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Image Search Results
Journal: PLoS ONE
Article Title: Allergen-Induced Dermatitis Causes Alterations in Cutaneous Retinoid-Mediated Signaling in Mice
doi: 10.1371/journal.pone.0071244
Figure Lengend Snippet: Systemic and topical OVA sensitization results in inflammation, disturbs epidermal barrier homeostasis, and induces PPARδ target gene expression in skin.
Article Snippet:
Techniques: Targeted Gene Expression, Binding Assay
Journal: PLoS ONE
Article Title: Allergen-Induced Dermatitis Causes Alterations in Cutaneous Retinoid-Mediated Signaling in Mice
doi: 10.1371/journal.pone.0071244
Figure Lengend Snippet: ( a ) IL-4 serum levels after systemic with or without additional topical OVA sensitization (n = 8). ( b ) ATRA levels in mouse skin determined by HPLC MS-MS method upon systemic (i.p.) and systemic plus topical (i.p.+e.c.) OVA sensitization (n = 3/group). ( c ) Ratio of Fabp5 vs. Crabp2 expression in the skin of OVA-treated mice (n = 6/group) compared to control mice (PBS i.p.). Data are presented as mean values ± SEM. Statistical significance ( p ) is based on one-way ANOVA followed by Tukey’s multiple comparison test for gene expression results and ELISA data. For HPLC MS-MS results, significance was determined using Student’s t -test.
Article Snippet:
Techniques: Tandem Mass Spectroscopy, Expressing, Control, Comparison, Gene Expression, Enzyme-linked Immunosorbent Assay
Journal: PLoS ONE
Article Title: Allergen-Induced Dermatitis Causes Alterations in Cutaneous Retinoid-Mediated Signaling in Mice
doi: 10.1371/journal.pone.0071244
Figure Lengend Snippet: ( a ) Fabp5 protein levels in the skin of mice with allergen-induced dermatitis. 150 µg proteins were loaded per lane and beta-actin was used as control for even protein loading. ( b ) Immunohistochemical analysis of Fabp5 protein expression in five-micrometer back skin sections of OVA-sensitized mice. ( c ) ATRA-induced nuclear receptor-mediated signaling pathways depending on the predominant cellular transport protein.
Article Snippet:
Techniques: Control, Immunohistochemical staining, Expressing, Protein-Protein interactions
Journal: Molecular medicine reports
Article Title: MicroRNA‑214 targets Wnt3a to suppress liver cancer cell proliferation.
doi: 10.3892/mmr.2017.7483
Figure Lengend Snippet: Figure 1. miR‑214 is downregulated in liver cancer and targets Wnt3a. (A) Reverse transcription‑quantitative polymerase chain reaction was performed to examine the expression of miR‑214 in 24 paired human hepatocellular carcinoma and non‑tumor tissues. (B) Relative expression of miR‑214 in liver cancer cell lines and a normal liver cell line. **P<0.01; *P<0.05. (C) miR‑214 seed region sequence in the 3'UTR of Wnt3a. (D) Wnt3a protein expression as detected by immunohistochemistry. (E) Protein expression levels of Wnt3a were measured by western blot analysis in HepG2 cells transfected with miR‑214 or miR‑ctrl. (F) miR‑214 was co‑transfected with pmirGLO, pmirGLO‑Wnt3a‑3'‑UTR‑wt or pmirGLO‑Wnt3a‑3'‑UTR‑mut in HepG2 cells. Relative luciferase activity was measured after 48 h. *P<0.05 vs. control. miR, microRNA; mut/M, mutant; UTR, untranslated region; wt/W, wild‑type.
Article Snippet: Membranes were then incubated with
Techniques: Polymerase Chain Reaction, Expressing, Sequencing, Immunohistochemistry, Western Blot, Transfection, Luciferase, Activity Assay, Control, Mutagenesis
Journal: Molecular medicine reports
Article Title: MicroRNA‑214 targets Wnt3a to suppress liver cancer cell proliferation.
doi: 10.3892/mmr.2017.7483
Figure Lengend Snippet: Figure 2. miR‑214 inhibits the proliferation of liver cancer cells. CCK8 assay was performed to detect the effects of miR‑214 on cell proliferation at 24, 48, and 72 h in (A) HepG2 and (B) Hep3B cells. CCK8 assay was performed to detect the effects of siWnt3a on cell proliferation at 24, 48 and 72 h in (C) HepG2 and (D) Hep3B cells. Wnt3a overexpression vector was co‑transfected with miR‑ctrl or miR‑214 into (E) HepG2 and (F) Hep3B cells, and cell proliferation was detected by CCK8 assay. *P<0.05; **P<0.01 vs. miR‑ctrl + Wnt3a‑ctrl. CCK8, Cell Counting kit‑8; ctrl, control; miR, microRNA; OD, optical density; si, small interfering RNA.
Article Snippet: Membranes were then incubated with
Techniques: CCK-8 Assay, Over Expression, Plasmid Preparation, Control, Small Interfering RNA
Journal: Molecular medicine reports
Article Title: MicroRNA‑214 targets Wnt3a to suppress liver cancer cell proliferation.
doi: 10.3892/mmr.2017.7483
Figure Lengend Snippet: Figure 3. Overexpression of miR‑214 or Wnt3a silencing affects cell cycle progression. Cell cycle analysis of (A) HepG2 and (B) Hep3B cells following transfection with miR‑214 or miR‑ctrl for 48 h. Cell cycle analysis of (C) HepG2 and (D) Hep3B cells following transfection with siWnt3a or si‑ctrl for 48 h. *P<0.05. ctrl, control; miR, microRNA; si, small interfering RNA.
Article Snippet: Membranes were then incubated with
Techniques: Over Expression, Cell Cycle Assay, Transfection, Control, Small Interfering RNA
Journal: Technology in Cancer Research & Treatment
Article Title: B7-H3 and CD39 Co-Localization in Gastric Cancer: A Potential Prognostic Biomarker and Potential Dual-Target for Immunotherapy
doi: 10.1177/15330338251380957
Figure Lengend Snippet: Expression Patterns of B7-H3 and CD39 in Gastric Precancerous Lesions and Gastric Cancer Tissues. (A) Representative IHC Expression Patterns of B7-H3 and CD39 Across Different Pathological Stages (CSG, CAG, LGIN, HGIN, and GC). (B) Quantitative Analysis of Positive Expression Areas of CD39. (C) Quantitative Analysis of Positive Expression Areas of B7-H3. (D) Representative Multiplex IHC Expression Patterns of B7-H3 and CD39 Across Different Pathological Stages (CSG, CAG, LGIN, HGIN, and GC). (E) Quantitative Analysis of Multiplex IHC Expression of B7-H3 and CD39. (F) Representative Co-Localization Expression of B7-H3 and CD39 in GC. IHC Scale Bars: 50 µm; mIHC Scale Bars: 100 µm.
Article Snippet: The following primary antibodies were used according to the manufacturer's instructions: mouse anti-human B7-H3 monoclonal antibody, 1/200 dilution (Cat No: 66 481-1-Ig, Proteintech, China),
Techniques: Expressing, Multiplex Assay
Journal: Technology in Cancer Research & Treatment
Article Title: B7-H3 and CD39 Co-Localization in Gastric Cancer: A Potential Prognostic Biomarker and Potential Dual-Target for Immunotherapy
doi: 10.1177/15330338251380957
Figure Lengend Snippet: Co-Localization of B7-H3 and CD39 in Gastric Cancer Cells Indicates Poor Prognosis. (A, B) Representative Immunohistochemical Images Showing Low and High Expression of B7-H3 (A) and CD39 (B) in Gastric Cancer (GC) Specimens. (C) Correlation Analysis of B7-H3 and CD39 Expression. (F, G, H, I) Kaplan-Meier Survival Curves for Overall Survival of GC Patients Based on the Expression Status of B7-H3 (F), CD39 (G), Dual High Expression of B7-H3 and CD39 (H), and Co-Localized Expression Status of B7-H3-CD39 (I). Scale Bars: 100 µm.
Article Snippet: The following primary antibodies were used according to the manufacturer's instructions: mouse anti-human B7-H3 monoclonal antibody, 1/200 dilution (Cat No: 66 481-1-Ig, Proteintech, China),
Techniques: Immunohistochemical staining, Expressing
Journal: Technology in Cancer Research & Treatment
Article Title: B7-H3 and CD39 Co-Localization in Gastric Cancer: A Potential Prognostic Biomarker and Potential Dual-Target for Immunotherapy
doi: 10.1177/15330338251380957
Figure Lengend Snippet: Absence of Correlation Between Co-localization of B7-H3 and CD39 Expression and CD8 + T Cell Infiltration in Gastric Cancer. (A, B) Representative Immunohistochemical Images Showing the Expression of B7-H3 with CD8 (A) or CD39 with CD8 (B) in the Same Patient. (C) Correlation Between B7-H3 Expression and CD8 Expression, and Between CD39 Expression and CD8 Expression. (D, E) Representative Multiplex Immunohistochemistry Images of B7-H3, CD39, and CD8 (D), and Correlation Analysis Between the Co-Localization Expression Score of B7-H3 and CD39 and the Extent of CD8 Infiltration (E). (F, G) Representative Multiplex Immunohistochemistry Images of CD39 and CD8, with Arrows Indicating CD39 + CD8 + T Cells (F), and the Proportion of CD39 + CD8 + T Cells within the CD8 + T Cell Population (G). Scale Bars: 100 µm.
Article Snippet: The following primary antibodies were used according to the manufacturer's instructions: mouse anti-human B7-H3 monoclonal antibody, 1/200 dilution (Cat No: 66 481-1-Ig, Proteintech, China),
Techniques: Expressing, Immunohistochemical staining, Multiplex Assay, Immunohistochemistry
Journal: Technology in Cancer Research & Treatment
Article Title: B7-H3 and CD39 Co-Localization in Gastric Cancer: A Potential Prognostic Biomarker and Potential Dual-Target for Immunotherapy
doi: 10.1177/15330338251380957
Figure Lengend Snippet: Kaplan-Meier Survival Curves for Gastric Cancer Patients Based on Specific Expression Statuses and Immune Cell Infiltration Levels. (A, B, C, D) Kaplan-Meier Survival Curves for GC Patients Stratified by B7-H3 High CD8 Low (A) Expression Status 、 CD39 High CD8 Low (B) Expression Status 、 B7-H3-CD39 Both high CD8 Low Expression Status (C) and B7-H3-CD39 Co-localization CD8 low Expression Status (D). (E, F) Kaplan-Meier Survival Curves for GC Patients Based on CD8 + T Cell Infiltration Levels (E) and CD39 + CD8 + T Cell Infiltration Status (F).
Article Snippet: The following primary antibodies were used according to the manufacturer's instructions: mouse anti-human B7-H3 monoclonal antibody, 1/200 dilution (Cat No: 66 481-1-Ig, Proteintech, China),
Techniques: Expressing
Journal: Cell Death and Differentiation
Article Title: Connexin43 dephosphorylation at serine 282 is associated with connexin43-mediated cardiomyocyte apoptosis
doi: 10.1038/s41418-019-0277-x
Figure Lengend Snippet: Cx43 expression and distribution in NRVMs transfected with different mutants. a–d NRVMs were transfected with virus carrying Cx43-wt, S279A or S282A gene (20 m.o.i. for each) for 24 h and lysed by RIPA (a, b) or RIPA + junctional/non-junctional isolation treatment (c, d). The lysates were analyzed by Western blot (a, c), and the fold changes in phosphorylated S282 (pS282), pS262, pS368 and Cx43 abundances in relative to those of vector cells (after normalized with GAPDH or β-actin) were thereby detected (b, d). Junctional and non-junctional fractions were referred to cell-membrane and cytosolic fractions to detect Cx43 abundance distributed in both regions (see Methods), respectively, and no difference in their pattern between the two regions was found among the different treatments. *P < 0.05, **P < 0.01, ***P < 0.001, unpaired two-tailed Student’s t test, n = 4–5 independent experiments for each group as indicated
Article Snippet: Antibodies used were as follows: rabbit anti-Fas, anti-N-Cad and anti-cytochrome C (Abcam), rabbit anti-pS282-Cx43 and anti-pS279-Cx43 (Biobyt), rabbit anti-Cox IV, anti-p-p38 MAPK (Thr180/Tyr182), anti-p38 MAPKα, anti-pS368-Cx43, anti-HA, anti-pS262-Cx43 and anti-Cx43 (Santa Cruz), and rabbit anti-ZO-1 (Proteintech), mouse anti-GAPDH and
Techniques: Expressing, Transfection, Isolation, Western Blot, Plasmid Preparation, Two Tailed Test