical analysis of 4‐hydroxynonenal (4‐HNE, brown color) in the cardiac tissue. (D) The levels of malondialdehyde (MDA). (E and F) The expression of gp91 phox , p67 phox , P‐p47 phox and p47 phox protein. (G and H) The expression of HO‐1 and NQO‐1 protein. Measurements were made 4 weeks after the administration of LA (100 μL, 50 mg/kg per day, 30 days, i.g.) or Dox (100 μL, 5 mg/kg per times, 4 times, i.p.). n = 6 in all group. Data represent the mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001. Two‐way ANOVA was used.

Article Snippet: Antibodies against HO‐1 (ER1802‐73), NQO‐1 (ET1702‐50), and NRF2 (HA721432) were acquired from HuaBio. (Hangzhou, China).

Techniques: Expressing, Immunohistochemical staining